ANALYTICAL
83, 484-520 (1977)
BIOCHEMISTRY
A Compilation
of Amino Acid Analyses of Proteins, Polypeptides, and Peptides XII. Residues DONALD
Department
of Biochemistry, Received
M.
per Molecule-9 KIRSCHENBAUM’
College of Medicine, Brooklyn, New York
Downstate 11203
Medical
Center-SUNY.
March 7, 1977; accepted July 26, 1977
I have changed the title of the series by the addition of the words “Polypeptides, and Peptides.” I felt this was necessary if the analyses of certain of the hormones of the hypophysis and the hormones (factors) of the hypothalamus are to be included. I have decided to include in these compilations the amino acid analyses of all substances for which amino acid analyses have been published. In this paper, the twelfth in the series and the ninth reporting amino acid analyses as residues per molecule, I have added an additional 272 proteins to the compilation (1). The major portion of the data I present is devoted to amino acid analyses of peptide and protein hormones and the hormones (factors) which control their release. As with previous publications in this series I have (a) rounded off the molecular weights to the nearest thousand for weights over 10,000 and to the nearest hundred for weights under 10,000; and (b) rounded off to an integral number the number of residues of amino acid reported. In Table 1, the Protein Index, I list the proteins and the sources from which they were obtained. In Table 2, I report the amino acid analyses derived from hydrolyzates or from sequences. If the sequence is the source I have indicated it in the footnote, and I have also reported the number of asparagine and glutamine residues and other amides. In addition, if a carbohydrate analysis was done, this too was reported in the footnote. For each analysis I have given a citation to the original literature, usually the first report of the data, and, for those proteins for which the sequence data supplied the analysis, I have given a citation to the column chromatographic analysis for amino acids. This permits a comparison to be made of the analytical data supplied by chromatographic methods with the absolute results of the sequence. ’ Faculty Exchange Scholar, State University of New York. 484 Copyright 0 1917 by Academic Ress, Inc. AU rights of reproduction in any form reserved.
1SSN OW3-2697
AMINO
ACID ANALYSES
OF PROTEINS.
485
XII
ACKNOWLEDGMENTS The Library of the Downstate Medical Center College of Medicine has been the major source of all publications examined. What was not available in the library was obtained for me from other libraries. I should like to thank the librarians for their most useful and continuing assistance. During the summers of 1971-1975, I was a Library Reader at the Library of the Marine Biological Laboratory, Woods Hole, Massachusetts. I should like to thank the librarians of that library for their assistance. I thank Mr. E. Becker for copy-reading assistance and for checking references.
REFERENCE
FORTEXT
1. The last published paper in this series is Kirschenbaum, 79, 470-501.
D. M. (1977) Anal. Biochem.
NOTE ADDED IN PROOF Corrections
for Part XI: Residues per Thousand Residues, 3l
Protein index numbefl
Residues reportedb
Conversion factof
10d 29 50 55 6Oc 97 125 126 143 178
983.5 967 963 905.4 972.5 986 1014 785 1162 1039
1.017 1.034 1.038 1.104 1.028 1.014 0.986 1.273 0.860 0.9625
a This is the number referring to the protein in Paper XI. * This is the value reported in the reference cited. c To convert the values given to 1000 residues one must multiply by this factor the given values. d The half-cystine content is 7.8 and not 2 as given. Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein
index index index index index index index index index index index index index index
no. no. no. no. no. no. no. no. no. no. no. no. no. no.
8: The number of residues of glycine should be 19.3 22: The number of residues of arginine should be 39 184: Proline = 82 residues. 187: Proline = 113 residues. 194: Proline = 71 residues. 245: There are an additional 70 residues of omithine 246: There are an additional 60 residues of omithine 247: There are an additional 75 residues of omithine 248: There are an additional 50 residues of omithine 249: There are an additional 78 residues of omithine 250: There are an additional 86 residues of omithine 251: There are an additional 43 residues of omithine 252: There are an additional 66 residues of omithine 253: There are an additional 52 residues of omithine
and not 193. and not 29.
present. present. present. present. present. present. present. present. present.
486 Correction
DONALD
M. KIRSCHENBAUM
for Part IX: Residues per Mole of Protein,
72
Footnote 6 should read “The amide ammonia is distributed as 20 asparagine residues and 8 glutamine residues (Goldstein, J., Konigsberg, W., and Hill, R. J. (1963) J. Biol. Chem. 238, 2016-2027).
Corrections
for Part IV: Residues per Thousand Residues, I3
Protein index no. 18: Valine = 46 residues. Protein index no. 130a: The total number of residues is 876 [including the 18 residues of hydroxyproline]. The conversion factor to bring the values to 1000 residues is 1.14. Protein index no. 149: The total number of residues is 1049.9 and a factor of 0.953 is needed to convert the values back to 1000 residues.
Corrections
for Part V: Residues per Thousand Residues, 24,5
Protein index no. 319: Tyrosine = 30 residues. There are 1022 residues reported and a factor of 0.978 is needed to convert the values reported to 1000 residues. Protein index no. 207: 983.2 residues reported and a factor of 1.016 is needed to convert the values to 1000 residues. Protein index no. 300: 1052 residues reported and a factor of 0.951 is needed to convert values to 1000 residues. Protein index no. 301: 1058 residues reported and a factor of 0.945 is needed to convert values to 1000 residues. Protein index no. 3 17: 798 residues reported and a factor of 1.25 is needed to convert values to 1000 residues. Protein index no. 328: 978 residues reported and a factor of 1.022 is needed to convert values to 1000 residues. Protein index no. 332: 1034 residues reported and a factor of 0.967 is needed to convert values to 1000 residues. Protein index no. 344: 931 residues reported and a factor of 1.074 is needed to convert values back to 1000 residues. r Kirschenbaum, Donald M. (1977) Anal. 2 Kirschenbaum, Donald M. (1975) Anal. 3 Kirschenbaum, Donald M. (1973) Anal. 4 Kirschenbaum, Donald M. (1973) Anal. 5 I should like to thank Dr. A. Reisner, information concerning these corrections.
Biochem. 79, 470-501. Biochem. 65, 466-499. Biochem. 53, 223-244. Biochem. 56, 208-236. CSIRO, N. S. W. Australia
for providing
the
AMINO
ACID ANALYSES
OF PROTEINS.
TABLE PROTEIN
1 Name 2 3 4 5
6 7 8 9
10 11 12 13 14 15 16
Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source
17 Name Source
18 Name Source
19 Name 20
21 22
Source Name Source Name Source Name Source
Hemagglutinin Lentil (Lens esculenta) Hemagglutinin, subunit H Hemagglutinin (No. 1) Hemagglutinin, subunit L Hemagglutinin (No. 1) Hirudin Leech Histone F2b Sea urchin (Parechinus angulosus) gonads Histone IIbl Rainbow trout testes Histone F3 Shark erythrocyte Histone F3 Sea urchin Histone F3 Mollusc Histone F3 Cycad Histone F3 Chicken erythrocytes Histone F3 (total) Calf thymus Histone F3 (dimer) Calf thymus Histone F3 (dimer) Duck erythrocytes Histone III Pea embryo Histone III Carp (Letiobus bubalus) testes Histone III Calf thymus Histone IV Calf thymus Histone GAR Rat tumor Histone GAR Pig thymus Histone LS Calf thymus Histone, alanine-rich arginine-rich Calf thymus
* ACTH: adrenocorticotropic
hormone.
487
XII
1 INDEX
23 24
Name Source Name Source
25
Name
26
Source Name
27 28
29 30
31 32
Source Name Source Name Source Name Source Name Source Name Source Name Source
33
Name
34
Source Name
35
Source Name
36
Source Name
37
Source Name
38
Source Name
39 40
Source Name Source Name
Histone ALK Calf thymus Histone ALG Sea urchin (Psammechinus miliaris) gonads Histone, arginine-lysinerich Calf thymus Histone AL, argininelysine-rich Calf thymus Histone Chicken erythrocytes Histone, acid-soluble from natural chromatin Calf thymus Hormone, ACTH* Porcine pituitary Hormone, ACTH Human pituitary Hormone, ACTH Ovine pituitary Hormone, ACTH Bovine pituitary Hormone, choleocystokininpancreozymin Porcine Hormone, chorionic gonadotropin, a-subunit Human placenta Hormone, chorionic gonadotropin, P-subunit Human placenta Hormone, chorionic somatomammotropin LI Human placenta Hormone, chorionic somatomammotropin 1a Monkey placenta Hormone, chorionic somatomammotropin 2” Monkey placenta Hormone, color change Crustacean Hormone, distal-retinal pigment Table
continued
DONALD
488
M. KIRSCHENBAUM
TABLE Source 41
Name Source
42 Name Source
43 Name Source 44 Name 45
Source Name
46
Source Name Source
41 Name 48
Source Name
49
Source Name Source
50
Name Source
51 Name Source
52 Name Source
53 Name Source
54 Name Source
55 Name Source
56 Name Source
Prawn (Pandalus borealis) eye stalk Hormone, follicle-stimulating Ovine pituitary Hormone, follicle-stimulating Ovine pituitary Hormone, follicle-stimulating Ovine pituitary Hormone, folhcle-stimulating Ovine pituitary Hormone, follicle-stimulating Ovine pituitary Hormone, follicle-stimulating, a-subunit Ovine pituitary Hormone, follicle-stimulating, P-subunit Ovine pituitary Hormone, follicle-stimulating Human pituitary Hormone, follicle-stimulating Human pituitary Hormone, follicle-stimulating, u-subunit Human pituitary Hormone, folhcle-stimulating, o-subunit Human pituitary Hormone, follicle-stimulating, p-subunit Human pituitary Hormone, follicle-stimulating, b-subunit Human pituitary Hormone, gastrin I and II* Porcine antra Hormone, gastrin I and II* and “Little” Human antra Hormone, gastrin “Big” Human antra
1 (Continued) 57 Name 58 59 60
61 62 63 64 65 66
Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source
67 Name Source
68 Name Source
69 Name Source
70 Name Source
71 Name Source
72 Name Source
73 Name Source
74 Name Source
75 Name Source
76 Name Source
77 Name Source
78 Name Source
79 Name Source
Hormone, gastrin I and II* Ovine antra Hormone, gastrin I and II* Bovine antra Hormone, gastrin I and IIb Canine antra Hormone, gastrin I and II* Feline antra Hormone, glucagon Porcine pancreas Hormone, glucagon Rat pancreas Hormone, glucagon Bovine pancreas Hormone, glucagon Rabbit pancreas Hormone, glucagon Human pancreas Hormone, glucagon Camel (Camelus dromedarius) pancreas Hormone, growth Equine pituitary Hormone, growth Human pituitary Hormone, growth Human pituitary Hormone, growth Bovine pituitary Hormone, growth Bovine pituitary Hormone, growth Ovine pituitary Hormone, growth Ovine pituitary Hormone, growth Ovine pituitary Hormone, hyperglycemic Cancer magister eyestalk Hormone, insulin II, alanyl chain Bonito pancreas Hormone, insulin II, glycyl chain Bonito pancreas Hormone, insulin, A chain Fin whale pancreas Hormone, insulin, B chain Fin whale pancreas
AMINO
ACID ANALYSES TABLE
80 Name Source 81 Name Source 82 Name Source 83 Name Source 84 Name Source 85 Name Source 86 Name Source 87 Name Source Name Source 89 Name Source PO Name Source 88
91 Name Source 92
Name Source
93 Name Source 94 Name Source 95 Name Source 96 Name Source 97 Name Source 98 Name Source 99 Name Source 100 Name Source 101 Name Source
Hormone, insulin, A chain Rabbit pancreas Hormone, insulin, B chain Rabbit pancreas Hormone, insulin, A chain Rat 1 pancreas Hormone, insulin, B chain Rat 1 pancreas Hormone, insuiin, A chain Rat 2 pancreas Hormone, insulin, B chain Rat 2 pancreas Hormone, insulin, A chain Mouse (Mus museums) pancreas Hormone, insulin, B chain Mouse (M. museums) pancreas Hormone, insulin Mouse (M. musculus) Hormone, insulin Mouse (M. muse&s) Hormone, insulin Mouse (Black Acomys cahirinus Hoechst) Hormone, insulin Mouse (Yellow A. cahirinus Hoechst) Hormone, insulin Mouse (Yellow A. cahirinus Geneva) Hormone, insulin, A chain Canine pancreas Hormone, insulin, I3 chain Canine pancreas Hormone, insuhn, A chain Sperm whale pancreas Hormone, insulin, B chain Sperm whale pancreas Hormone, insulin, A chain Sei whale pancreas Hormone, insulin, B chain Sei whale pancreas Hormone, insulin, A chain Elephant pancreas Hormone, insulin, B chain Elephant pancreas Hormone, insulin, A chain Caprine pancreas
OF PROTEINS.
489
XII
1 (Conrinued) 102 Source 103 Name Source 104 Name Source 105 Name Source 106 Name Source 107 Name Source Name Source 109 Name Source 110 Name Source 111 Name Source 112 Name Source 113 Name Source 114 Name Source 108
11.5 Name Source 116 Name Source 117 Name Source 118
Name Source
119 Name Source 120
Name Source
121
Name Source
Hormone, insulin, B chain Caprine pancreas Hormone, insulin, A chain Equine pancreas Hormone, insulin, B chain Equine pancreas Hormone, insulin, A chain Duck pancreas Hormone, insulin, B chain Duck pancreas Hormone, ins&n, A chain Rattlesnake (Crotalus arrox) pancreas Hormone, insulin, A chain Cattle pancreas Hormone, insulin, B chain Cattle pancreas Hormone, insulin, A chain Human pancreas Hormone, insulin, B chain Human pancreas Hormone, insulin, A chain Guinea pig pancreas Hormone, insulin, B chain Guinea pig pancreas Hormone, insulin, A chain Coypu (Hystricomorpha) pancreas Hormone, insulin, B chain Coypu (Hystricomorpha) pancreas Hormone, insulin, A chain Fish: bonito, tuna, and swordfish pancreases Hormone, insulin, B chain Fish: bonito, tuna, and swordfish pancreases Hormone, insulin, A chain Cod fish (Gadus callarias) pancreas Hormone, insulin, B chain Cod fish (G. callarias) pancreas Hormone, insulin, A chain Angler fish (Lophius piscatorius) pancreas Hormone, insulin, B chain Angler fish (L. piscaforius) pancreas
-.Table continued
490
DONALD
M. KIRSCHENBAUM
TABLE 122 Name
128
Source Name Source Name Source Name Source Name Source Name Source Name
129
Source Name
130
Source Name
131
Source Name
132
Source Name
133
Source Name
123 124 125 126 127
Source
134 Name Source
135 Name Source
136 Name Source
137 Name Source 138 Name 139 140
Source Name Source Name Source
Hormone, insulin, A chain Ovine pancreas Hormone, insulin, B chain Ovine pancreas Hormone, insulin, A chain Porcine pancreas Hormone, insulin, B chain Porcine pancreas Hormone, light-adapting Shrimp (Pandalus borealis) Hormone, /3-lipotropic Porcine pituitary Hormone, lipotropic (p-lipotropin) Porcine pituitary Hormone, lipotropic (p-lipotropin) Human pituitary Hormone, lipotropic (p-lipotropin) Ovine pituitary Hormone, lipotropic (y-lipotropin) Porcine pituitary Hormone, lipotropic (y-lipotropin) Ovine pituitary Hormone, luteinizing, P-subunit Bovine pituitary Hormone, luteinizing, a-subunit Equine pituitary Hormone, luteinizing, P-subunit Equine pituitary Hormone, luteinizing Equine pituitary Hormone, luteinizing, a-subunit Human pituitary Hormone, luteinizing, P-subunit Human pituitary Hormone, luteinizing, p-subunit Human pituitary Hormone, luteinizing Human pituitary
1 (Conrinued) 141 Name Source
142 Name Source
143 Name Source
144 Name Source
145 Name Source
146 Name Source
147 Name Source
148 Name Source
149 Name Source
150 Name Source
151 Name Source
152 Name Source
153 Name Source
154 Name 155
Source Name Source
156 Name Source
157 Name
Hormone, luteinizing, a-subunit Ovine pituitary Hormone, luteinizing, a-subunit Ovine pituitary Hormone, luteinizing, p-subunit Ovine pituitary Hormone, luteinizing, P-subunit Ovine pituitary Hormone, luteinizing Ovine pituitary Hormone, luteinizing, a-subunit Porcine pituitary Hormone, luteinizing, p-subunit Porcine pituitary Hormone, luteinizing, C-l subunit Rat pituitary Hormone, luteinizing, C-2 subunit Rat pituitary Hormone, luteinizing Rat pituitary Hormone, luteinizing hormone-releasing Porcine hypothalamus Hormone, a-melanocytestimulating Bovine pituitary Hormone, or-melanocytestimulating Porcine pituitary Hormone, cy-melanocytestimulating Equine pituitary Hormone, wmelanocytestimulating Ovine pituitary Hormone, a-melanocytestimulating Dogfish (Squalus acanrhias) pituitary Hormone, wmelanocytestimulating
AMINO
ACID ANALYSES TABLE
Source
158 Name
159
Source Name Source
160 Name Source
161 Name
162
Source Name Source
163 Name Source
164 Name Source 165
Name Source
166
Name Source
167 Name Source
168 Name Source
169 Name Source
170 Name Source
171 Name Source 172
Name Source
Monkey pituitary Hormone, P-melanocytestimulating Human pituitary Hormone, /%melanocytestimulating Bovine pituitary Hormone, P-melanocytestimulating Ovine pituitary Hormone, P-melanocytestimulating Porcine pituitary Hormone, P-melanocytestimulating Equine pituitary Hormone, @melanocytestimulating Monkey pituitary Hormone, P-melanocytestimulating Dogfish (S. acanthias) pituitary Hormone, P-melanocytestimulating Dogfish (Scyliorhinus caniculus) pituitary Hormone, aspartotocin, hormone II’ Dogfish (S. acanthias) neurohypophysis Hormone, glumitocind Ray (Raia batis) neurohypophysis Hormone, glumitocind Ray (R. clavata) neurohypophysis Hormone, glumitocin d Ray (R. naevus) neurohypophysis Hormone, glumitocind Ray (R. fullonica) neurohypophysis Hormone, isotocine Pollack (Pollachius virens) neurohypophysis Hormone, isotocine Hake (Merluccius merluccius) neurohypophysis
OF PROTEINS.
491
XII
1 (Conrinued) 173
Name Source
174 Name Source
175 Name Source 176
Name Source
177
Name Source
178
Name Source
179 Name Source
180 Name Source
181 Name Source
182 Name Source 183
Name Source
184 Name Source
185 Name Source
186 Name Source 187 Name Source
188 Name
Hormone, isotocine Whiting (G. luscus) neurohypophysis Hormone, isotocine Tuna (Germ0 alalunga) neurohypophysis Hormone, isotocine Mackerel (Scomber scombrus) neurohypophysis Hormone, isotocine Cod (G. morrhua) neurohypophysis Hormone, isotocine Carp (Cyprinus carpio) neurohypophysis Hormone, isotocin’ Bony fish (Polypterus bichir) neurohypophysis Hormone, isotocin’ Salmon (Oncorhynchus tschawytscha) neurohypophysis Hormone, mesotocin’ Viper (Vipera aspis) neurohypophysis Hormone, mesotocin’ Frog (Rana esculenta) neurohypophysis Hormone, mesotocinf Chicken (Gallus gallus) neurohypophysis Hormone, mesotocin f Goose (Anser anser) neurohypophysis Hormone, mesotocin’ Turkey (Meleagris gallopavo) neurohypophysis Hormone, mesotocin f Leopard frog (R. pipiens) neurohypophysis Hormone, mesotocinf Toad (Bufo bufo) neurohypophysis Hormone, mesotocinf African lungfish (Protopterus annectens) neurohypophysis Hormone, mesotocinf Table
continued
492
DONALD
M. KIRSCHENBAUM
TABLE Source
African lungfish (Protopterus neurohypophysis Hormone, mesotocin’ Cobra (Naja naja) neurohypophysis Hormone, mesotocinf Elaphid (Elaphe quadrivirgata) neurohypophysis Hormone, ocytocin Bovine neurohypophysis Hormone, ocytocin Porcine neurohypophysis Hormone, ocytocin Human neurohypophysis Hormone, ocytocin Equine neurohypophysis Hormone, ocytocin Finback whale (Balaenoptera physalus) neurohypophysis Hormone, ocytocin Hippopotamus (Hippopotamus amphibus) neurohypophysis Hormone, ocytocin Ovine neurohypophysis Hormone, ocytocin Ratfish (Hydrolagus collei) neurohypophysis Hormone, vasotocing Chicken (G. gallus) neurohypophysis Hormone, vasotocina Goose (A. anser) neurohypophysis Hormone, vasotocinO Turkey (M. gallopavo) neurohypophysis Hormone, vasotocinP Toad (B. bufo) neurohypophysis Hormone, vasotocing Frog (R. esculenta) neurohypophysis Hormone, vasotocin’ Viper (V. aspis) neurohypophysis
1 (Continued) 205
Name Source
206
Name Source
207
Name Source
208
Name Source
209
Name Source
210
Name Source
dolloi)
189 Name Source
190 Name Source
191 Name Source
192 Name Source
193 Name 194 195
1%
197
198
Source Name Source Name Source
Name Source
Name Source Name Source
199 Name Source 200
Name Source
201
Name Source
202
Name Source
203
Name Source
204
Name Source
211 Name Source 212
Name Source
213 Name Source
214 Name Source 215
Name Source
216
Name Source Name Source Name Source Name Source
217 218 219 220
Name Source
221 Name 222
Source Name
Hormone, vasotocin’ Cobra (N. naja) neurohypophysis Hormone, vasotocin” Elaphid (E. quadrivirgata) neurohypophysis Hormone, vasotocin9 Carp (C. carpio) neurohypophysis Hormone, vasotocina Pollack (P. virens) neurohypophysis Hormone, vasotocin9 Whiting (G. luscus) neurohypophysis Hormone, vasotocin’ Salmon (0. tschawytscha) neurohypophysis Hormone, vasotocinP Cod (G. morhua) neurohypophysis Hormone, vasotocin” Mackerel (S. scombrus) neurohypophysis Hormone, vasotocin’ Tuna (G. alalunga) neurohypophysis Hormone, vasotocin’ Bony fish (P. bichir) neurohypophysis Hormone, valitocin” Dogfish (S. acanthias) neurohypophysis Hormone, vasopressin Bovine neurohypophysis Hormone, vasopressin Human neurohypophysis Hormone, vasopressin Equine neurohypophysis Hormone, vasopressin Finback whale (B. physalus) neurohypophysis Hormone, vasopressin Hippopotamus (H. amphibus) neurohypophysis Hormone, vasopressin Ovine neurohypophysis Hormone, vasopressin
AMINO
ACID ANALYSES TABLE
Source
223 Name Source
224 Name Source
225 Name Source
226 Name 227 228 229 230 231 232
Source Name Source Name Source Name Source Name Source Name Source Name Source
233 Name Source
234 Name Source
235 Name 236 237 238 239 240 241 242
Source Name Source Name Source Name Source Name Source Name Source Name Source Name
Mouse (strains CBA/ FACAM and SF/CAM) neurohypophysis Hormone, Lys8-vasopressin Mouse (strain Peru) neurohypophysis Hormone, LyGvasopressin Porcine neurohypophysis Hormone, Lyss-vasopressin Hippopotamus (H. amphibus) neurohypophysis Hormone, parathyroid Human parathyroid Hormone, parathyroid I Bovine parathyroid Hormone, parathyroid II Bovine parathyroid Hormone, parathyroid Porcine parathyroid Hormone, proparathyroid Bovine parathyroid Hormone, polypeptide Chicken pancreas Hormone, red pigmentconcentrating Shrimp (P. borealis) nerve cells Hormone, prolactin Fish (Tilapia mossambica) rostral pars distalis Hormone, prolactin Fish (T. mossambica) caudal adenohypophysis Hormone, prolactin Bovine pituitary Hormone, prolactin Ovine pituitary Hormone, prolactin Porcine pituitary Hormone, prolactin Human pituitary Hormone, prolactin Human amniotic fluid Hormone, prolactin Rat pituitary Hormone, secretin Porcine Hormone, sexual
OF PROTEINS.
493
XII
1 (Conrinued) Source
243 Name Source
244 Name Source
245 Name Source
246 Name Source
247 Name Source
248 Name Source
249 Name Source
250 Name Source
251 Name Source
252 Name Source
253 Name Source
254 Name Source
255 Name Source
256 Name Source
257 Name Source
258 Name Source
259 Name Source
260 Name
Volvox carteri male spheroids Hormone, thyrocalcitonin Bovine Hormone, thyrocalcitonin Chicken ultimobranchial gland Hormone, thyrocalcitonin Eel pericardium and esophagus Hormone, thyrocalcitonin Human C cell tumor Hormone, thyrocalcitonin Porcine thyroid tissue Hormone, thyrocalcitonin Salmon (Oncorhynchus) ultimobranchial gland Hormone, thyrocalcitonin Rat Hormone, thyrocalcitonin Ovine Hormone, thymopoietin II Bovine thymus Hormone, thyrotropic Ovine pituitary Hormone, thyrotropic, a-subunit Human pituitary Hormone, thyrotropic, P-subunit Human pituitary Hormone, thyrotropin, component IV Human pituitary Hormone, thyrotropic, a-subunit Bovine pituitary Hormone, thyrotropic, P-subunit Bovine pituitary Hormone, luteinizingreleasing i Ovine hypothalamus Hormone, luteinizingreleasing Porcine hypothalamus Hormone, melanotropinrelease-inhibiting Table
continued
494
DONALD
M. KIRSCHENBAUM
TABLE Source
261 Name Source 262 Name Source 263 Name Source 264 Name Source 265 Name Source 266 Name Source 261 Name Source 268 Name Source 269 Name Source 270 Name Source 271 Name Source 272 Name Source 273 Name
Source
214 Name Source 275 Name Source
276 Name Source
Rat hypothalamus, stalk median eminence Hormone, melanotropinrelease-inhibiting Bovine hypothalamus Hormone, growth hormone release-inhibiting Ovine hypothalamus Hormone, thyrot~pinreleasing Ovine hypothalamus Hormone, thyrotropinreleasing Porcine hypothalamus Hydrogenase Ciosiridium pasteurianum W5 Hydrogenase 4.2 form Chromatium sp. Hydrogenase 4.4 form Chromatium sp. L-a-Hydroxyacid oxidase, isozyme A Rat liver L-a-Hydroxyacid oxidase, isozyme B Rat liver D-@-Hydroxybutyrate apodehydrogen~e Bovine heart mitochondria p-Hydroxyphenylpyruvate hydroxylase Chicken liver 3&Hydroxysteroid oxidase Brevibacterium sterolicum ~mid~olylacetolphosphate: L-glutamate aminotransferase Salmonella typhimurium Initiation factor-Ml Rabbit reticulocytes Inosine monophosphate dehydrogenase Aerobacter aerogenes Inosine monophosphate dehydrogenase Bacillus subtilis
1 (Continued) 277 Name Source 278 Name Source 279 Name Source 280 Name Source 281 Name Source 282 Name Source 283 Name Source 284 Name Source 285 Name Source 286 Name Source 287 Name Source 288 Name Source 209 Name Source 290 Name Source 291 Name Source 292 Name Source 293 Name Source 294 Name Source 295 Name Source 296 Name Source
Inosine monophosphate dehydrogenase Escherich~a coli Indole-3-glycerolphosphate synthetase E. coli Invertase, external Yeast (Saccharomyces strain FH4C) Invertase, internal Yeast Isocitrate dehydrogenase Yeast Isocitrate dehydrogenase Rhodopseudomonas spheroides Isocitrate dehydrogenase B. stearothermophilus Isocitrate dehydrogenase E. coli Isocitrate dehydrogenase Bovine heart Isocitrate dehydrogenase A. aerogenes Isocitrate dehydrogenase Azotobacter vinelandii Isocitrate dehydrogenase Porcine heart Is&rate lyase Pseudomonas ~ndigofera Isoleucyl-tRNA synthetase (EC 6.1.1.5) E. coli MRE 600 Isoleucyl-tRNA synthetase (EC 6.1.1.5.) E. coli Isoleu~yI-tRNA synthetase (EC 6.1.1.5) E. coli Isomaltase Rabbit small intestine Isomerase S. ~ph~murium Isomeroreductase S. ~phjmurium C-55 Isoprenoid alcohol phosphokinase Staphylococcus aureus
AMINO
ACID ANALYSES TABLE
297 Nume Source
298 Name 299
Source Name
@-Isopropylmalate drogenase
dehy-
OF PROTEINS.
1 (Continued) Source
300 Name
S. typhimurj~m
cu-Isopropylmalate synthase S. typhimurium strain CV123 a-Isopropylmalate synthase
495
XII
Source
301 Name Source
S. ty~him~rium
~-Isopropylm~ate tase
strain CV241 synthe-
Neurospora
ru-Isopropylmalate
synthase
S. typhimurium
o This is also known as placental lactogen. b Form I is not sulfated on the tyrosine phenolic group, while Form II is sulfated; the sequence is the same. o Asn4-ocytocin. d Ser’, Gin*-ocytocin. e Seti, Ilea-ocytocin. f IleE-ocytocin. 9 Args-ocytocin. h VaP-ocytocin. i I have used the name “hormone” for these substances for two reasons. (i) I want to include them in this table with the analyses of the hormones they influence; and (ii) they have been called hypothalamic factors (hormones) by the IUPAC-IUB Commission on Biochemical Nomenclature Recommendations (1974). [(1975) Biochemistry 14,2559-2560.1
10 10 12 6 7 4 10 18 15 10 -1
9 3 2 10 5 4
18 1
30 30 34 19 I8 15 38 53 48 29 0 --
23 9 9 25 11 17 --
52 1
Glycine Alanine Vnline Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x 1O-3 Reference
2
1”
Aminoacid
-
8 1
2 2 1 2 1 2
4 5 4 2 1 2 7 6 5 6 tr* -
3
2
9 0 4 4 2 3 4 4 9 13 6-01 0 3 0 1 1014 2 0 -114 -
4
6
3
4
223 ooo---o---------
tr 0 10 13 11 12 122
_ 5
2 123 18
15
6 10
6
__
12 7 6 6 10 5 15 11 2 123 18 2 4 3
12
8 7 18
7
ANALYSES
7 18
ACID
5 14 3 18 4106666 1 16 247 5.56 6 3 3 6 185 4 11
5
A~UNO
6
2 123 18 2 4 3
12 7 6 6 10 5 15
7 18
9
_ 6
12 7 6 5 10 5 15 1 1 123 18 2 5 3
7 19
10
Residues
7a
-.-If
7 18 6 12 7 6 6 10 5 15 f 2 135 18 2 4 3
11
per
OF PROTEINS,
TABLE
13
17 8
-
17 8
-
17 8
__
2 145 20 2 4 3
14 8 7 8 10 6 15
7 19
14
weight
10 9 20 20 77766 13 13 7 7 7 8 6 7 9 9 6 6 16 I7 2 11 2 2 156 146 19 18 3 2 4 4 3 3
12
molecular
POLYPEPTIDES,
2
9
12 7 5 7 10 5 1.5 11 1 127 17 2 5 2 00 108
7 19
15 7 18
16
910 10
2 119 18 2 4 3
12 7 6 6 10 5 15
of protein
AND PEV~IDES
10” 11
7 18 6 12 7 6 5 10 5 15 2 2 11” 18 2 4 3 0
17 17 7 9 8 6 11 2 7 5 6 0 1 10’2 14 2 2 4 0 4’2 12
18
2 7 5 6 0 I 10’2 14 2 2 4 0 4’2 13
17 7 9 8 6
19
412 14 14
912 14 2 2 4 0
11 7 9 8 6 16 2 7 6 6 0 1
20
14 15
6’3
20 8 3 2 5 o-
14 8 6 10 0 2
7 13 9 6 6
21
14 16
-
12’4 18 2 2 2
5 8 12 0 0
11 6 16 -14 2
14 12 4 1 3 0 11’5 17
fj 5 4
14 17 8 16
23 7 19 6 12 -14 -14 -14
22
8 12
0
9 10
0
Aspartic
Glutamic acid Half-cystine
-
Reference
x 1O-3
MW
18
3
3
Phenylalanine Tyrosine
-
2
Histidine
Tryptophan Amide ammonia
11
24
Arginine
19
0 11” -
12
11
Lysine
14
00
13
Methionine
5
3
Threonine
4
7
6 5
16
8
Serine
acid
6
Isoleucine
-16
16
Leucine
Proline
8
Valine
17
14
16
18
25
24”
Glycine
acid
Alanine
Amino
20
-
-18
0
3
4
12
15
0
0
9 12
5
4
5
6
16
8
17
14
26
8
14
22
-
16
21
-
-
o-
1233 2 3
2311
16
34
8 0
5
6
6
5
4
8
6
13
9
28
1111
5 0
2
5
21
9
5
6
6
23
7
27
23
-
11 1
2
3
4
5 0
2
0
2
4
0
2
3
3
3
29
23
-19
1
2
3
4
5 0
2
0
3
4
0
1
3
3
3
30
25
-20
1 1
3 2
1
3
4
1
5 0
2
0
3
4
0
1
3
3
3
31
26
-
11 2
3 2
11
3
4
13
5 0
2
0
3
4
0
12
3
3
3
27
3.8
321
1 1
3
2
1 0
5
0
5
2
2
1
1
2
33
28
0 823 -22
4
3 4
3
6
3
10
6 9
8
8
7
1
4
7
5
4
34
28
-22
0 924
3
1 2
12
4
1
12
11 9
10
13
22
5
12
12
8
8
35
per molecular
Residues 32
2 (Continued)
TABLE
30
22
1 1925
8
7 11
11
9
6
4
22 25
12
18
5
7
25
7
6
7
36
21
9
8
11
37
32
22
2
6
4 9
8
10
5
4
19 27
10
15
9
-26
weight
32
22
-
2
4
8 10
8
10
5
4
19 25
9
16
8
7
23
9
9
9
38
of protein
33
227
1
0
0 1
0
0
0
0
1 1
0
1
1
0
1
0
0
1
39
11
13 15
1
34
1.9
028
0
0
0 0
1
0
2
0
35
30
4 -29
6
4 6
5
2 12
36
25
1 -28
5
4 5
5
2 9
9
12
11
11
1 2
3
8
2
1 11
6
9 7
7
42
5 11
11
11 8
8
41
6 10
3
1
1
1
2
40
37
32
2 -30
4
5 7
7
3 14
7
28
21
14
15
7 13
16
17 12
13
43
39 continued
Table
33
4 -32
10
6 7
8
4 15
16
17
16
19
12
8 11
9
13 11
9
45
38
23
4 -31
8
5 5
7
3 15
17
15
14
17
11
7 10
7
12 11
8
44
16 39
2 -33
5
4
3
3
9
4
8 8
6
8
5
7
2
2
5
7
4
46
7
2
7
3
40
8
3
25
7 5
5 3
39
11
15
5
19
8
2
0
-
15 23 21
-34
20
8
20 15 11
11 10 9 10
41
33
-35
10
9 6
13
13
19
11
7
7
16
4
10
5
5
6
16 15
11 15
I
11
12
13
15
49
5
Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x IO+ Reference
48
6
47”
Amino acid
-
43
-36
4
4
3 3
6
3
5 9 10
8
8
6
11
7 4
4
4
50
44
10
8=
0
4
4
3 3
6
3
6 9 10
8
8
7
7 4
5
4
51
3
3
738 13
46
1
1 -36 45
8
7
3
5
5 3
7
10 12 1
11 12 1 8
9
13
7
6
5
7
6
7
6
53
9
14
7
5
6
5
6
6
6
52
2 (Continued)
47
-
1
2
1 I
0
0
0
48
1 -39
2 -
49
----_I 50
1
2
0 1 1
1 1 1 2
0
0
0
0
2
112
1 0 0 0 1 1
2
0
0
8
6
5
1 0 0 1
2
0
0
0
1
2
2
57
5 1 0
3
1
2
4
0
1 0 1 0 1 0 0 1
56
6
2
1 0 0 0 1 0 0 1
5.5
2
54
50
1
2
0 1 1
0
0
0
5
1 0 0 1
0
0
1
2
2
58
51
1
2
0 1 1
0
0
2
0
5
1 0 0 1
0
0
0
2
2
59
52
1
2
0 1 1
0
0
1
0
5
1 0 0 1
0
1
0
2
2
60
53
4 -40
I
2
2
1
2
1
1
0
3
4
3
4
0
0
2
1 1 1
61
Residues per molecular weight of protein
TABLE
1
2
54
55
1 1-l ----_ ----___
2 2 222227
1
2
1 1
1 1
3
4
3
4
000004
3
4
3
4
000007
1 1 1 1
63
2 000006
1 1 1
62
56
2
1
2
1 1
3
4
3
4
1 1 1 1
64
57
2
1
2
1 1
3
4
3
4
1 1 1 1
65
58
11
2
1
2
1 1
3
4
3
4
1 1 1 1
66
59
-41
12
3
14
4 10
25
16
8
15
8 17 7 26
67
61
22 -42
1
8
13
3
63
23 -43
1
8
13
3
9
11
11
3
4
27
20
10
18
8
8
26
7
7
8
69
9
3
4
26
20
10
18
8
8
26
7
7
8
68
16
acid
Glutamic
6
1
Phenylalanine
Tyrosine
Tryptophan
x lO-3
Reference
MW
64
-4r -
13
Histidine
ammonia
13 3
13 3
Amide
11
12
Lysine Arginine
66
17 -45
1
6
13
4
4
4
4
Methionine
24
16
12
26
7
Half-cystine
25
acid
Aspartic
13
7 6
Isoleucine Proline
12
24
Leucine
12
6
Valine
Serine
7 6
14
Threonine
10
10
Glycine
Alanine
15
71
acid
70”
Amino
68
16 -46
1
666
13
13 3
11
4
4
24
16
12
13
776 668
27
7
15
9
72
69
-
1
13
13 3
11
4
4
24
16
12
12
26
7
15
9
73
72
-
21
4212
-48 -
70
1220
2
-48
2
-48
-48
7
8
-46
-as
2012 221
5
4
-48
-48
75
1
-47
12
12 3
11
4
4
23
16
12
12
24
7
15
11
74
73
-
-
0
2
1
1
0
2
3
1
0
1
4
20
3
3
76
74
-
-
0
1
0
1
0
4
4
3
0
0
2
0
1
77
0 4
0
0
0
0
4
4
2
1
2
0
2
1
75
-49
1 0
75
2 -50
0
2
3
1 2
1
0
2
3
1
1
1
0 1
4
3
2
3
79
76
-49
4
0
2
0
0 0
0
0
4
4
2
1
2
2 0
2
1
0
1
80
76
-50
2
0
2
3
1 2
1
0
2
3
1
1
1 2
0
4
3
1
3
81
per molecular
Residues 78
2 (Continued)
TABLE
76
-49
4
0
2
0
0 0
0
0
4
3
3
1
2
2 0
2
1
0
1
82
weight
76
-51
1
0
2
3
1 2
2
0
2
3
0
3 1
1
0
4
3
1
3
83
76
4 -50
0
2
0
0 0
0
0
4
3
3
1
2
2 0
2
1
0
1
84
of protein 86
1
128
77
-51 76
00000000 l-------
222--443
20222222 30323333
10111111
10221111
10101-o-
24234655
33367767
0303
1
10221111 228 3
02
42466666
3
1012
31344444
85
77
-
128
2=
0
3
87
77
-
328 228
2
4
88
77
_
3444
328 228
2
4
1111
89
Table
77
_
328 228
2
4
90
continued
77
_
328 228
2
4
91
77
-52
328 228
2
4
92
acid
Glutamic
0
0 0
2
0 4 -49
Arginine
Histidine
Phenylalanine
Tyrosine
Tryptophan
x 1O-3
Reference
MW
76
0
Lysine
ammonia
0
Methionine
Amide
4
Half-cystine
4
1
2
1
Serine
acid
0
Proline
Aspartic
2
Isoleucine
Threonine
1
2
Leucine
1
Valine
1
93a
Alanine
acid
Glycine
Amino
76
0 2 -50
2
2 3
1
1
0
2
3
1
1
1
1
0
4
3
2
3
94
80
0 4 -48
2
0 0
0
0
0
4
4
2
1
2
0
2
2
1
0
1
95
80
-49
-50
80
0 4
2
0 0
0
0
0
4
4
2
1
2
0
1
2
1
1
1
97
0 2
2
2 3
1
1
0
2
3
1
1
1
1
0
4
3
2
3
96
80
0 2 -50
2
2 3
1
1
0
2
3
1
1
1
1
0
4
3
2
3
98
76
0 4 -49
2
0 0 2
76
76
0 4 -49
2 0 2 -50
0 0
0
0
4 0
4
2
0
1
0
1
2
2
1
2
101
2 3
1
1
0 0
2 0
3
1
2
1
1
0
4
3
1
3
100
4 0
4
2
1
1
0
1
2
2
0
2
99
76
0 2 -50
2
2 3
1
1
2 0
3
1
1
1
1
0
4
3
2
3
102
per
Residues
81
0 4 -49
2
0 0
0
0
4 0
2 4
1
1
0
2
2
1
0
2
103
81
0 2 -50
2
2 3
1
1
2 0
3
1
1
1
1
0
4
3
2
3
104
molecular
2 (Continued)
TABLE
82
-53
0 5
2
0 0
0
0
4 0
5
3
0
1
1
1
2
1
0
1
105
weight
82
-50
0 2 -54
83
0 5
2
0
2 2
0 0
0
4 0
5
3
0
1
1
1
2
1
0
1
107
1 2
1
2 0
3
1
1
2
1
4
0
2
3
3
106
of protein
84
0 4 -49
2
0 0
0
0
4 0
4
2
0
2
0
1
2
2
1
1
108
84
0 2 -50
2
2 3
1
1
2 0
3
1
1
1
1
0
4
3
2
3
109
85
0 4 -49
2
0 0
0
0
0
4
4
2
1
2
0
2
2
1
0
1
110
85
0 2 -50
2
3
2
1
1
0
2
3
1
2
1
1
0
4
3
1
3
111
76
0 4 -55
1
0
1
1
0
0
4
3
2
3
1
0
1
1
1
0
2
112
76
0 2 -50
2
3
1
1
1
0
2
2
4
1
3
1
1
3
3
0
2
113
86
6 -13
0
1
0
0
1
0
1
4
2
1 5
2
0
2
1 1
1 0
114
86
3 -56
0
3
2
1
4
0
0
2
2
1 3
3
1
0
3 3
2 0
115
0
1
2
1 0
0
4
acid
acid
Leucine
Isoleucine
Proline
Serine Threonine
Aspartic
Glutamic
x lo-$
Reference
MW
87
0
2
2
87
-
-
0
Tryptophan
ammonia
1
Tyrosine
Amide
1
Phenylalanine
-
1
Histidine
-
1
0
Lysine Arginine
2
0 1
0 1
2
4
Methionine
1
3
0
4
3
Half-cystine
3
3 1
1
Valine
2
3
1
117
0
116”
Alanine
acid
Glycine
Amino
4
88
-49
0
1
1
1
1
0 0
4
2
5
0
1 0
2
1
1
0
1
118
88
2 -50
0
2
2
2
1
1 1
2
1
3
0
3 1
0
4
2
2
3
119
4
89
-49
0
1
1
1
1
0 0
4
3
4
0
1 0
2
1
1
0
1
120
89
2 -50
0
2
2
2
1
0 0
2
1
3
0
1 1
0
4
3
3
3
121
4 90
-49
0
2
0
0
0
0 0
4
4
2
0
0 1
1
2
2
1
2
122
-50
1 1
0 2 2
1
-49
90
90
0 4
2
0
0
90
0 2
2
3
2
1
1
0 0
2 0
3
4 0
4
1
0
2
1
3 4
2
3
125
1 2
0
1
124
91
-57
0 3
0
0
0
1
0
0 2
1
2
1
2
1
1 3
1
1
2
126
92
-58
1 5
3
3
2
4
10
0 2
14
5
3
3
9
5 1
3
15
8
127
per molecular
Residues
0 2 -50
2
3
2
1
0 1
2
3
1
1
1 1
0
4
3
2
3
123
2 (Continued)
TABLE
93
-
1 4
3
3
2
4
10
0 2
14
5
3
3
9
5 1
3
15
8
128
weight
94
-59
1 8
3
3
2
5
9
0 2
11
10
4
4
6
8 2
2
8
11
129
96
-60
1 6
3
3
2
5
10
0 2
16
4
4
5
5
6 2
2
13
8
130
of protein
97
-61
1 1
2
1
1
3
4
0 1
11
3
0
1
8
3 0
1
13
5
131
98
-62
1 2
2
1
1
4
4
0 1
13
2
1
3
4
4 0
1
11
5
132
101
-69
0 3
2
3
3
8
2
12 3
6
5
7
8
20
12 5
8
8
7
133
4
104
-64
-
4
2
4
5
7 1
7
5
7
5
6
4
4 4
5
4
134
continued
Table
-66
108a
1
2
3 2
10
3
1
12
7 7
7
7
16
5
8
11
5
8
138
106
-65
0
4
3 4
3
6
3
10
5 9
8
8
6
1
4
7
4
4
137
104
-64
3
104
-64
-
1
9 3 7
1 3
5
9
2
1 2
13
8
13 9 12
----
-
17 15 4 6
6
7
13
8
9 10
5 6 4
10 13
4 9
136
135
7
8
Serine
Threonine
3
10
Lysine
Arginine
27
109
-
-67
108b
MW
Reference
x lo+
1
Tryptophan Amide ammonia
-68
2-
Tyrosine
10
6
5
1
2
Phenylalanine
8
6
9 5
12
11
13
11
18
6
6
Histidine
Methionine
12 2
Half-cystine
8
7
16
Proline
acid
4
Isoleucine
acid
8
Leucine
Aspartic
11
Valine
Glutamic
7
9
8
5
140
139”
8
acid
Glycine Alanine
Amino
112
-69
-66
5
5
3
3
10
10 4
8
6
9
6
7
2
2
5
7
4
141
-
111
-66
0
5
5
3
3
10
10 4
7
6
9
6
7
2
2
5
7
5
142
115
-70
2
0
2
3
3
8
2
12 3
6
5
7
8
21
5
12
8
8
7
143
111
-71
-66
o-
2
3
3
8
2
12 3
6
5
7
8
20
5
12
8
8
7
144
116
28
-72
7
7
5
9
11
14 5
12
11
13
11
22
6
12
12
12
10
145
119
-13
6
0
5
3
3
3
10
10 4
7
4
9
6
5
2
3
4
8
4
146 8
119
-74
3
4
3
10
9 3
7
7
8
7
7
4
4
4
8
5
4
1
9
1
10 2
6
6
8
9
20
3
11
10
9
7
149
120
16 120
16
2 5 3 o3 -75 -715
3
1
10
0
12 1
3
4
6
10
21
4
13
7
11
148
7
120
31
-15
7
5
12
11
18 4
13
13
15
14
27
7
16
14
15
12
150
1
121
1 -76
1 1” 123
-
1
0
0
0
2
0
0
124
1”
1
1111111111
1
111111
10
0
0
0
0
10
11111111111
0
1
1111111
0
0
0
1111111
0
0
12
153
1”
1
1
0
0
0
0
2
0
0
0
0
154
126
-
of protein
111111 0 0
152
weight
11111
0
10
0
2 0
151
per molecular
Residues 147
2 (Continued)
TABLE
127
1”
1
1
0
0
0
0
2
0
0
0
0
155
128
-
-78
1
1
2
0
0
0
2
2
0
0
0
0
156
-” 129
1 1
1
0
0
0
0
2
13
0
0
0
0
157
2.7 131
066
1
1
2
3
1111
0
3
2
0
12
0
0
0
2 10
158
2.1 132
066
1
1
111
2
0
11
2
0
3
0
0
0
2
159
127
2.1
066
1
1
2
0
2
0
2
3
0
0
0
2 0
160
2.1 133
066
1
1
2
0
2
2
0
1
3
0
0
0
2 0
161
0
0
0
0
0
2
1
0
2
acid
acid
Alanine Valine
Leucine
Isoleucine
Proline
Serine
Threonine
Aspartic
Glutamic
1
1
1
1
066
Histidine
Phenylalanine
Tyrosine
Tryptophan
Amide
Reference
x lo+
134
2.1
2
Arginine
MW
2
Lysine
ammonia
0 1
Half-cystine Methionine
2
2
0
2
Glycine
129
2.1
0%
1
1
1
1
3
1
0 1
2
2
0
1
2
0
0
163
acid
162”
Amino
128
1.9
066
1
1
2
1
1
1
0 0
0
3
0
1
1
0
1
1
0
2
164
128
2.1
066
1
1
1
1
1
2
0 2
0
3
0
0
1
1
0
1 0
3
165
135
1’9
2
0
1
0
0
0
0
2 0
0
2
0
0
1
1
1
0 0
1
166
136, 137
1.0
380
0
1
0
0
0
0
2 0
1
1
0
1
1
1
0
0 0
1
167-170 1
1
138- 142
1.0
28’
0
1
0
0 0
143-
1.0
382
0
1
0
0 0
0
0
0 0
2
1
1
0
0
1
0 2
0
0
2
0
1
0
1
1
0 2
0
0
149
180-190
per molecular
Residues 171-179
2 (Continued)
TABLE
150-
1.0
382
0
1
0
0 0
0
0
2
1
1
0
0
1
1 1
0
0
1
157
191-198
weight
1.0 -ma
382
0
1
0
1 0
0
0
2
1
1
0
0
1
0 1
0
0
1
199-214
of protein
135
1.0
3”
0
1
0
0 0
0
2 0
1
1
0
0
1
1
1 0
0
1
215
1.0 -84b
3”
0
1
1
1 0
0
2 0
1
1
0
0
1
0
0
0 0
1
216-222
1.0 -Sk
0 382
1
1
0 0
1
2 0
1
1
0
0
1
0
0
0 0
1
223-225
Table
164
-
-
0
2
5
5
9
2
0
10
10
1
6
2
10 1
8
7
5
226
166
-
8”
1
1
2
5 4
9
2
0
11
9
1
8
2
8 3
7
7
4
228
continued
165
-
8=
1 1
2
4
5
9
2
0
11
9
0
8
2
8 3
8
7
4
227
229”
8 0
8
acid
acid
Isoleucine
Serine Threonine
Aspartic
Glutamic
41
5
22
19
9
23
11
17
20
4
1
0
1
10
0
Reference
x 1O-3
-
170
-
168
8
171
4
172
0.9
173
-
286 -87
MW
l--
110
P
Tryptophan Amide ammonia
3
0
0
Tyrosine
14
15
7
12
0
0
6
0
121
6=
0 3
12
13
0 1
1 0
12
10
1
173
-88
-87
3
5
7
11
10
6
15
17
9
15
7
24
0
12
12
234
13
11
233
0
1
232
Histidine Phenylalanine
Arginine
12 6
9 5
Lysine
0
2
1
4 0
6
1 2
1
3
3
1
231
11 0
9
9 0
3 24
8
9
42 7
230
Methionine
Half-cystine
1 0
3 2
Leucine
Proline
9
10
Valine
5 6
acid
Alanine
Glycine
Amino
2
174
-
-
8
6
7
11
9
7
6
22
22
9
15
11
11
23=
9
10
11
235
177
23
1899
2
7
6
8
11
9
7
6
22
22
9
15
11
11
23”
10
9
11
236
2--20
178
23
2091
7
6
9
13
9
4
6
24
22
5
16
7
15
26
11
9
8
237
913
29
20
15 9
10
181
-
65604
66714
11 10 77512
101011
181
-
11
10
240
182
-
8
603
28
22
12 6
12
910 24 22
13
11
239
44202
28 6-
19
15 9
9
10
25
12 9
9
238
per
Residues
molecular
2 (Continued)
TABLE
183
-
184
185
-
-95
-95
0
1
2
2
3
495
395
2
0
2 5
2
3
244
186
-
1 0 494 -
2
2
1 11
1
2 10
1
4
4 2
2
0
1 3
1
3
243
of protein
193 28
-93
9
7
13
242
392 -
4
06
311
213
416 212
0
0
19 610
113
2
241
weight
187
-
496
0
0 1
1 1
2
2 0
3
2
4
3
2
0
2 5
1
3
245
189
_
59’
0
1
1 3
0
1
1
2
2
3
5
1
2
1
1 2
2
4
246
190
-
1 5=
1
1 3
2
0
1
2
1
4
4 2
2
0
3
1
1
3
247
192
59’
1 0
0
1
1
2
0
2
3
2
5
4
2
0
5
1
0
3
248
193
597
1 0
2
1
0
1
1
2
2
3
5
2
2
1
3
1
1
4
249
194
494
3 1
I
1
1
1
1
2
1
4
2
4
2
0
3
1
1
3
250
5.6 195
699
0
2
1
0
2
5
0
0
8
4
4
3
2
0
8
6
3
1
251
8
9
7
17
11
16
14 15
Leucine
Isoleucine
Proline
Serine
Threonine
Aspartic Glutamic
3
3
7
5
Arginine Histidine
ammonia
MW x lO-3 Reference
Amide
Tryptophan
Phenylalanine Tyrosine
28 1%
4
10 -
-197
0
4
7
5
13
Lysine
Methionine
9 2
15 5
9
6
8
1
4
7
Half-cystine
acid acid
6
11
Valine
5
5
14
253
11
252”
Alanine
Acid
Glycine
Amino
198
11 o-
4
3
5
7
12 2
9 7
11
5
7
9
6
4
6
4
254
199
200
5 0
5
3
3
10
10 4
6 8
9
6
7
2
2
5
7
4
256
30 _
18
11
8
10
16
21 5
22 23
24
18
17
13
14
15
17
16
255
200
_
11 0
4
3
4
9
12 5
9 7
11
5
7
6
4
6
6
4
257
204
-103
1
1
1
0
1
1
0
0
1 0
0
0
1
1
1 0
0
0
2
258
205
-103
1
10
10
0
10
10
0
0
10 0
0
0
10
1
1 0
0
0
2
259 1
206
*103 -104
0
0
0
0
0
0
1
1 0
0
0
207
0 0 ,103 -104
0
0
0
0 0
0
0 0
0
0
1
1 0
0
0
1
261
207
1 1105
0
3
0
0
0 2
2
0
1
2
1
0
0 0
0
1
1
262
209
-
0 1103
0
0
1
0
0 0
0
1
0
0
0
1
0 0
0
0
0
263
per molecular
Residues 260
2 (Continued)
TABLE
210
-
13
6
58 12
11
12
76
81
24
26
26
38 39
22
37
32
265
59’06 212
24
23
57
14 26
14
101
86
43
48
39
76 48
61
85 120
266
98 213
19 13 -107
of protein
0 11 0 1103 -
0
1
0
0 0
0
1
0
0
0
1
0 0
0
0
0
264
weight
---
5
11
14
7
15
7 25
4
44
33
19
26
0 16
30
23
31
30
268
5
9
14
7
20
6 24
5
38
34
18
24
16
36 0
23
34
25
269
4
9
11
6
15
10 16
6
29
26
18r09
23’09
12
22 11’09
191°9
24
23
270
98’OS 40 40 32 213 214 214 213
-
19 13
24
22
57
15 27
12
101
87
44
45
38
76 50
63
83 132
267
33 217
-
65
9
219
-
16
12 19
20
61
8
9
61
54
37
43
22 40
46
44
43
39
274
continued
218
59
74
6
17
7 0
4 15
33
15
4
13
12 8
6
12
4
13
74
54
15 20
25 34
12 23
24 30
60
44
52
31
273
7 57
17
22
0
23
272
Table
49 216
5 59
17
24
14
19
31
8
57 -109a
22 44
25
19
18
36
27 31
33
271
35
33
30
22
13
19
21
27
acid
acid
Valine
Leucine
Isoleucine
Proline
Serine
Threonine
Aspartic
Glutamic
x 10-s
Reference
MW
Amide
165
221
220
7
93
38
-
25
6
Tyrosine
ammonia
32
8
Histidine Phenylalanine
-
2.5
7
Arginine
Tryptophan
63
19
25
Lysine
47
8
Methionine
14
3
139
105
96
74
62
86
81
111
116
143
216
Half-cystine
41
38
275a
Alanine
acid
Glycine
Amino
-
222
54
8
8
12
8
24
20
8
4
48
32
-110
17 -110
20
33
32
44
40
277
45 223
-
2
14
14
10
21
16
5
6
52
44
13
23
15
22
45
34
55
29
278
224
270
1501”
33
65
80
16
27
60
21
5
115
178
84
114
65
40
83
69
68
71
279
Residues
TABLE
25
135
30
31
77
29
32
85
14
0
124
165
80
151
63
38
77
73
84
115
280
per
40 226
-
3
9
12
9
16
24
5
2
38 31
30
27
18
29
32
27
30
32
281
molecular
2 (Continued)
50 227
-
5
14
17
8
18
26
11
5
38
42
26
18 23
25
35
28
43
42
282
weight
228
93
10 -112
2.5
32
10
37
66
18
101 -
76
4728
2528
41
69
51
63
88
76
283
of protein
80 229
-
-
24
14 23
28
57
8 10
75 84
36
31 34
51
58 66
75
62
284
230
-
-
2
12 9
12
17
26
13
6
43 39
22
19
17
23 26
31
36
32
285
78 231
-
-
-
13
16
23
63
9
3
90
69
39
87
28
30
48
35
80
81
286
80 232
-
7
19
17
13
24
52
8
3
70 61
39
33 42
39
60
42
76
45
287
40
9
233
-
-
12
10
15
26
11
7
37
41
19
19
17
24
32
30
34
32
288
21
158
Tryptophan
Amide
x lo+
-
19
32
102
84
Tyrosine
31
26
235
71
Phenylalanine
234
47
Histidine
61 45
23
14
91
88
46
44
48 47
222
114 94
Lysine Arginine
MW
43
Methionine
ammonia
21
Half-cystine
240
acid
Glutamic
Serine
197
90
Isoleucine Proline
120
83 80
Leucine
acid
59
156 140
Aspartic
93
Threonine
72
176
266
Glycine
Alanine Valine
83
290
acid
289”
Amino
237
114
236
112
33 -
-
30
24
67 44
21
7
83
101
55
55
43 44
83
81
107
82
292
-
25
33
32
25
65 49
25
15
99
99
48
46
49 47
77 80
82 100
291
41
21 46
25 43
12
96
238
100
-
-
114
68
42
48 50
65
50
42
50
293
Residues
TABLE
13
3
7
6
-
239
240
57
6
17
17
8
22
5
33
15
17
56 5
50
22
12
3
33 4
26
29
-
19 24
11 12
28
49
33
57
49
295
15
27
29
27
28
294
per molecular
2 (Continued) weight
17 241
-
4
4
10
3
5
8
4
8 0
8
8
8
4
23
23
11
14
9
296
of protein
70 242
-
17 7
13 22
37
28
15
9
67
22 68
37
42 33
58
33
74
58
297
48
11
243
-
13 13
25
28
9
5
50
23 49
24
25 14
28
31
39
30
298
48
9
243
-
12 13
21
26
11
5
51
21 48
22
22 16
30
28
37
31
299
-
14 66
Table
244
143
-
18
35
22 47
79 71
16
21
140
143
continued
245
48
11
11
13 13
28 2.5
9
5
50
49
23
24
75 82
28 25
31
39
30
301
100 62
94
107
97
300
to Table
2
o!See Table 1 for identification of protein, polypeptide, or peptide. 1 - Not done. 2 tr, Trace. 3 From sequence; plus 1 residue e-N-methyllysine. * Amino acid analyses and a previously suggested sequence may be found in Refs. (7b,c). 5 Includes 1 residue of methyllysine with dimethyllysine predominating; some trimethyllysine detected. 8 Includes 1 residue of methyllysine. ’ Plus 2 residues of methyllysine, with the monomethyl derivative predominating and a small amount of dimethyl derivative. * From sequence; the amide ammonia is distributed as 1 asparagine and 9 glutamine residues. 9 Plus 2 residues of methyllysine. lo From sequence; the amide ammonia is distributed as 1 asparagine and 8 glutamine residues. ” Plus 2 residues of methyllysine. From the sequence; the amide ammonia is distributed as 2 asparagine and 8 glutamine residues. i* Plus 1 residue of methyllysine. From the sequence; the amide ammonia is distributed as 2 asparagine and 2 glutamine residues. There are also 2 acetyl groups present; one is on the N-terminal amino acid. See also Ref. (12b). I3 From sequence; the amide ammonia is distributed as 3 asparagine and 3 glutamine residues. I4 There are 6 or 7 residues of isoleucine, 6 or 7 residues of proline, 4 or 5 residues of serine, 1 or 2 residues of half-cystine and 1 or 2 residues of methyllysine. i5 From sequence; the amide ammonia is distributed as 6 asparagine and 5 glutamine residues. The N-terminus is acetylated.
Footnotes
I6 5 or 6 residues of proline. i7 From sequence; the amide ammonia is distributed as 6 asparegine and 7 glutamine residues. There is an N-terminal acetyl group. is From sequence; there is an N-terminal acetyl group. The same composition is obtained from analysis of 24- and 72-hr hydrolysates. I9 See Ref. (24). 2oSee Ref. (26). *I From sequence: the amide ammonia is distributed as 1 asparagine residue, 1 glutamine residue, and 1 C-terminal amide. One tyrosine exists as a phenolic sulfate ester. 22There are 9 residues of galactose, 9 residues of mannose, 1 residue of fucose, 11 residues of N-acetylglucosamine, 3 residues of N-acetylgalactosamine, and 8 sialic acid residues (29). *3 From sequence; the amide ammonia is distributed as 5 glutamine and 3 asparagine residues. *4 From sequence; the amide ammonia is distributed as 5 glutamine and 4 asparagine residues. 25 From sequence; the amide ammonia is distributed as 7 asparagine and 12 glutamine residues or as 6 asparagine and 12 glutamine residues (31). 266 or 7 residues of isoleucine. 27From sequence; there is 1 asparagine residue and 1 terminal amide. 28Analyses uncorrected for incomplete hydrolysis or destruction during hydrolysis. 29There are 20 or 21 residues of hexoses, 1 residue of fucose, 15 residues of glucosamine, and 5 residues of sialic acid. Galactosamine is absent (35). 3o Carbohydrate content in percentage: total hexose, 9.7; mannose, 3.1; galactose, 3.6; total hexosamine, 4.5; glucosamine, 3.1; galactosamine, 1.4; fucose, 0.6; sialic acid, 5.4.
8 3
g 2 E; s x s g
WI 22
3123,000 is the amino acid portion of the total weight of FSH which is considered to weigh 33,000 (38). 32Carbohydrate content in residues per mole: glucosamine, 14; galactosamine, 2; fucose, 2; mannose, 10; galactose, 5; sialic acid, 6. 3aCarbohydrate content in residues per mole: glucosamine, 7; galactosamine, 1; fucose, 0.4; mannose, 5; galactose, 2; sialic acid, 2. 34Carbohydrate content in residues per mole: glucosamine, 9: galactosamine, 1; fucose, 2; mannose, 5; galactose, 4; sialic acid, 5. 3sAnother amino acid analysis can be found in Ref. (42). 36 From sequence; carbohydrate is present. 3’ From sequence; the amide ammonia is distributed as 4 glutamine and 4 asparagine residues. Amino acid analyses by column chromatographic method can be found in Ref. (46). s8From sequence, the amide ammonia is distributed as 3 glutamine and 4 asparagine residues. Amino acid analysis by column chromatographic method can be found in Ref. (46). ** Zollinger-Ellison tumor fractions analyzed [Gregory, R. A., Tracy, H. J., Agarwal, K. L., and Grossman, M. I. (1969) Gut 10, 603-6081. 40From sequence; the amide ammonia is distributed as 3 glutamine and 1 asparagine residues. From electrophoretic examination of other glucagons it would appear that all have the same number of amide groups (54-58). 41 From sequence; column chromatographic analysis can be found in Ref. (60). 12 From sequence; the amide ammonia is distributed as 9 asparagine and 13 glutamine residues. Column chromato~aphic analysis can be found in Ref. (62). 43 From sequence; the amide ammonia is distributed as 9 asparagine and 14 glutamine residues. 44 Thirty percent of the molecules have leucine replaced by vahne (65). Reported here is the amino acid analysis of the leucine sequence. *5 From sequence; the amide ammonia is distributed as 6 asparagine and 11 glutamine residues. The analysis of the leucine sequence is cited here (see footnote 44). Column chromatographic analyses cited in Ref. (67). * From sequence; the amide ammonia is distributed as 5 asparagine and 11 glutamine residues. 47 Amino acid analyses by column chromatography cited in Ref. (71). 48 Arginine, 3 or 4 residues: threonine, 2 or 3 residues; serine, 4 or 5 residues; glycine, 5 or 6 residues; alanine, 4 or 5 residues; half-cystine, 1 or 2 residues; methionine, 2 or more residues. 4g From sequence; the amide ammonia is distributed as 2 asparagine and 2 glutamine residues. Jo From sequence; the amide ammonia is distributed as 1 asparagine residue and 1 glutamine residue. 51 From sequence; the amide ammonia is distributed as 1 glutamine residue. In Ref. (78) can be found the analysis of insulin from SpragueDawley rat. s2 See Ref. (79) for additional analyses of mouse insulins. 53 From sequence; the amide ammonia is distributed as 3 asparagine and 2 glutamine residues. 54 The data for the p-chain is not correctly described in Ref. (83). 65 From sequence; the amide ammonia is distributed as 3 glutamine and 1 asparagine residues; see also Ref. (86). SeFrom sequence; the amide ammonia is distributed as 1 asparagine and 2 glutamine residues. I7 From sequence; the amide ammonia is distributed as 2 asparagine residues and 1 C-terminal amide. Table continued
s z s E 2
;I E
2 $
b E;
0
Footnotes to Table 2 continued s8 From sequence; the amide ammonia is distributed as 3 ~utamine and 2 asparagine residues. 59 From sequence; the amide ammonia is distributed as 3 glutamine and 5 asparagine residues. See also Ref. (95). W From sequence; the amide ammonia is distributed as 4 glutamine and 2 asparagine residues. See also Refs. (99) and (100) for column chromatographic amino acid analyses and revision of previous structure. E1From sequence; the amide ammonia is assigned to 1 residue of glutamine. OzFrom sequence; the amide ammonia is assigned to 2 residues of glutamine. es From sequence; an N-terminal acyl group is present. The amide ammonia is distributed as 2 glutamine and 1 asparagine residues. Carbohydrate has been reported as follows (values expressed per milligram without correction for moisture and ash). Subunit CI: sugars, totalamount, 152 pg; fucose 0.037 pmol; mannose, 0.46 Kmol; galactose, trace; glucose, trace; N-acetylglucosamine, 0.288 or 0.112 pmol (an error was made in printing and one of these values refers to something else) (102). Subunit CII: sugars, total amount, 109 pg; fucose, 0.060 pmol; mannose, 0.232 pmol; Nacetylglucosamine, 0.191 or 0.120 (an error was made in printing and one of these values refers to something else) (102). Carbohydrate has also been reported as follows (103) in relative numbers of residues and the assumption of 10% moisture. Subunit CI: fucose, 0.4; mannose, 6.8; galactose, 0.1; glucosamine, 5.3; galactosamine, 1.6. Subunit CII: fucose, 0.7; mannose, 2.5; galactose, 0; glucosamine, 3.6; g~actosamine, 1.4. Intact luteinizing hormone; fucose, 1.6; mannose, 8.7; glucosamine, 8.7; galactosamine, 3.6. Amino acid analyses done by column chromatography may be found in Refs. (102) and (103).
61 Carbohydrate reported as grams per 100 g (piven in order of a-subunit, psubunit, and hormone): fucose, 0.34,0.67,0.60; mannose, 5.37,2.62,4.32; galactose, 1.75, 3.65, 3.31; glucosamine, 5.73, 4.82, 4.72; galactosamine, 1.59, 1.64, 2.90; sialic acid, 4.97, 9.47, 7.70 (104). An earlier carbohydrate analysis can be found in Ref. (105). 85 From sequence. Column chromatographic amino acid analyses can be found in Refs. (106) and (107). Carbohydrate analyses (reported as residues per mole assuming 5.0 residues of valine): fucose, 0.5; mannose, 4.3; galactose, 2.2; glucosamine, 7.2; galactosamine, 1.1; sialic acid, 0.2 (107). W From sequence. w From sequence; an N-terminal acyl group is also reported (109). Column chromatographic analyses can be found in Ref. (107). Carbohydrate analysis (reported as residues per mole assuming 9 residues of valine): fucose, 0.6; mannose, 2.0; galactose, 0.9; glucosamine, 3.3; galactosamine, 0.5; sialic acid, 0 (107). W Amino acid analyses were reported for three different times of hydrolysis: 24, 48, and 72 hr. I have taken the 72-hr results for aIJ amino acids, except that the 26hr result was used for threonine, serine, and methionine. The value for tyrosine is 5 or 6 residues. All results are uncorrected for hydrolytic destruction, moisture, and ash. Carbohydrate results, reported as residues per 27,OOOg, are: sialic acid, 1.6; hexoses, 18.1; hexosamine, 7.5. See also Refs. (110) and (111). m Column chromatographic analysis can be found in Refs. (112), (113), and (114). Carbohydrate analyses for subunits A and B prepared by countercurrent distribution and by sulfitolysis and chromatography can be found in Ref. (113). ‘O From sequence; the amide ammonia is distributed as 2 glutamine residues and 1 carbohydrate-blocked asparagine residue. Column chromatographic analysis can be found in Ref. (115).
2 s $
z
k E
” AR N-terminal acyl group is present. 72 Hydrolysis in 6 N HCl for 24 hr. No corrections made for decomposition losses. Carbohydrate: (6hr hydrolysis in 4 N HCl; reported as residues per 28,300 daltons): glucosamine, 7; galactosamine, 3.2. Additional chromatographic analyses may be found in Refs. (117), (118), and (113) and additional carbohydrate results in Ref. (117). t3 From sequence; the amide ammonia is distributed as 2 glutamine and 4 asparagine residues of which 2 asparagine residues have carbohydrate attached. 74From sequence; the amide ammonia is distributed as 2 glutamine and 1 asparagine residues of which 1asparagine has carbohydrate attached. There is an N-terminal acyl group. There is a possible form with 1 arginine residue replaced by a glutamyl residue. r5 Carbohydrate (reported as residues per mole in the order C-t, C-2, intact hormone): giucosamine, 8, 4, 13; galactosamine 1, 1, 3; galactose, I, I, 2; mannose, 3, 2, 6; fucose, 1, 1, 2. 78 From sequence. See Ref. (122) for column chromatographic analysis. 77 From sequence. There is an N-terminal acyl group and the amide is C-terminal. See Ref. (125). 78 Some 50% of the molecules are C-terminal amidated. A tyrosyl dogfish hormone is mentioned here; it has 1 tyrosine residue in addition to the other residues of the a-MSH (130). From sequence. rB From sequence; amide ammonia is distributed as an asparagine residue and a C-terminal glycine amide. so From sequence; the amide ammonia is distributed as 1 asparagine residue, 1 glutamine residue, and 1 C-terminal glycine amide. *I From sequence; the amide ammonia is distributed as 1 asparagine residue and 1 C-terminal glycine amide. Table
continued
8ZFrom sequence; the amide ammonia is distributed as 1 asparagine residue, 1 glutamine residue, and 1 C-terminal glycine amide. *3 From enzymatic hydrolysis and from sequence; the amide ammonia is distributed as 5 glutamine residues and 3 asparagine residues (165,166). Amino acid analyses of interest can be found in Ref. (167). BdFrom enzymatic digestion (169) and sequence (168); the amide ammonia is distributed as 5 glutamine residues and 3 asparagine residues. 84itReferences (139,140,142-145,147,149,158-1~). WJ References (152-156,161,162). ** References (155,162,163). 85 From sequence; the amide ammonia is distributed as 3 glutamine residues, 2 asparagine residues, and 1 C-terminal amide. SfiFrom sequence; the amide ammonia is distributed as 1 asparagine residue and 1 C-terminal amide. a1 Uncorrected for hydrolytic destruction; results calculated on basis of 196 residues per mole, excluding tryptophan. BBThis preparation contains carbohydrate. 89 In the amino acid content, Ref. (175) reports one less leucine residue in the sequence. Column chromatographic analysis can be found in Ref. (176). e0 From sequence; the amide ammonia is distributed as 11 asparagine residues and 7 glutamine residues. Although 22 leucine residues are reported in Ref. (177), the correct number is 23 residues (178). 111From sequence; the amide ammonia is distributed as 12 asparagine residues and 8 glutamine residues. Column chromatographic analysis can be found in Refs. (178-180). 92 From sequence; the amide ammonia is distributed as 2 glutamine residues and 1 C-terminal amide.
Ln z
% 9 3 ffZ p x E
5 g v,
ki?
b F3
Liz
$2
to Table
2 continued
s3Results based on 2 residues of histidine per 15,000 MW. There are 8 or 9 arginine residues, and the presence of tryptophan is questionable. Carbohydrate analysis gave the fobllowing results (in percentages): arabinose, 6.6; xylose, 25.5; mannose, 15.6; galactose, 4.4; glucose, 32.5; acetylglucosamine, 3.9; unknown peak, 11.3. s4 From sequence; the amide ammonia is dist~buted as 3 asparagine residues and I C-terminal amide. g5Aspartic acid; 1 or 2 residues; tyrosine, 0 or 1 residue; serine and threonine values not corrected for losses during hydrolysis. BBFrom sequence: amide ammonia is distributed as 1 asparagine residue, 2 glutamine residues, and 1 C-terminal amide. Column chromatographic analyses can be found in Ref. (188). *’ Prom sequence; amide ammonia is dist~buted as 2 asparagine residues, 2 glutamine residues, and t C-terminal amide. s8 From sequence; amide ammonia is dist~buted as 4 asparagine residues and I C-terminal amide, In Ref. (191) the structure of porcine calcitonin-I is reported. The analysis is exactly the same as No. 247. O9From sequence; the amide ammonia is distributed as 4 glutamine and 2 asparagine residues. There is an error on p. 362 of Ref. (19.5) in the paragraph “amino acid composition of TPII:” 4 proline residues are reported as present in the sequence but there are only 2 residues. loo No correction made for moisture or ash. Values adjusted to 14.4 residues of aspartic acid which has been rounded off to I4 residues; 3.3 residues of glucosamine and 1.0 residue of galactosamine present. lo* From sequence; column chromatographic analysis can be found in Ref. (197).
Fooinotes
lo2 From sequence; amino acid analyses and carbohydrate analyses can also be found in Refs. (202) and (203). Carbohydrate analyses from Ref. (201): a-subunit, p-subunit (residues per molecule): fucose, 0.3, 0.9; mannose, 5.8, 2.5; galactose, 0.2, 0; glucosamine, 6.4,3.1; galactosamine, 2.5, 1.5. rM From sequence; there is a C-terminal amide. See Ref. (211). lo4 A recent report states that this is inactive (208). ‘05 From sequence; there is 1 asparaghte residue. *06This molecular weight includes 12 atoms of iron and sulfur. lo7 There are 3.7 atoms of iron and 4.0 atoms of sulfide in 4.2 form. ‘OSThere are 3.6 atoms of iron and 3.9 atoms of sulfide in 4.4 form. log These values have not been corrected for low recoveries due to degradation or nonrelease during hydrolysis. rosa3 half-cystine residues found upon amino acid analysis, and 4 residues found by pCMB titration. Ilo Threonine, 24 or 2.5 residues; serine, 19-21 residues. ‘I* 38 residues of glucosamine. rl* In addition to these results from a 20-hr hydrolysate the results of a 22-hr hydrolysate are also reported in Ref. (228). ‘I3 Following reported as residues per 100,000 MW: glucosamine (as N-acetyl derivative), 21; galactosamine (as N-acetyi derivative), 4; glucose, 3; fucose, 5; mannose, 6, galactose, 6 (238). ‘I* From sequence. Column chromatographic amino acid analyses may be found in Refs. (246-248). There is one sulfite group attached to a tyrosine residue.
!iL
!2
13 3 6 s: jr; 9 g
AMINO
ACID ANALYSES
REFERENCES
OF PROTEINS.
XII
513
FOR TABLE 2
1. Fliegerova, O., Salvetova, A., Ticha, M., and Kocourek, J. (1974) B&him. Biophys. Acta 351, 416-426. 2. Petersen, T. E., Roberts, H. R., Sottrup-Jensen, L., and Magnusson, S. (1976) Protides Biol. Fluids 23, 145- 149. 3. Strickland, W. N., Strickland, M., Brandt, W. F., Morgan, M., and Von Holt, C. (1974) FEES Lett. 40, 161-166. 4. Bailey, G. S., and Dixon, G. H. (1973) J. Biol. Chem. 248, 5463-5472. 5. Brandt, W. F., Strickland, W. N., and Von Holt, C. (1974) FEES Lett. 40, 349-352. 6. Brandt, W. F., Strickland, W. N., Morgan, M., and Von Holt, C. (1974) FEES Lett. 40, 167-172. 7. (a) Brandt, W. F., and Von Holt, C. (1974) Eur. J. Biochem. 46, 419; (b) (1971) FEES Lett. 14, 338-340; (c) (1972) FEES Lett. 23, 357-360. 8. Marzluff, Jr., W. F., Sanders, L. A., Miller, D. M.. and McCarthy, K. S. (1972) J. Biol.
Chem.
247, 2026-2033.
9. Patthy. L., Smith, E. L., and Johnson, J. (1973) J. Biol. Chem. 248, 6834-6840. 10. Hooper, J. A., Smith, E. L., Sommer, K. R., and Chalkley, R. (1973) J. Biol. Chem. 248,
3275-3279.
11. De Lange, R. J., Hooper, J. A., and Smith, E. L. (1973) J. Biol. Chem. 248, 3261-3274. 12. (a) De Lange, R. J., Fambrough, D. M., Smith, E. L., and Bonner, J. (1969) J. Bid. Chem. 244, 319-334; (b) Ogawa, Y., Quagliarotti, G., Jordan, J., Taylor, C. W., Starbuck, W. C., and Busch, H. (1969) J. Biol. Chem. 244, 4387-4392. 13. Sautiere, P.. Tyrou, D., Moschetto, Y., and Biserte, G. (1971) Biochimie 53, 479-483. 14. Sautiere, P., Lambelin-Breynaert, M. D., Moschetto, Y., and Biserte, G. (1971) Biochimie 53, 711-715. 15. Ishikawa, K., Hayashi, H., and Iwai, K. (1972) J. Biochem. (Tokyo) 72, 299-326. 16. Yokotsuka, K., Kikuchi, A., and Shimura, K. (1972) J. Biochem. (Tokyo) 71, 133-146. 17. Sautiere, P., Tyrou, D., Laine, B., Mizon, J., Ruffin, P., and Biserte, G. (1974) Eur. J. Biochem. 41, 563-576. 18. Wouters-Tyrou, D., Sautiere, P., and Biserte, G. (1974) Biochim. Biophys. Acta 342, 360-366.
19. Yeoman, L. C., Olson, M. 0. J., Sugano, N., Jordan, J., Taylor, C. W., Starbuck, W. C., and Busch, H. (1972) J. Biol. Chem. 247, 6018-6023. 20. Sautiere, P., Tyrou, D., Laine, B., Mizon, J., Lambelin-Breynaert, M. D., Ruffin, P., and Biserte, G. (1972) C’. R. Acad. Sci. Paris 274D, 1422-1425. 21. Champagne, M., Pouyet, J., Ouellet, L.. and Garel, A. (1970) Bull. Sot. Chim. Bioj. 52, 377-390. 22.
23. 24. 25. 26.
27. 28. 29. 30. 31. 32. 33. 34.
Sonnenbichler, J., and Nobis, P. C. (1970) Eur. J. Biochem. 16, 60-65. Graf, L., Bajusz, S., Patthy, A., Barat, E., and Cseh, C. (1971) Acta Biochim. Biophys. 6, 415-418. Riniker, B., Sieber, P., Rittel, W., and Zuber, H. (1972) Nature New Biol. 235, 114- 116. Johl, A., Riniker, B., and Schenkel-Hulliger, L. (1974) FEES Lett. 45, 172-174. Li. C. H. (1972) Biochem. Biophys. Res. Commun. 49, 835-839. Mutt, V., and Jorpes, J. E. (1971) Biochem. J. 125, 57p-58~. Morgan, F. J., Birken, S., and Canfield, R. E. (1975) J. Biol. Chem. 250, 5247-5258. Bahl, 0. P. (1969) J. Biol. Chem. 244, 567-574. Li, C. H., Dixon, J. S., and Chung, D. (1973) Arch. Biochem. Biophys. 155, 95- 110. Niall, N. D., Hogan, M. L., Tregear, G. W., Segre, G. V., Hwang, P., and Friesen, H. (1973) Rec. Progr. Harm. Res. 29, 387-416. Shome, B., and Friesen, H. G. (1971) Endocrinology 89, 631-641. Fernlund, P., and Josefsson, L. (1972) Science 177, 173-175. Femlund, P. (1971) Biochim. Biophys. Acta 237, 519-529.
514
DONALD
M. KIRSCHENBAUM
35. De La Llosa, P., Hermier, C., De La Llosa, P., and Jutisz, M. (1965) Bull. Sot. Chim. Biol. 47, 1073- 1078. 36. Papkoff, H., Gospodarowicz, D., and Li, C. H. (1967) Arch. Biochem. Biophys. 120,434-439.
37. Cahill, C. L., Shetlar, M. R., Payne, R. W., Endecott, B., and Li, Y. T. (1968) Biochim. Biophys.
Acta
154, 40-52.
38. Sherwood, 0. D., Grimek, H. J., and McShan, W. H. (1970) J. Biol. Chem. 245, 2328-2336. 39. Grimek, H. J., and McShan, W. H. (1974) J. Biol. Chem. 249, 5725-5732. 40. Papkoff, H., Mahlmann, L. J., and Li, C. H. (1967) Biochemistry 6, 3976-3982. 41. Saxena, B. B., and Rathnam, P. (1971) J. Biol. Chem. 246, 3549-3554. 42. Amir, S. M., and Parlow, A. F. (1972) Proc. Sot. Exp. Biol. Med. 139, 1120-1122. 43. Shome, B., and Parlow, A. F. (1974) J. Clin. Endocrinol. Metabol. 39, 199-202. 44. Rathnam, P., and Saxena, B. B. (1975) .I. Biol. Chem. 250, 6735-6746. 45. Shome, B., and Parlow, A. F. (1974) J. Clin. Endocrinol. Metabol. 39, 203-205. 46. Saxena, B. B., and Rathnam, P. (1976) J. Biol. Chem. 251, 993-1005. 47. Gregory, H., Hardy, P. M., Jones, D. S., Kenner, G. W., and Sheppard, R. C. (1964) Nature (London) 204,93 l-933. 48. Bentley, P. H., Kenner, G. W., and Sheppard, R. C. (1966) Nature (London) 209, 583-585. 49. Gregory, R. A., and Tracy, H. J. (1973) Mt. Sinai J. Med. 40, 359-364. 50. Agarwal, K. L., Beacham, J., Bentley, P. H., Gregory, R. A., Kenner, G. W., Sheppard, R. C., and Tracy, H. J. (1968) Nature (London) 219, 614-615. 51. Agarwal, K. L., Kenner, G. W., and Sheppard, R. C. (1969) Experientia 25,346-348. 52. Agarwal, K. L., Kenner, G. W., and Sheppard, R. C. (1969) J. Amer. Chem. Sot. 91, 3096-3097.
53. (a) Bromer, W. W., Staub, A., Diller, E. R., Bird, H. L., Sinn, L. G., and Behrens, 0. K. (1957) J. Amer. Chem. Sot. 79, 2794-2798; (b) Bromer, W. W., Sinn, L. G., and Behrens, 0. K. (1957) J. Amer. Chem. Sot. 79, 2807-2810. 54. Sundby, F., and Markussen, J. (1971) Horm. Metabol. Res. 3, 184-187. 55. Bromer, W. W., Boucher, M. E., and Koffenberger, J. E., Jr. (1971) J. Biol. Chem. 246, 2822-2827. 56. Sundby, F., and Markussen, J. (1972) Harm. Metabol. Res. 4, 56. 57. Thomsen, J., Kristiansen, K., and Brunfeldt, K. (1972) FEBS Lett. 21, 315-319. 58. Sundby, F., Markussen, J., and Danko, W. (1974) Horm. Metabol. Res. 6, 425. 59. Zakin, M. M., Paskus, E., Dellacha, J. M., Paladini, A. C., and Santome, J. A. (1973) FEBS Left. 34, 353-355. 60. Conde, R. D., Paladini, A. C., Santome, J. A., and Dellacha, J. M. (1973) Eur.
J. Biochem.
32, 563-568.
61. Li, C. H., and Dixon, J. S. (1971) Arch. Biochem. Biophys. 146, 233-236. 62. (a) Dixon, J. S., and Li, C. H. (1962) J. Gen. Physiol. Suppl. 45, 169-178; (b) Meisinger, M. A. P., Cirillo, V. J., Davis, G. E., and Reisfeld, R. A. (1964) Nature (London) 201, 820-821; (c) Bewley, T. A., Brovetto-Cruz, J., and Li, C. H. (1969)
Biochemistry
8, 4701-4708.
63. Niall, H. D., Hogan, M. L., Tregear, G. W., Segre, G. V., Hwang, P., and Friesen, H. (1973) Rec. Progr. Horm. Res. 29, 387-416. 64. Santome, J. A., Dellacha, J. M., Paladini, A. C., Wolfenstein, C. E. M., Pena, C., Poskus, E., Daurat, S. T., Biscoglio, M. J., De Sese, Z. M. M., and De Sanguesa, A. V. F. (1971) FEBS Lett. 16, 198-200. 65. Daurat, S. T., Femandez, H. N., Dellacha, J. M., Paladini, A. C., and Santome, J. A. (1970) 6th Nat. Meet. Sot. Arg. Inves. Bioquim., abstract P 39; cited in Ref. (64). 66. Wallis, M. (1973) FEBS Lett. 35, 11-14.
AMINO
ACID ANALYSES
OF PROTEINS.
XII
51.5
67. (a) Parcells, A. J. (1961) Nature (London) 192, 971-972; (b) Glaser, C. B., and Li, C. H. (1974) Biochemistry 13, 1044-1047. 68. Li, C. H., Gordon, D., and Knorr, J. (1973) Arch. Biochem. Biophys. 156, 493-508. 69. Fernandez, H. N., Pena, C., Poskus, E., Biscoglio, M. J., Paladini, A. C., Dellacha, J. M., and Santome, J. A. (1972) FEBS Lett. 25, 265-270. 70. Bellair, J. T. (1972) Biochem. Biophys. Res. Commun. 46, 1128-1134. 71. Dellacha, J. M., Enero, M. A., Santome, J. A., and Paladini, A. C. (1970) Eur. J. Biochem.
72. 73. 74. 75. 76. 77. 78. 79. 80. 81. 82. 83. 84. 85. 86. 87. 88. 89. 90. 91. 92. 93. 94. 95. 96. 97. 98. 99. 100. 101. 102.
12, 289-295.
Kleinholz, L. H. (1975) Nature (London) 258, 256-257. Kotaki, A. (1962) J. Biochem. (Tokyo) 51, 301-309. Kotahi, A. (1963) J. Biochem. (Tokyo) 53, 61-70. Hama, H., Titani, K., Sakaki, S., and Narita. K. (1964) J. Biochem. (Tokyo) 56, 285-293. Smith, L. F. (1966) Amer. J. Med. 40, 662-666. Bunzli, H. F., and Humbel, R. E. (1972) Hoppe-Seyler’s Z. Physiol. Chem. 353, 444-450. Steiner, D. F., Clark, J. L., Nolan, C., Rubenstein, A. H., Margoliash, E., Aten, B., and Oyer, P. E. (1969) Rec. Progr. Norm. Res. 25, 207-282. Markussen, J. (1971) Int. J. Protein Res. 3, 149-155. Ishihara, Y., Saito, T., Ito, Y., and Fujino, M. (1958) Nature(London) 181, 1468-1469. Harris, J. I., Sanger, F., and Naughton, M. A. (1956) Arch. Biochem. Biophys. 65, 427-438. Markussen, J., and Sundby, F. (1973) Int. J. Protein Res. 5, 37-48. Vensel, W. H., Pollock, H. G., and Kimmel, J. R. (1974) Fed. Proc. 33, Abstract No. 413. (a) Sanger, F., and Tuppy, H. (1951) Biochem. J. 49, 463-481, 481-490; (b) Sanger, F., and Thompson, E. 0. P. (1953) Biochem. J. 53, 353-366, 366-374. Nicol, D. S. H. W., and Smith, L. F. (1960) Nature (London) 187, 483-485. Smith, L. F. (1972) Diabetes 21, 457-460. Neumann, P., and Humbel, R. E. (1969) Int. J. Protein Res. 1, 125-140. Reid, K. B. M., Grant, P. T., and Youngson, A. (1968) Biochem. J. 110, 289-296. Neumann, P. A., Koldenhof, M., and Humbel, R. E. (1969) Hoppe-Seyler’s Z. Physiol. Chem. 350, 1286- 1288. Brown, H., Sanger, F., and Kitai, R. (1953) Biochem. J. 60, 556-565. Fernlund, P. (1976) Biochim. Biophys. Acta 439, 17-25. Graf, L., Barat, E., Cseh, C., and Sajgo, M. (1971) Biochim. Biophys. Acta 229, 276-278. Gilardeau, C., and Chretien, M. (1972) in Chemistry and Biology of Peptides (Meienhofer, J., ed.), pp. 609-611. Ann Arbor Science, Ann Arbor, Mich. Li, C. H., and Chung, D. (1976) Nature (London) 260, 622-624. Chretien, M., Gilardeau, C., Seidah, N., and Lis, M. (1976) Canad. J. Biochem. 54, 778-782. Graf, L., and Li, C. H. (1973) Biochem. Biophys. Res. Commun. 53, 1304-1309. Graf, L., Cseh, G., and Sajgo, M. (1971) in Polypeptide Hormones (Goth, E., and Forenyi, J., eds.), pp., 185-189. Akademiai Kiado, Budapest. Chretien, M., and Li, C. H. (1967) Canad. J. Biochem. 45, 1163-1174. Li, C. H., Barnafi, L., Chretien, M., and Chung, D. (1965) Nature (London) 208, 1093-1094. Chretien, M., Gilardeau, C., and Li, C. H. (1972) Int. J. Peptide Protein Res. 4, 263-265. Maghuin-Rogister, G., and Hennen, G. (1973) Eur. J. Biochem. 39, 235-253. Hennen, G., Maghuin-Rogister, G., and Mamoir, G. (1970) FEBS Lett. 9, 20-26.
516
DONALD
M. KIRSCHENBAUM
103. Pierce, J. G., Liao, T. H., Howard, S. M., Shome, B., and Cornell, J. S. (1971) Rec. Progr. Horm. Res. 27, 165-212. 104. Landefeld, T. D., and McShan, W. H. (1974) Biochemistry 13, 1389-1393. 105. Landefeld, T. D., Grimek, H. J., and McShan, W. H. (1972) Biochem. Biophys. Res. Commun. 46, 463-469. 106. Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem. Biophys. Res. Commun. 48, 530-537.
107. Hartree, A. S., Thomas. M., Braikevitch, M., Bell, E. T., Christie, D. W., Spaull, G. V., Taylor, R., and Pierce, J. G. (1971) J. Endocrinol. 51, 169-180. 108. (a) Shome, B., and Parlow, A. F. (1973) Fed. Proc. 32, 281, abstract No. 372; (b) Closset, J., Henner, G., and Lequim, R. M. (1973) FEBS Lerr. 29, 97-100. 109. Rathnam, P., and Saxena, B. B. (1970) J. Biol. Chem. 245, 3725-3731. 110. Rathnam, P., and Saxena, B. B. (1971) J. Biol. Chem. 246, 7087-7094. 111. Ward, D. N., Reichert, L. E., Liu, W-K., Nahm, H. S., Hsia, J., Lamkin, W. M., and Jones, N. S. (1973) Rec. Progr. Horm. Res. 29, 533-561. 112. Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Arch. Biochem. Biophys. 153, 554-572.
113. Lamkin, W. M., Fujino, M., Mayfield, J. D., Holcomb, G. H., and Ward, D. N. (1970) Biochim. Biophys. Acta 214, 290-298. 114. Sairam, M. R., and Li, C. H. (1974) Arch. Biochem. Biophys. 165, 709-714. 115. Sairam, M. R., Samy, T. S. A., Papkoff, H., and Li, C. H. (1972) Arch. Biochem. Biophys. 153, 572-586. 116. Gospodarowicz, D. (1972) J. Biol. Chem. 247, 6491-6498. 117. Papkoff, H., Gospodarowicz, D., Candiotti, A., and Li, C. H. (1965) Arch. Biochem. Biophys. 111, 431-438. 118. Ward, D. N., Walborg, E. F., and Adams-Mayne, M. (1961) Biochim. Biophys. Acta 50, 224-232.
119. Maghuin-Rogister,
G., Combamous,
Y., and Hennen, G. (1973) Eur. J. Biochem.
39, 255-263.
120. Ward, D. N., Reichert, L. E., Jr., Fitach, B. A., Nahm, H. S., Sweeney, C. M., and Neill, J. D. (1971) Biochemistry 10, 1796-1802. 121. Matsuo, H., Baba, Y., Nair, R. M. G., Arimura, A., and Schally, A. V. (1971) Biochem. Biophys. Res. Commun. 43, 1334-1339. 122. Schally, A. V., Nair, R. M. G., Redding, T. W., and Arimura, A. (1971) J. Biol. Chem. 246, 7230-7236. 123. Lo, T. B., Dixon, J. S., and Li, C. H. (1961) Biochim. Biophys. Acra 53, 584-586. 124. Harris, J. I., and Lerner, A. B. (1957) Nature (London) 179, 1346-1347. 125. Harris, J. I. (1959) Biochem. J. 71, 451-459. 126. Dixon, J. S., and Li, C. H. (1960) J. Amer. Chem. Sot. 82, 4568-4572. 127. Lee, T. H., Lerner, A. B., and Buettner-Janusch, V. (1963) Biochim. Biophys. Acta 71, 706-709. 128. Lowry, P. J., Bennett, H. P. J., McMartin, C., and Scott, A. P. (1974) Biochem. J. 141,439-444.
129. Lee, T. N., Lerner, A. B., and Buettner-Janusch, V., (1961) J. Biol. Chem. 236, 1390-1394. 130. Lowry, P. J., and Chadwick, A. (1970) Biochem. J. 118, 713-718. 131. Harris, J. I. (1959) Nature (London) 184, 167-169. 132. Geschwind, I. I., Li, C. H., and Barnafi, L. (1957) J. Amer. Chem. Sot. 79, 1003- 1004. 133. (a) Harris, J. I., and Roos, P. (1956) Nature (London) 178, 90; (b) Geschwind, I. I., Li, C. H., and Barna8, L. (1957) J. Amer. Chem. Sot. 79, 620-625.
AMINO
ACID
ANALYSES
OF PROTEINS.
517
XII
134. Dixon, J. S., and Li, C. H. (1961) Gen. Camp. Endocrinol. 1, 161-169. 135. Acher, R., Chauvet, J., and Chauvet, M. T. (1972) Eur. J. Biochem. 29, 12-19. 136. Chauvet, J., Chauvet, M. T., Beaupain, D., and Acher, R. (1965) C. R. Acad. Sci. Paris
261, 4234-4236.
137. Acher, R., Chauvet, J., and Chauvet, M. T. (1967) Nature (London) 216, 1037-1038. 138. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1962) B&him. Biophys. Acta
58, 624-625.
139. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1968) Gen. Camp. Endocrinol. 11, 535-538.
140. Acher, R., Chauvet, J., Chauvet. M. T., and Crepy, D. (1965) Comp. Physiol.
Biochem.
14, 245-254.
141. Acher, R., Chauvet, J., and Chauvet, M. T. (1970) FEB.9 Lerr. 11, 332-335. 142. Wilson, N., and Smith, M. (1969) Gen. Comp. Endocrinol. 13, 412-424. 143. Acher, R., Chauvet. J., and Chauvet, M. T. (1968) Biochim. Biophys. Acra 154, 255-257. 144. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1964) Biochim. Biophys. Acra 90, 613-615. 145. Acher, R., Chauvet, J., and Chauvet, M. T. (1970) Eur. J. Biochim. 17, 509-513. 146. Acher, R., Chauvet, J., and Chauvet, M. T. (1969) Nature (London) 221, 759-760. 147. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1967) Gen. Camp. Endocrinol.
8, 337-343.
148. Acher, R., Chauvet, J., and Chauvet, M. T. (1970) Nature (London) 227, 186-187. 149. Acher, R., Chauvet, J., and Chauvet, M. T. (1969) Gen. Camp. Endocrinol. 13, 357-360. 150. (a) Du Vigneaud, V., Ressler, C., and Trippett, S. (1953) J. Biol. Chem. 205, 949-957; (b) Tuppy, H., and Michl, H. (1953) Monarsh. Chemie 84, 1011-1020. 151. Pierce, J. G., Gordon, S., and Du Vigneaud, V. (1952) J. Biol. Chem. 199, 929-940. 152. Light, A., and Du Vigneaud, V. (1958) Proc. Sot. Exp. Biol. Med. 98, 692-696. 153. Acher, R., Chauvet, J., and Lenci, M. T. (1958) Bull. Sot. Chim. Biol. 40, 2005-2018. 154. Acher, R., Chauvet, J., and Chauvet. M. T. (1964) Nature (London) 201, 191-192. 155. Ferguson, D. R., and Pickering, B. T. (1969) Gen. Camp. Endocrinol. 13, 425-429. 156. Acher, R., Chauvet, J., and Lenci, M. T. (1959) C. R. Acad. Sci. 248, 1435-1438. 157. Pickering, B. T.. and Heller, H. (1969) J. Endocrinol. 45, 597-606. 158. Acher, R., Chauvet, J., Lenci, M. T., Morel, F., and Maetz, J. (1960)Biochim. Biophys. Acfa
42, 379-380.
159. Heller, H.. and Pickering, B. T. (1961) J. Physiol. 155, 98-114. 160. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1961) Biochim. Acra
Biophys.
51, 419-420.
161. (a) Du Vigneaud, V., Lawler, H. C., and Popenoe, E. A. (1953) J. Amer. Chem. Sot. 75, 4880-4881; (b) Acher, R., and Chauvet, J. (1953) Biochim. Biophys. Acra 12, 487-488. 162. Stewart, A. D. (1968) J. Endocrinol. 44, XIX-XX. 163. Popenoe, E. A., Lawler, H. C., and Du Vigneaud, V. (1952) J. Amer. Chem. Sot. 74, 3713. 164. Keutmann, H. T., Barling, P. M., Hendy, G. N., Segre, G. V., Niall, H. D., Aurbach, G. D., Potts, J. T.. and O’Riordan, J. L. H. (1974) Biochemistry 13, 1646-1652.
165. Niall, H. D.. Keutmann, H., Sauer, Potts, J., Jr. (1970) Hoppe-Seyler’s 166. Keutmann, H. T., Aurbach, G. D., Potts, J. T., Jr. (1971) Biochemistry
R., Hogan, M., Dawson, B., Aurbach, 2. Physiol.
Chem.
351,
G., and
1586-1588.
Dawson, B. F., Niall, H. D., Deftos, L. J., and 10, 2779-2787.
518
DONALD
M. KIRSCHENBAUM
167. Tashjian, A., Ontjes, D., and Munson, P. L. (1964) Biochemistry 3, 1175-1182. 168. Sauer, R. T., Niall, H. D., Hogan, M. L., Keutmann, H. T., O’Riordan, J. L. H., and Potts, J. T., Jr. (1974) Biochemistry 13, 1994-1999. 169. Woodhead, J. S., O’Riordan, J. L. H., Keutmann, H. T., Stoltz, M. L., Dawson, B. F., Niall, H. D., Robinson, C. J., and Potts, J. T., Jr. (1971) Biochemistry 10,2787-2792. 170. Hamilton, J. W., Niah, H. D., Keutmann, H. T., Potts, J. T., Jr., and Cohn, D. V. (1973) Fed. Proc. 32, 269, abstract No. 315. 171. Kimmel, J. R., Hayden, L. J., and Pollock, H. G. (1975) J. Biol. Chem. 250, 9369-9376.
172. Fernlund, P. (1974) Biochim. Biophys. Acta 371, 304-311. 173. Farmer, S. W., Clarke, W. C., Papkoff, H., Nishioka, R. S., Bern, H. A., and Li, C. H. (1975) Life Sci. 16, 149-158. 174. Wallis, M. (1974) FEBS Lett. 44, 205-208. 175. Graf, L. (1971) in Polypeptide Hormones (Goth, E., and Forenyi, J., eds.), pp. 255-262, Akademiai Kiado, Budapest. 176. Yudaev, N. A., Pankov, Y. A., Elizarova, G. P., Han, Z., and Nikolaeva, 0. P. (1975) Bioorg. Chem. 1, 97-112. 177. Li, C. H., Dixon, J. S., Lo, T. B., Schmidt, K. D., and Pankov, Y. A. (1970) Arch. 178.
Biochem. Biophys. 141, 705-737. Li, C. H. (1976) Znt. J. Peptide Protein Res. 8, 205-224. Eppstein, S. (1964) Nature (London) 202, 899-900. Clarke, W. C., and Li, C. H. (1974)Arch. Biochem. Biophys.
179. 180. 181. Hwang, P., Murray, Biochemistry
161, 313-318.
J. B., Jacobs, J. W., Niall, H. D., and Friesen, H. (1974)
13, 2354-2358.
182. Ellis, S., Grindeland,
R. E., Nuenke, J. M., and Callahan, P. X. (1969) Endocrinology
85, 886-894.
183. 184. 185. 186. 187. 188. 189. 190. 191. 192.
Mutt, V., Jorpes, J. E., and Magnusson, S. (1970) Eur. J. Biochem. 15, 513-519. Starr, R. C., and Jaenicke, L. (1974) Proc. Nat. Acad. Sci. USA 71, 1050-1054. Brewer, H. B., Jr., and Ronan, R. (1969) Proc. Nat. Acad. Sci. USA 63, 940-947. Nieto, A., Moya, F., and Candela, J. L. R. (1973) Biochim. Biophys. Acra 322, 383-391. Noda, T., and Narita, K. (1976) J. Biochem. (Tokyo) 79, 353-359. Otani, M., Yamauchi, H., Meguro, T., Kitazawa, S., Watanabe, S., and Orimo, H. (1976) J. Biochem. (Tokyo) 79, 345-352. Neher, R., Riniker, B., Rittel, W., and Zuber, H. (1968) Helv. Chim. Acta 51, 1900-1905. Potts, J. T., Jr., Niall, H. D., Keutmann, H. T., Brewer, H. B., and Deftos, L. J. (1968) Proc. Nat. Acad. Sci. USA 59, 1320-1328. Barg, W., Jr., Englert, M. E., Davies, M. C., Colucci, D. F., Snedeker, E. H., Dziobkowski, C., and Bell, P. H. (1970) Biochemistry 9, 1671-1676. Niall, H. D., Keutmann, H. T., Copp, D. H., and Potts, J. T., Jr. (1969) Proc. Nat. Acad.
Sci.
USA
64, 771-778.
193. Raulais, D., Hagaman, J., Ontjes, D. A., Lundblad, R. L., and Kingdon, H. S. (1976) Eur. J. Biochem. 64, 607-611. 194. Sauer, R., Niall, H. D., and Potts, J. T., Jr. (1970) Fed. Proc. 29,728 abstract No. 2723. 195. Schlesinger, D. H., and Goldstein, G. (1975) Cell 5, 361-365. 196. Pierce, J. G., and Wynston, L. L. (1960) Biochim. Biophys. Acta 43, 538-540. 197. Sairam, M. R., and Li, C. H. (1973) Biochem. Biophys. Res. Commun. 51, 336-342. 198. Sairam, M. R., and Li, C. H. (1973) Biochem. Biophys. Res. Commun. 54, 426-431. 199. Roos, P., Jacobson, G., and Wide, L. (1975) Biochim. Biophys. Acra 379, 247-261. 200. Liao, T. H., and Pierce, J. G. (1971) J. Biol. Chem. 246, 850-865. 201. Pierce, J. G. (1971) Endocrinology 89, 1331-1344.
AMINO
ACID ANALYSES
OF PROTEINS.
519
XII
202. Hennen, G., Maghuin-Rogister, G., and Mamoir, G. (1970) FEBS Lett. 9, 20-26. 203. Carsten, M. E., and Pierce, J. G. (1960) J. Biol. Chem. 235, 78-84. 204. Burgus, R., Butcher, M., Amoss, M., Ling, N., Monahan, M., Rivier, J., Fellows, R., Blackwell, R., Vale, W., and Guillemin, R. C. (1972) Proc. Nat. Acad. Sci. USA 69, 278-282. 205.
Baba, Y., Matsuo, H., and Schally, A. V. (1971) Biochem.
Biophys.
Res.
Commun.
44, 459-468.
Celis, M. E., Taleisnik, S., and Walter, R. (1971) Proc. Nat. Acad. Sci. USA 68, 1428- 1433. 207. Nair, R. M. G., Kastin, A. J., and Schally, A. V. (1971) Biochem. Biophys. Res. Commun. 43, 1376- 1381. 208. Grant, N. H., Clark, D. E., and Rosanoff (1973) Biochem. Biophys. Res. Commun. 51, lOO- 106. 209. Brazeau, P., Vale, W., Burugs, R., Ling, N., Butcher, M.. Rivier, J., and Guillemin
206.
(1973)
Science
179, 77-79.
210. Burgus, R., Dunn, T. F., Desiderio, D., and Guillemin, Paris
269D,
R. (1969) C. R. Acad.
Sci.
1870-1873.
211. Nair, R. M. G., Barrett, J. F., Bowers, C. Y., and Schally, A. V. (1970) Biochemistry 9, 1103-1106. 212. Chen, J. S., and Mortenson, E. (1974) B&him. Biophys. Acta 371, 283-298. 213. Gitlitz, P. H., and Krasna, A. I. (1970) Biochemistry 14, 2564-2568. 214. Duley, J. A., and Holmes, R. S. (1976) Eur. J. Biochem. 63, 163-173. 215. Bock, H. G., and Fleischer, S. (1975)J. Biol. Chem. 250, 5774-5781. 216. Wada, G. H., Fellman, J. H., Fujita, T. S., and Roth, E. S. (1975) J. Biol. Chem. 250, 6720-6726.
217. 218. 219. 220. 221.
Uwajima, T., Yagi, H., and Terada, 0. (1974) Agr. Biol. Chem. 38, 1149-I 153. Martin, R. G., Voll, M. J., and Appella, E. (1967)J. Biol. Chem. 242, 1175-1181. Merrick. W. C.. and Anderson, W. F. (1975)J. Biol. Chem. 250, 1197-1206. Heyde, E., and Morrison, J. F. (1976) Biochim. Biophys. Acra 429, 635-644. Yokosawa, H., Tobita, T., and Yamada, T. (1971) Biochim. Biophys. Acta 227,
222.
Krishnaiah, K. V. (1975) Arch. Biochem. Biophys. 170, 567-575. Creighton, T. E., and Yanofsky, C. (1966) J. Biol. Chem. 241, 4616-4624. Neumann, N. P., and Lampen, J. 0. (1967) Biochemisfry 6,468-475. Gascon, S., Neumann, N. P., and Lampen, J. 0. (1968)J. Biol. Chem. 243, 1573- 1577. Illingworth, J. A. (1972) Biochem. J. 129, 1119-1124. Buzdygon, B. E.. Braginski, J. E., and Chung, A. E. (1973) Arch. Biochem. Biophys.
538-553.
223. 224. 225. 226.
227.
159, 400-408.
228. Howard, R. L., and Becker, R. R. (197O)J. Biol. Chem. 245, 3186-3194. 229. Reeves, H. C., Daumy, G. O., Lin, C. C., and Houston. M. (1972) Biochim. Biophys.
Acta
258, 27-39.
230. Fan, C. C., and Plaut, G. W. E. (1974) J. Biol. Chem. 249, 4839-4845. 231. Barrera, C. R., and Jurtshuk. P. (1970) Biochim. Biophys. Acta 220, 416-429. 232. Chung, A. E.. and Franzen, J. S. (1969) Biochemisfry 8, 3175-3184. 233. Shen, W. C., Mauck, L., and Colman, R. F. (1974) J. Biol. Chem. 249, 7942-7949. 234. Shiio, I., Shiio, T., and McFadden, B. A. (1965) Biochim. Biophys. Acta 96, 114- 122. 235. Durekovic, A., Flossdorf, J., and Kula, M. R. (1973) Eur. J. Biochem. 36, 528-533. 236. Baldwin, A., and Berg, P. (1966) J. Biol. Chem. 241, 831-838. 237. Piszkiewicz. D., and Goitein. R. K. (1974) Biochemistry 13, 2505-2511. 238. Cogoli, A., Eberle, A., Sigrist, H., Joss, C., Robinson, E., Mosimann, H., and Semenza, G. (1973) Eur. J. Biochem. 33, 40-48. 239. Margolies, M. N., and Goldberger, R. F. (1967) J. Biol. Chem. 242, 256-264.
520
DONALD
M. KIRSCHENBAUM
240. Hofler, J. G., Decedue, C. J., Luginbuhl, G. H., Reynolds, J. A., and Burns, R. 0. (1975) J. Bid. Chem. 250, 877-882. 241. Sandermann, H., Jr., and Strominger, J. L. (1971) Proc. Nat. Acad. Sci. USA 68, 2441-2443. 242. Parsons, S. J., and Burns, R. 0. (1969) J. Eiol. Chem. 244, 996- 1003. 243. Bartholemew, J. C., and Calve, J. M. (1971) Biochim. Biophys. Acta 250, 568-576. 244. Webster, R. E., and Nelson, C. A., and Gross, S. R. (1965) Biochemistry 4,2319-2327. 245. Bartholomew, J. C., and Calvo, J. M. (1971) Biochim. Biophys. Acta 250, 577-587. 246. Bagdy, D., Barabas, E., and Graf, L. (1973) Thromb. Res. 2, 229-238. 247. Markwardt, F., and Walsmann, P. (1967) Hoppe-Seyler’s Z. Physiol. Chem. 348, 1381-1386. 248. De La Llosa, P., Tertrin, C., and Jutisz, M. (1963) Bull. Sot. Chim. Biol. 45, 69-74.
83, 484-520 (1977)
BIOCHEMISTRY
A Compilation
of Amino Acid Analyses of Proteins, Polypeptides, and Peptides XII. Residues DONALD
Department
of Biochemistry, Received
M.
per Molecule-9 KIRSCHENBAUM’
College of Medicine, Brooklyn, New York
Downstate 11203
Medical
Center-SUNY.
March 7, 1977; accepted July 26, 1977
I have changed the title of the series by the addition of the words “Polypeptides, and Peptides.” I felt this was necessary if the analyses of certain of the hormones of the hypophysis and the hormones (factors) of the hypothalamus are to be included. I have decided to include in these compilations the amino acid analyses of all substances for which amino acid analyses have been published. In this paper, the twelfth in the series and the ninth reporting amino acid analyses as residues per molecule, I have added an additional 272 proteins to the compilation (1). The major portion of the data I present is devoted to amino acid analyses of peptide and protein hormones and the hormones (factors) which control their release. As with previous publications in this series I have (a) rounded off the molecular weights to the nearest thousand for weights over 10,000 and to the nearest hundred for weights under 10,000; and (b) rounded off to an integral number the number of residues of amino acid reported. In Table 1, the Protein Index, I list the proteins and the sources from which they were obtained. In Table 2, I report the amino acid analyses derived from hydrolyzates or from sequences. If the sequence is the source I have indicated it in the footnote, and I have also reported the number of asparagine and glutamine residues and other amides. In addition, if a carbohydrate analysis was done, this too was reported in the footnote. For each analysis I have given a citation to the original literature, usually the first report of the data, and, for those proteins for which the sequence data supplied the analysis, I have given a citation to the column chromatographic analysis for amino acids. This permits a comparison to be made of the analytical data supplied by chromatographic methods with the absolute results of the sequence. ’ Faculty Exchange Scholar, State University of New York. 484 Copyright 0 1917 by Academic Ress, Inc. AU rights of reproduction in any form reserved.
1SSN OW3-2697
AMINO
ACID ANALYSES
OF PROTEINS.
485
XII
ACKNOWLEDGMENTS The Library of the Downstate Medical Center College of Medicine has been the major source of all publications examined. What was not available in the library was obtained for me from other libraries. I should like to thank the librarians for their most useful and continuing assistance. During the summers of 1971-1975, I was a Library Reader at the Library of the Marine Biological Laboratory, Woods Hole, Massachusetts. I should like to thank the librarians of that library for their assistance. I thank Mr. E. Becker for copy-reading assistance and for checking references.
REFERENCE
FORTEXT
1. The last published paper in this series is Kirschenbaum, 79, 470-501.
D. M. (1977) Anal. Biochem.
NOTE ADDED IN PROOF Corrections
for Part XI: Residues per Thousand Residues, 3l
Protein index numbefl
Residues reportedb
Conversion factof
10d 29 50 55 6Oc 97 125 126 143 178
983.5 967 963 905.4 972.5 986 1014 785 1162 1039
1.017 1.034 1.038 1.104 1.028 1.014 0.986 1.273 0.860 0.9625
a This is the number referring to the protein in Paper XI. * This is the value reported in the reference cited. c To convert the values given to 1000 residues one must multiply by this factor the given values. d The half-cystine content is 7.8 and not 2 as given. Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein Protein
index index index index index index index index index index index index index index
no. no. no. no. no. no. no. no. no. no. no. no. no. no.
8: The number of residues of glycine should be 19.3 22: The number of residues of arginine should be 39 184: Proline = 82 residues. 187: Proline = 113 residues. 194: Proline = 71 residues. 245: There are an additional 70 residues of omithine 246: There are an additional 60 residues of omithine 247: There are an additional 75 residues of omithine 248: There are an additional 50 residues of omithine 249: There are an additional 78 residues of omithine 250: There are an additional 86 residues of omithine 251: There are an additional 43 residues of omithine 252: There are an additional 66 residues of omithine 253: There are an additional 52 residues of omithine
and not 193. and not 29.
present. present. present. present. present. present. present. present. present.
486 Correction
DONALD
M. KIRSCHENBAUM
for Part IX: Residues per Mole of Protein,
72
Footnote 6 should read “The amide ammonia is distributed as 20 asparagine residues and 8 glutamine residues (Goldstein, J., Konigsberg, W., and Hill, R. J. (1963) J. Biol. Chem. 238, 2016-2027).
Corrections
for Part IV: Residues per Thousand Residues, I3
Protein index no. 18: Valine = 46 residues. Protein index no. 130a: The total number of residues is 876 [including the 18 residues of hydroxyproline]. The conversion factor to bring the values to 1000 residues is 1.14. Protein index no. 149: The total number of residues is 1049.9 and a factor of 0.953 is needed to convert the values back to 1000 residues.
Corrections
for Part V: Residues per Thousand Residues, 24,5
Protein index no. 319: Tyrosine = 30 residues. There are 1022 residues reported and a factor of 0.978 is needed to convert the values reported to 1000 residues. Protein index no. 207: 983.2 residues reported and a factor of 1.016 is needed to convert the values to 1000 residues. Protein index no. 300: 1052 residues reported and a factor of 0.951 is needed to convert values to 1000 residues. Protein index no. 301: 1058 residues reported and a factor of 0.945 is needed to convert values to 1000 residues. Protein index no. 3 17: 798 residues reported and a factor of 1.25 is needed to convert values to 1000 residues. Protein index no. 328: 978 residues reported and a factor of 1.022 is needed to convert values to 1000 residues. Protein index no. 332: 1034 residues reported and a factor of 0.967 is needed to convert values to 1000 residues. Protein index no. 344: 931 residues reported and a factor of 1.074 is needed to convert values back to 1000 residues. r Kirschenbaum, Donald M. (1977) Anal. 2 Kirschenbaum, Donald M. (1975) Anal. 3 Kirschenbaum, Donald M. (1973) Anal. 4 Kirschenbaum, Donald M. (1973) Anal. 5 I should like to thank Dr. A. Reisner, information concerning these corrections.
Biochem. 79, 470-501. Biochem. 65, 466-499. Biochem. 53, 223-244. Biochem. 56, 208-236. CSIRO, N. S. W. Australia
for providing
the
AMINO
ACID ANALYSES
OF PROTEINS.
TABLE PROTEIN
1 Name 2 3 4 5
6 7 8 9
10 11 12 13 14 15 16
Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source
17 Name Source
18 Name Source
19 Name 20
21 22
Source Name Source Name Source Name Source
Hemagglutinin Lentil (Lens esculenta) Hemagglutinin, subunit H Hemagglutinin (No. 1) Hemagglutinin, subunit L Hemagglutinin (No. 1) Hirudin Leech Histone F2b Sea urchin (Parechinus angulosus) gonads Histone IIbl Rainbow trout testes Histone F3 Shark erythrocyte Histone F3 Sea urchin Histone F3 Mollusc Histone F3 Cycad Histone F3 Chicken erythrocytes Histone F3 (total) Calf thymus Histone F3 (dimer) Calf thymus Histone F3 (dimer) Duck erythrocytes Histone III Pea embryo Histone III Carp (Letiobus bubalus) testes Histone III Calf thymus Histone IV Calf thymus Histone GAR Rat tumor Histone GAR Pig thymus Histone LS Calf thymus Histone, alanine-rich arginine-rich Calf thymus
* ACTH: adrenocorticotropic
hormone.
487
XII
1 INDEX
23 24
Name Source Name Source
25
Name
26
Source Name
27 28
29 30
31 32
Source Name Source Name Source Name Source Name Source Name Source Name Source
33
Name
34
Source Name
35
Source Name
36
Source Name
37
Source Name
38
Source Name
39 40
Source Name Source Name
Histone ALK Calf thymus Histone ALG Sea urchin (Psammechinus miliaris) gonads Histone, arginine-lysinerich Calf thymus Histone AL, argininelysine-rich Calf thymus Histone Chicken erythrocytes Histone, acid-soluble from natural chromatin Calf thymus Hormone, ACTH* Porcine pituitary Hormone, ACTH Human pituitary Hormone, ACTH Ovine pituitary Hormone, ACTH Bovine pituitary Hormone, choleocystokininpancreozymin Porcine Hormone, chorionic gonadotropin, a-subunit Human placenta Hormone, chorionic gonadotropin, P-subunit Human placenta Hormone, chorionic somatomammotropin LI Human placenta Hormone, chorionic somatomammotropin 1a Monkey placenta Hormone, chorionic somatomammotropin 2” Monkey placenta Hormone, color change Crustacean Hormone, distal-retinal pigment Table
continued
DONALD
488
M. KIRSCHENBAUM
TABLE Source 41
Name Source
42 Name Source
43 Name Source 44 Name 45
Source Name
46
Source Name Source
41 Name 48
Source Name
49
Source Name Source
50
Name Source
51 Name Source
52 Name Source
53 Name Source
54 Name Source
55 Name Source
56 Name Source
Prawn (Pandalus borealis) eye stalk Hormone, follicle-stimulating Ovine pituitary Hormone, follicle-stimulating Ovine pituitary Hormone, follicle-stimulating Ovine pituitary Hormone, folhcle-stimulating Ovine pituitary Hormone, follicle-stimulating Ovine pituitary Hormone, follicle-stimulating, a-subunit Ovine pituitary Hormone, follicle-stimulating, P-subunit Ovine pituitary Hormone, follicle-stimulating Human pituitary Hormone, follicle-stimulating Human pituitary Hormone, follicle-stimulating, u-subunit Human pituitary Hormone, folhcle-stimulating, o-subunit Human pituitary Hormone, follicle-stimulating, p-subunit Human pituitary Hormone, follicle-stimulating, b-subunit Human pituitary Hormone, gastrin I and II* Porcine antra Hormone, gastrin I and II* and “Little” Human antra Hormone, gastrin “Big” Human antra
1 (Continued) 57 Name 58 59 60
61 62 63 64 65 66
Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source Name Source
67 Name Source
68 Name Source
69 Name Source
70 Name Source
71 Name Source
72 Name Source
73 Name Source
74 Name Source
75 Name Source
76 Name Source
77 Name Source
78 Name Source
79 Name Source
Hormone, gastrin I and II* Ovine antra Hormone, gastrin I and II* Bovine antra Hormone, gastrin I and IIb Canine antra Hormone, gastrin I and II* Feline antra Hormone, glucagon Porcine pancreas Hormone, glucagon Rat pancreas Hormone, glucagon Bovine pancreas Hormone, glucagon Rabbit pancreas Hormone, glucagon Human pancreas Hormone, glucagon Camel (Camelus dromedarius) pancreas Hormone, growth Equine pituitary Hormone, growth Human pituitary Hormone, growth Human pituitary Hormone, growth Bovine pituitary Hormone, growth Bovine pituitary Hormone, growth Ovine pituitary Hormone, growth Ovine pituitary Hormone, growth Ovine pituitary Hormone, hyperglycemic Cancer magister eyestalk Hormone, insulin II, alanyl chain Bonito pancreas Hormone, insulin II, glycyl chain Bonito pancreas Hormone, insulin, A chain Fin whale pancreas Hormone, insulin, B chain Fin whale pancreas
AMINO
ACID ANALYSES TABLE
80 Name Source 81 Name Source 82 Name Source 83 Name Source 84 Name Source 85 Name Source 86 Name Source 87 Name Source Name Source 89 Name Source PO Name Source 88
91 Name Source 92
Name Source
93 Name Source 94 Name Source 95 Name Source 96 Name Source 97 Name Source 98 Name Source 99 Name Source 100 Name Source 101 Name Source
Hormone, insulin, A chain Rabbit pancreas Hormone, insulin, B chain Rabbit pancreas Hormone, insulin, A chain Rat 1 pancreas Hormone, insulin, B chain Rat 1 pancreas Hormone, insuiin, A chain Rat 2 pancreas Hormone, insulin, B chain Rat 2 pancreas Hormone, insulin, A chain Mouse (Mus museums) pancreas Hormone, insulin, B chain Mouse (M. museums) pancreas Hormone, insulin Mouse (M. musculus) Hormone, insulin Mouse (M. muse&s) Hormone, insulin Mouse (Black Acomys cahirinus Hoechst) Hormone, insulin Mouse (Yellow A. cahirinus Hoechst) Hormone, insulin Mouse (Yellow A. cahirinus Geneva) Hormone, insulin, A chain Canine pancreas Hormone, insulin, I3 chain Canine pancreas Hormone, insuhn, A chain Sperm whale pancreas Hormone, insulin, B chain Sperm whale pancreas Hormone, insulin, A chain Sei whale pancreas Hormone, insulin, B chain Sei whale pancreas Hormone, insulin, A chain Elephant pancreas Hormone, insulin, B chain Elephant pancreas Hormone, insulin, A chain Caprine pancreas
OF PROTEINS.
489
XII
1 (Conrinued) 102 Source 103 Name Source 104 Name Source 105 Name Source 106 Name Source 107 Name Source Name Source 109 Name Source 110 Name Source 111 Name Source 112 Name Source 113 Name Source 114 Name Source 108
11.5 Name Source 116 Name Source 117 Name Source 118
Name Source
119 Name Source 120
Name Source
121
Name Source
Hormone, insulin, B chain Caprine pancreas Hormone, insulin, A chain Equine pancreas Hormone, insulin, B chain Equine pancreas Hormone, insulin, A chain Duck pancreas Hormone, insulin, B chain Duck pancreas Hormone, ins&n, A chain Rattlesnake (Crotalus arrox) pancreas Hormone, insulin, A chain Cattle pancreas Hormone, insulin, B chain Cattle pancreas Hormone, insulin, A chain Human pancreas Hormone, insulin, B chain Human pancreas Hormone, insulin, A chain Guinea pig pancreas Hormone, insulin, B chain Guinea pig pancreas Hormone, insulin, A chain Coypu (Hystricomorpha) pancreas Hormone, insulin, B chain Coypu (Hystricomorpha) pancreas Hormone, insulin, A chain Fish: bonito, tuna, and swordfish pancreases Hormone, insulin, B chain Fish: bonito, tuna, and swordfish pancreases Hormone, insulin, A chain Cod fish (Gadus callarias) pancreas Hormone, insulin, B chain Cod fish (G. callarias) pancreas Hormone, insulin, A chain Angler fish (Lophius piscatorius) pancreas Hormone, insulin, B chain Angler fish (L. piscaforius) pancreas
-.Table continued
490
DONALD
M. KIRSCHENBAUM
TABLE 122 Name
128
Source Name Source Name Source Name Source Name Source Name Source Name
129
Source Name
130
Source Name
131
Source Name
132
Source Name
133
Source Name
123 124 125 126 127
Source
134 Name Source
135 Name Source
136 Name Source
137 Name Source 138 Name 139 140
Source Name Source Name Source
Hormone, insulin, A chain Ovine pancreas Hormone, insulin, B chain Ovine pancreas Hormone, insulin, A chain Porcine pancreas Hormone, insulin, B chain Porcine pancreas Hormone, light-adapting Shrimp (Pandalus borealis) Hormone, /3-lipotropic Porcine pituitary Hormone, lipotropic (p-lipotropin) Porcine pituitary Hormone, lipotropic (p-lipotropin) Human pituitary Hormone, lipotropic (p-lipotropin) Ovine pituitary Hormone, lipotropic (y-lipotropin) Porcine pituitary Hormone, lipotropic (y-lipotropin) Ovine pituitary Hormone, luteinizing, P-subunit Bovine pituitary Hormone, luteinizing, a-subunit Equine pituitary Hormone, luteinizing, P-subunit Equine pituitary Hormone, luteinizing Equine pituitary Hormone, luteinizing, a-subunit Human pituitary Hormone, luteinizing, P-subunit Human pituitary Hormone, luteinizing, p-subunit Human pituitary Hormone, luteinizing Human pituitary
1 (Conrinued) 141 Name Source
142 Name Source
143 Name Source
144 Name Source
145 Name Source
146 Name Source
147 Name Source
148 Name Source
149 Name Source
150 Name Source
151 Name Source
152 Name Source
153 Name Source
154 Name 155
Source Name Source
156 Name Source
157 Name
Hormone, luteinizing, a-subunit Ovine pituitary Hormone, luteinizing, a-subunit Ovine pituitary Hormone, luteinizing, p-subunit Ovine pituitary Hormone, luteinizing, P-subunit Ovine pituitary Hormone, luteinizing Ovine pituitary Hormone, luteinizing, a-subunit Porcine pituitary Hormone, luteinizing, p-subunit Porcine pituitary Hormone, luteinizing, C-l subunit Rat pituitary Hormone, luteinizing, C-2 subunit Rat pituitary Hormone, luteinizing Rat pituitary Hormone, luteinizing hormone-releasing Porcine hypothalamus Hormone, a-melanocytestimulating Bovine pituitary Hormone, or-melanocytestimulating Porcine pituitary Hormone, cy-melanocytestimulating Equine pituitary Hormone, wmelanocytestimulating Ovine pituitary Hormone, a-melanocytestimulating Dogfish (Squalus acanrhias) pituitary Hormone, wmelanocytestimulating
AMINO
ACID ANALYSES TABLE
Source
158 Name
159
Source Name Source
160 Name Source
161 Name
162
Source Name Source
163 Name Source
164 Name Source 165
Name Source
166
Name Source
167 Name Source
168 Name Source
169 Name Source
170 Name Source
171 Name Source 172
Name Source
Monkey pituitary Hormone, P-melanocytestimulating Human pituitary Hormone, /%melanocytestimulating Bovine pituitary Hormone, P-melanocytestimulating Ovine pituitary Hormone, P-melanocytestimulating Porcine pituitary Hormone, P-melanocytestimulating Equine pituitary Hormone, @melanocytestimulating Monkey pituitary Hormone, P-melanocytestimulating Dogfish (S. acanthias) pituitary Hormone, P-melanocytestimulating Dogfish (Scyliorhinus caniculus) pituitary Hormone, aspartotocin, hormone II’ Dogfish (S. acanthias) neurohypophysis Hormone, glumitocind Ray (Raia batis) neurohypophysis Hormone, glumitocind Ray (R. clavata) neurohypophysis Hormone, glumitocin d Ray (R. naevus) neurohypophysis Hormone, glumitocind Ray (R. fullonica) neurohypophysis Hormone, isotocine Pollack (Pollachius virens) neurohypophysis Hormone, isotocine Hake (Merluccius merluccius) neurohypophysis
OF PROTEINS.
491
XII
1 (Conrinued) 173
Name Source
174 Name Source
175 Name Source 176
Name Source
177
Name Source
178
Name Source
179 Name Source
180 Name Source
181 Name Source
182 Name Source 183
Name Source
184 Name Source
185 Name Source
186 Name Source 187 Name Source
188 Name
Hormone, isotocine Whiting (G. luscus) neurohypophysis Hormone, isotocine Tuna (Germ0 alalunga) neurohypophysis Hormone, isotocine Mackerel (Scomber scombrus) neurohypophysis Hormone, isotocine Cod (G. morrhua) neurohypophysis Hormone, isotocine Carp (Cyprinus carpio) neurohypophysis Hormone, isotocin’ Bony fish (Polypterus bichir) neurohypophysis Hormone, isotocin’ Salmon (Oncorhynchus tschawytscha) neurohypophysis Hormone, mesotocin’ Viper (Vipera aspis) neurohypophysis Hormone, mesotocin’ Frog (Rana esculenta) neurohypophysis Hormone, mesotocinf Chicken (Gallus gallus) neurohypophysis Hormone, mesotocin f Goose (Anser anser) neurohypophysis Hormone, mesotocin’ Turkey (Meleagris gallopavo) neurohypophysis Hormone, mesotocin f Leopard frog (R. pipiens) neurohypophysis Hormone, mesotocinf Toad (Bufo bufo) neurohypophysis Hormone, mesotocinf African lungfish (Protopterus annectens) neurohypophysis Hormone, mesotocinf Table
continued
492
DONALD
M. KIRSCHENBAUM
TABLE Source
African lungfish (Protopterus neurohypophysis Hormone, mesotocin’ Cobra (Naja naja) neurohypophysis Hormone, mesotocinf Elaphid (Elaphe quadrivirgata) neurohypophysis Hormone, ocytocin Bovine neurohypophysis Hormone, ocytocin Porcine neurohypophysis Hormone, ocytocin Human neurohypophysis Hormone, ocytocin Equine neurohypophysis Hormone, ocytocin Finback whale (Balaenoptera physalus) neurohypophysis Hormone, ocytocin Hippopotamus (Hippopotamus amphibus) neurohypophysis Hormone, ocytocin Ovine neurohypophysis Hormone, ocytocin Ratfish (Hydrolagus collei) neurohypophysis Hormone, vasotocing Chicken (G. gallus) neurohypophysis Hormone, vasotocina Goose (A. anser) neurohypophysis Hormone, vasotocinO Turkey (M. gallopavo) neurohypophysis Hormone, vasotocinP Toad (B. bufo) neurohypophysis Hormone, vasotocing Frog (R. esculenta) neurohypophysis Hormone, vasotocin’ Viper (V. aspis) neurohypophysis
1 (Continued) 205
Name Source
206
Name Source
207
Name Source
208
Name Source
209
Name Source
210
Name Source
dolloi)
189 Name Source
190 Name Source
191 Name Source
192 Name Source
193 Name 194 195
1%
197
198
Source Name Source Name Source
Name Source
Name Source Name Source
199 Name Source 200
Name Source
201
Name Source
202
Name Source
203
Name Source
204
Name Source
211 Name Source 212
Name Source
213 Name Source
214 Name Source 215
Name Source
216
Name Source Name Source Name Source Name Source
217 218 219 220
Name Source
221 Name 222
Source Name
Hormone, vasotocin’ Cobra (N. naja) neurohypophysis Hormone, vasotocin” Elaphid (E. quadrivirgata) neurohypophysis Hormone, vasotocin9 Carp (C. carpio) neurohypophysis Hormone, vasotocina Pollack (P. virens) neurohypophysis Hormone, vasotocin9 Whiting (G. luscus) neurohypophysis Hormone, vasotocin’ Salmon (0. tschawytscha) neurohypophysis Hormone, vasotocinP Cod (G. morhua) neurohypophysis Hormone, vasotocin” Mackerel (S. scombrus) neurohypophysis Hormone, vasotocin’ Tuna (G. alalunga) neurohypophysis Hormone, vasotocin’ Bony fish (P. bichir) neurohypophysis Hormone, valitocin” Dogfish (S. acanthias) neurohypophysis Hormone, vasopressin Bovine neurohypophysis Hormone, vasopressin Human neurohypophysis Hormone, vasopressin Equine neurohypophysis Hormone, vasopressin Finback whale (B. physalus) neurohypophysis Hormone, vasopressin Hippopotamus (H. amphibus) neurohypophysis Hormone, vasopressin Ovine neurohypophysis Hormone, vasopressin
AMINO
ACID ANALYSES TABLE
Source
223 Name Source
224 Name Source
225 Name Source
226 Name 227 228 229 230 231 232
Source Name Source Name Source Name Source Name Source Name Source Name Source
233 Name Source
234 Name Source
235 Name 236 237 238 239 240 241 242
Source Name Source Name Source Name Source Name Source Name Source Name Source Name
Mouse (strains CBA/ FACAM and SF/CAM) neurohypophysis Hormone, Lys8-vasopressin Mouse (strain Peru) neurohypophysis Hormone, LyGvasopressin Porcine neurohypophysis Hormone, Lyss-vasopressin Hippopotamus (H. amphibus) neurohypophysis Hormone, parathyroid Human parathyroid Hormone, parathyroid I Bovine parathyroid Hormone, parathyroid II Bovine parathyroid Hormone, parathyroid Porcine parathyroid Hormone, proparathyroid Bovine parathyroid Hormone, polypeptide Chicken pancreas Hormone, red pigmentconcentrating Shrimp (P. borealis) nerve cells Hormone, prolactin Fish (Tilapia mossambica) rostral pars distalis Hormone, prolactin Fish (T. mossambica) caudal adenohypophysis Hormone, prolactin Bovine pituitary Hormone, prolactin Ovine pituitary Hormone, prolactin Porcine pituitary Hormone, prolactin Human pituitary Hormone, prolactin Human amniotic fluid Hormone, prolactin Rat pituitary Hormone, secretin Porcine Hormone, sexual
OF PROTEINS.
493
XII
1 (Conrinued) Source
243 Name Source
244 Name Source
245 Name Source
246 Name Source
247 Name Source
248 Name Source
249 Name Source
250 Name Source
251 Name Source
252 Name Source
253 Name Source
254 Name Source
255 Name Source
256 Name Source
257 Name Source
258 Name Source
259 Name Source
260 Name
Volvox carteri male spheroids Hormone, thyrocalcitonin Bovine Hormone, thyrocalcitonin Chicken ultimobranchial gland Hormone, thyrocalcitonin Eel pericardium and esophagus Hormone, thyrocalcitonin Human C cell tumor Hormone, thyrocalcitonin Porcine thyroid tissue Hormone, thyrocalcitonin Salmon (Oncorhynchus) ultimobranchial gland Hormone, thyrocalcitonin Rat Hormone, thyrocalcitonin Ovine Hormone, thymopoietin II Bovine thymus Hormone, thyrotropic Ovine pituitary Hormone, thyrotropic, a-subunit Human pituitary Hormone, thyrotropic, P-subunit Human pituitary Hormone, thyrotropin, component IV Human pituitary Hormone, thyrotropic, a-subunit Bovine pituitary Hormone, thyrotropic, P-subunit Bovine pituitary Hormone, luteinizingreleasing i Ovine hypothalamus Hormone, luteinizingreleasing Porcine hypothalamus Hormone, melanotropinrelease-inhibiting Table
continued
494
DONALD
M. KIRSCHENBAUM
TABLE Source
261 Name Source 262 Name Source 263 Name Source 264 Name Source 265 Name Source 266 Name Source 261 Name Source 268 Name Source 269 Name Source 270 Name Source 271 Name Source 272 Name Source 273 Name
Source
214 Name Source 275 Name Source
276 Name Source
Rat hypothalamus, stalk median eminence Hormone, melanotropinrelease-inhibiting Bovine hypothalamus Hormone, growth hormone release-inhibiting Ovine hypothalamus Hormone, thyrot~pinreleasing Ovine hypothalamus Hormone, thyrotropinreleasing Porcine hypothalamus Hydrogenase Ciosiridium pasteurianum W5 Hydrogenase 4.2 form Chromatium sp. Hydrogenase 4.4 form Chromatium sp. L-a-Hydroxyacid oxidase, isozyme A Rat liver L-a-Hydroxyacid oxidase, isozyme B Rat liver D-@-Hydroxybutyrate apodehydrogen~e Bovine heart mitochondria p-Hydroxyphenylpyruvate hydroxylase Chicken liver 3&Hydroxysteroid oxidase Brevibacterium sterolicum ~mid~olylacetolphosphate: L-glutamate aminotransferase Salmonella typhimurium Initiation factor-Ml Rabbit reticulocytes Inosine monophosphate dehydrogenase Aerobacter aerogenes Inosine monophosphate dehydrogenase Bacillus subtilis
1 (Continued) 277 Name Source 278 Name Source 279 Name Source 280 Name Source 281 Name Source 282 Name Source 283 Name Source 284 Name Source 285 Name Source 286 Name Source 287 Name Source 288 Name Source 209 Name Source 290 Name Source 291 Name Source 292 Name Source 293 Name Source 294 Name Source 295 Name Source 296 Name Source
Inosine monophosphate dehydrogenase Escherich~a coli Indole-3-glycerolphosphate synthetase E. coli Invertase, external Yeast (Saccharomyces strain FH4C) Invertase, internal Yeast Isocitrate dehydrogenase Yeast Isocitrate dehydrogenase Rhodopseudomonas spheroides Isocitrate dehydrogenase B. stearothermophilus Isocitrate dehydrogenase E. coli Isocitrate dehydrogenase Bovine heart Isocitrate dehydrogenase A. aerogenes Isocitrate dehydrogenase Azotobacter vinelandii Isocitrate dehydrogenase Porcine heart Is&rate lyase Pseudomonas ~ndigofera Isoleucyl-tRNA synthetase (EC 6.1.1.5) E. coli MRE 600 Isoleucyl-tRNA synthetase (EC 6.1.1.5.) E. coli Isoleu~yI-tRNA synthetase (EC 6.1.1.5) E. coli Isomaltase Rabbit small intestine Isomerase S. ~ph~murium Isomeroreductase S. ~phjmurium C-55 Isoprenoid alcohol phosphokinase Staphylococcus aureus
AMINO
ACID ANALYSES TABLE
297 Nume Source
298 Name 299
Source Name
@-Isopropylmalate drogenase
dehy-
OF PROTEINS.
1 (Continued) Source
300 Name
S. typhimurj~m
cu-Isopropylmalate synthase S. typhimurium strain CV123 a-Isopropylmalate synthase
495
XII
Source
301 Name Source
S. ty~him~rium
~-Isopropylm~ate tase
strain CV241 synthe-
Neurospora
ru-Isopropylmalate
synthase
S. typhimurium
o This is also known as placental lactogen. b Form I is not sulfated on the tyrosine phenolic group, while Form II is sulfated; the sequence is the same. o Asn4-ocytocin. d Ser’, Gin*-ocytocin. e Seti, Ilea-ocytocin. f IleE-ocytocin. 9 Args-ocytocin. h VaP-ocytocin. i I have used the name “hormone” for these substances for two reasons. (i) I want to include them in this table with the analyses of the hormones they influence; and (ii) they have been called hypothalamic factors (hormones) by the IUPAC-IUB Commission on Biochemical Nomenclature Recommendations (1974). [(1975) Biochemistry 14,2559-2560.1
10 10 12 6 7 4 10 18 15 10 -1
9 3 2 10 5 4
18 1
30 30 34 19 I8 15 38 53 48 29 0 --
23 9 9 25 11 17 --
52 1
Glycine Alanine Vnline Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x 1O-3 Reference
2
1”
Aminoacid
-
8 1
2 2 1 2 1 2
4 5 4 2 1 2 7 6 5 6 tr* -
3
2
9 0 4 4 2 3 4 4 9 13 6-01 0 3 0 1 1014 2 0 -114 -
4
6
3
4
223 ooo---o---------
tr 0 10 13 11 12 122
_ 5
2 123 18
15
6 10
6
__
12 7 6 6 10 5 15 11 2 123 18 2 4 3
12
8 7 18
7
ANALYSES
7 18
ACID
5 14 3 18 4106666 1 16 247 5.56 6 3 3 6 185 4 11
5
A~UNO
6
2 123 18 2 4 3
12 7 6 6 10 5 15
7 18
9
_ 6
12 7 6 5 10 5 15 1 1 123 18 2 5 3
7 19
10
Residues
7a
-.-If
7 18 6 12 7 6 6 10 5 15 f 2 135 18 2 4 3
11
per
OF PROTEINS,
TABLE
13
17 8
-
17 8
-
17 8
__
2 145 20 2 4 3
14 8 7 8 10 6 15
7 19
14
weight
10 9 20 20 77766 13 13 7 7 7 8 6 7 9 9 6 6 16 I7 2 11 2 2 156 146 19 18 3 2 4 4 3 3
12
molecular
POLYPEPTIDES,
2
9
12 7 5 7 10 5 1.5 11 1 127 17 2 5 2 00 108
7 19
15 7 18
16
910 10
2 119 18 2 4 3
12 7 6 6 10 5 15
of protein
AND PEV~IDES
10” 11
7 18 6 12 7 6 5 10 5 15 2 2 11” 18 2 4 3 0
17 17 7 9 8 6 11 2 7 5 6 0 1 10’2 14 2 2 4 0 4’2 12
18
2 7 5 6 0 I 10’2 14 2 2 4 0 4’2 13
17 7 9 8 6
19
412 14 14
912 14 2 2 4 0
11 7 9 8 6 16 2 7 6 6 0 1
20
14 15
6’3
20 8 3 2 5 o-
14 8 6 10 0 2
7 13 9 6 6
21
14 16
-
12’4 18 2 2 2
5 8 12 0 0
11 6 16 -14 2
14 12 4 1 3 0 11’5 17
fj 5 4
14 17 8 16
23 7 19 6 12 -14 -14 -14
22
8 12
0
9 10
0
Aspartic
Glutamic acid Half-cystine
-
Reference
x 1O-3
MW
18
3
3
Phenylalanine Tyrosine
-
2
Histidine
Tryptophan Amide ammonia
11
24
Arginine
19
0 11” -
12
11
Lysine
14
00
13
Methionine
5
3
Threonine
4
7
6 5
16
8
Serine
acid
6
Isoleucine
-16
16
Leucine
Proline
8
Valine
17
14
16
18
25
24”
Glycine
acid
Alanine
Amino
20
-
-18
0
3
4
12
15
0
0
9 12
5
4
5
6
16
8
17
14
26
8
14
22
-
16
21
-
-
o-
1233 2 3
2311
16
34
8 0
5
6
6
5
4
8
6
13
9
28
1111
5 0
2
5
21
9
5
6
6
23
7
27
23
-
11 1
2
3
4
5 0
2
0
2
4
0
2
3
3
3
29
23
-19
1
2
3
4
5 0
2
0
3
4
0
1
3
3
3
30
25
-20
1 1
3 2
1
3
4
1
5 0
2
0
3
4
0
1
3
3
3
31
26
-
11 2
3 2
11
3
4
13
5 0
2
0
3
4
0
12
3
3
3
27
3.8
321
1 1
3
2
1 0
5
0
5
2
2
1
1
2
33
28
0 823 -22
4
3 4
3
6
3
10
6 9
8
8
7
1
4
7
5
4
34
28
-22
0 924
3
1 2
12
4
1
12
11 9
10
13
22
5
12
12
8
8
35
per molecular
Residues 32
2 (Continued)
TABLE
30
22
1 1925
8
7 11
11
9
6
4
22 25
12
18
5
7
25
7
6
7
36
21
9
8
11
37
32
22
2
6
4 9
8
10
5
4
19 27
10
15
9
-26
weight
32
22
-
2
4
8 10
8
10
5
4
19 25
9
16
8
7
23
9
9
9
38
of protein
33
227
1
0
0 1
0
0
0
0
1 1
0
1
1
0
1
0
0
1
39
11
13 15
1
34
1.9
028
0
0
0 0
1
0
2
0
35
30
4 -29
6
4 6
5
2 12
36
25
1 -28
5
4 5
5
2 9
9
12
11
11
1 2
3
8
2
1 11
6
9 7
7
42
5 11
11
11 8
8
41
6 10
3
1
1
1
2
40
37
32
2 -30
4
5 7
7
3 14
7
28
21
14
15
7 13
16
17 12
13
43
39 continued
Table
33
4 -32
10
6 7
8
4 15
16
17
16
19
12
8 11
9
13 11
9
45
38
23
4 -31
8
5 5
7
3 15
17
15
14
17
11
7 10
7
12 11
8
44
16 39
2 -33
5
4
3
3
9
4
8 8
6
8
5
7
2
2
5
7
4
46
7
2
7
3
40
8
3
25
7 5
5 3
39
11
15
5
19
8
2
0
-
15 23 21
-34
20
8
20 15 11
11 10 9 10
41
33
-35
10
9 6
13
13
19
11
7
7
16
4
10
5
5
6
16 15
11 15
I
11
12
13
15
49
5
Glycine Alanine Valine Leucine Isoleucine Proline Serine Threonine Aspartic acid Glutamic acid Half-cystine Methionine Lysine Arginine Histidine Phenylalanine Tyrosine Tryptophan Amide ammonia MW x IO+ Reference
48
6
47”
Amino acid
-
43
-36
4
4
3 3
6
3
5 9 10
8
8
6
11
7 4
4
4
50
44
10
8=
0
4
4
3 3
6
3
6 9 10
8
8
7
7 4
5
4
51
3
3
738 13
46
1
1 -36 45
8
7
3
5
5 3
7
10 12 1
11 12 1 8
9
13
7
6
5
7
6
7
6
53
9
14
7
5
6
5
6
6
6
52
2 (Continued)
47
-
1
2
1 I
0
0
0
48
1 -39
2 -
49
----_I 50
1
2
0 1 1
1 1 1 2
0
0
0
0
2
112
1 0 0 0 1 1
2
0
0
8
6
5
1 0 0 1
2
0
0
0
1
2
2
57
5 1 0
3
1
2
4
0
1 0 1 0 1 0 0 1
56
6
2
1 0 0 0 1 0 0 1
5.5
2
54
50
1
2
0 1 1
0
0
0
5
1 0 0 1
0
0
1
2
2
58
51
1
2
0 1 1
0
0
2
0
5
1 0 0 1
0
0
0
2
2
59
52
1
2
0 1 1
0
0
1
0
5
1 0 0 1
0
1
0
2
2
60
53
4 -40
I
2
2
1
2
1
1
0
3
4
3
4
0
0
2
1 1 1
61
Residues per molecular weight of protein
TABLE
1
2
54
55
1 1-l ----_ ----___
2 2 222227
1
2
1 1
1 1
3
4
3
4
000004
3
4
3
4
000007
1 1 1 1
63
2 000006
1 1 1
62
56
2
1
2
1 1
3
4
3
4
1 1 1 1
64
57
2
1
2
1 1
3
4
3
4
1 1 1 1
65
58
11
2
1
2
1 1
3
4
3
4
1 1 1 1
66
59
-41
12
3
14
4 10
25
16
8
15
8 17 7 26
67
61
22 -42
1
8
13
3
63
23 -43
1
8
13
3
9
11
11
3
4
27
20
10
18
8
8
26
7
7
8
69
9
3
4
26
20
10
18
8
8
26
7
7
8
68
16
acid
Glutamic
6
1
Phenylalanine
Tyrosine
Tryptophan
x lO-3
Reference
MW
64
-4r -
13
Histidine
ammonia
13 3
13 3
Amide
11
12
Lysine Arginine
66
17 -45
1
6
13
4
4
4
4
Methionine
24
16
12
26
7
Half-cystine
25
acid
Aspartic
13
7 6
Isoleucine Proline
12
24
Leucine
12
6
Valine
Serine
7 6
14
Threonine
10
10
Glycine
Alanine
15
71
acid
70”
Amino
68
16 -46
1
666
13
13 3
11
4
4
24
16
12
13
776 668
27
7
15
9
72
69
-
1
13
13 3
11
4
4
24
16
12
12
26
7
15
9
73
72
-
21
4212
-48 -
70
1220
2
-48
2
-48
-48
7
8
-46
-as
2012 221
5
4
-48
-48
75
1
-47
12
12 3
11
4
4
23
16
12
12
24
7
15
11
74
73
-
-
0
2
1
1
0
2
3
1
0
1
4
20
3
3
76
74
-
-
0
1
0
1
0
4
4
3
0
0
2
0
1
77
0 4
0
0
0
0
4
4
2
1
2
0
2
1
75
-49
1 0
75
2 -50
0
2
3
1 2
1
0
2
3
1
1
1
0 1
4
3
2
3
79
76
-49
4
0
2
0
0 0
0
0
4
4
2
1
2
2 0
2
1
0
1
80
76
-50
2
0
2
3
1 2
1
0
2
3
1
1
1 2
0
4
3
1
3
81
per molecular
Residues 78
2 (Continued)
TABLE
76
-49
4
0
2
0
0 0
0
0
4
3
3
1
2
2 0
2
1
0
1
82
weight
76
-51
1
0
2
3
1 2
2
0
2
3
0
3 1
1
0
4
3
1
3
83
76
4 -50
0
2
0
0 0
0
0
4
3
3
1
2
2 0
2
1
0
1
84
of protein 86
1
128
77
-51 76
00000000 l-------
222--443
20222222 30323333
10111111
10221111
10101-o-
24234655
33367767
0303
1
10221111 228 3
02
42466666
3
1012
31344444
85
77
-
128
2=
0
3
87
77
-
328 228
2
4
88
77
_
3444
328 228
2
4
1111
89
Table
77
_
328 228
2
4
90
continued
77
_
328 228
2
4
91
77
-52
328 228
2
4
92
acid
Glutamic
0
0 0
2
0 4 -49
Arginine
Histidine
Phenylalanine
Tyrosine
Tryptophan
x 1O-3
Reference
MW
76
0
Lysine
ammonia
0
Methionine
Amide
4
Half-cystine
4
1
2
1
Serine
acid
0
Proline
Aspartic
2
Isoleucine
Threonine
1
2
Leucine
1
Valine
1
93a
Alanine
acid
Glycine
Amino
76
0 2 -50
2
2 3
1
1
0
2
3
1
1
1
1
0
4
3
2
3
94
80
0 4 -48
2
0 0
0
0
0
4
4
2
1
2
0
2
2
1
0
1
95
80
-49
-50
80
0 4
2
0 0
0
0
0
4
4
2
1
2
0
1
2
1
1
1
97
0 2
2
2 3
1
1
0
2
3
1
1
1
1
0
4
3
2
3
96
80
0 2 -50
2
2 3
1
1
0
2
3
1
1
1
1
0
4
3
2
3
98
76
0 4 -49
2
0 0 2
76
76
0 4 -49
2 0 2 -50
0 0
0
0
4 0
4
2
0
1
0
1
2
2
1
2
101
2 3
1
1
0 0
2 0
3
1
2
1
1
0
4
3
1
3
100
4 0
4
2
1
1
0
1
2
2
0
2
99
76
0 2 -50
2
2 3
1
1
2 0
3
1
1
1
1
0
4
3
2
3
102
per
Residues
81
0 4 -49
2
0 0
0
0
4 0
2 4
1
1
0
2
2
1
0
2
103
81
0 2 -50
2
2 3
1
1
2 0
3
1
1
1
1
0
4
3
2
3
104
molecular
2 (Continued)
TABLE
82
-53
0 5
2
0 0
0
0
4 0
5
3
0
1
1
1
2
1
0
1
105
weight
82
-50
0 2 -54
83
0 5
2
0
2 2
0 0
0
4 0
5
3
0
1
1
1
2
1
0
1
107
1 2
1
2 0
3
1
1
2
1
4
0
2
3
3
106
of protein
84
0 4 -49
2
0 0
0
0
4 0
4
2
0
2
0
1
2
2
1
1
108
84
0 2 -50
2
2 3
1
1
2 0
3
1
1
1
1
0
4
3
2
3
109
85
0 4 -49
2
0 0
0
0
0
4
4
2
1
2
0
2
2
1
0
1
110
85
0 2 -50
2
3
2
1
1
0
2
3
1
2
1
1
0
4
3
1
3
111
76
0 4 -55
1
0
1
1
0
0
4
3
2
3
1
0
1
1
1
0
2
112
76
0 2 -50
2
3
1
1
1
0
2
2
4
1
3
1
1
3
3
0
2
113
86
6 -13
0
1
0
0
1
0
1
4
2
1 5
2
0
2
1 1
1 0
114
86
3 -56
0
3
2
1
4
0
0
2
2
1 3
3
1
0
3 3
2 0
115
0
1
2
1 0
0
4
acid
acid
Leucine
Isoleucine
Proline
Serine Threonine
Aspartic
Glutamic
x lo-$
Reference
MW
87
0
2
2
87
-
-
0
Tryptophan
ammonia
1
Tyrosine
Amide
1
Phenylalanine
-
1
Histidine
-
1
0
Lysine Arginine
2
0 1
0 1
2
4
Methionine
1
3
0
4
3
Half-cystine
3
3 1
1
Valine
2
3
1
117
0
116”
Alanine
acid
Glycine
Amino
4
88
-49
0
1
1
1
1
0 0
4
2
5
0
1 0
2
1
1
0
1
118
88
2 -50
0
2
2
2
1
1 1
2
1
3
0
3 1
0
4
2
2
3
119
4
89
-49
0
1
1
1
1
0 0
4
3
4
0
1 0
2
1
1
0
1
120
89
2 -50
0
2
2
2
1
0 0
2
1
3
0
1 1
0
4
3
3
3
121
4 90
-49
0
2
0
0
0
0 0
4
4
2
0
0 1
1
2
2
1
2
122
-50
1 1
0 2 2
1
-49
90
90
0 4
2
0
0
90
0 2
2
3
2
1
1
0 0
2 0
3
4 0
4
1
0
2
1
3 4
2
3
125
1 2
0
1
124
91
-57
0 3
0
0
0
1
0
0 2
1
2
1
2
1
1 3
1
1
2
126
92
-58
1 5
3
3
2
4
10
0 2
14
5
3
3
9
5 1
3
15
8
127
per molecular
Residues
0 2 -50
2
3
2
1
0 1
2
3
1
1
1 1
0
4
3
2
3
123
2 (Continued)
TABLE
93
-
1 4
3
3
2
4
10
0 2
14
5
3
3
9
5 1
3
15
8
128
weight
94
-59
1 8
3
3
2
5
9
0 2
11
10
4
4
6
8 2
2
8
11
129
96
-60
1 6
3
3
2
5
10
0 2
16
4
4
5
5
6 2
2
13
8
130
of protein
97
-61
1 1
2
1
1
3
4
0 1
11
3
0
1
8
3 0
1
13
5
131
98
-62
1 2
2
1
1
4
4
0 1
13
2
1
3
4
4 0
1
11
5
132
101
-69
0 3
2
3
3
8
2
12 3
6
5
7
8
20
12 5
8
8
7
133
4
104
-64
-
4
2
4
5
7 1
7
5
7
5
6
4
4 4
5
4
134
continued
Table
-66
108a
1
2
3 2
10
3
1
12
7 7
7
7
16
5
8
11
5
8
138
106
-65
0
4
3 4
3
6
3
10
5 9
8
8
6
1
4
7
4
4
137
104
-64
3
104
-64
-
1
9 3 7
1 3
5
9
2
1 2
13
8
13 9 12
----
-
17 15 4 6
6
7
13
8
9 10
5 6 4
10 13
4 9
136
135
7
8
Serine
Threonine
3
10
Lysine
Arginine
27
109
-
-67
108b
MW
Reference
x lo+
1
Tryptophan Amide ammonia
-68
2-
Tyrosine
10
6
5
1
2
Phenylalanine
8
6
9 5
12
11
13
11
18
6
6
Histidine
Methionine
12 2
Half-cystine
8
7
16
Proline
acid
4
Isoleucine
acid
8
Leucine
Aspartic
11
Valine
Glutamic
7
9
8
5
140
139”
8
acid
Glycine Alanine
Amino
112
-69
-66
5
5
3
3
10
10 4
8
6
9
6
7
2
2
5
7
4
141
-
111
-66
0
5
5
3
3
10
10 4
7
6
9
6
7
2
2
5
7
5
142
115
-70
2
0
2
3
3
8
2
12 3
6
5
7
8
21
5
12
8
8
7
143
111
-71
-66
o-
2
3
3
8
2
12 3
6
5
7
8
20
5
12
8
8
7
144
116
28
-72
7
7
5
9
11
14 5
12
11
13
11
22
6
12
12
12
10
145
119
-13
6
0
5
3
3
3
10
10 4
7
4
9
6
5
2
3
4
8
4
146 8
119
-74
3
4
3
10
9 3
7
7
8
7
7
4
4
4
8
5
4
1
9
1
10 2
6
6
8
9
20
3
11
10
9
7
149
120
16 120
16
2 5 3 o3 -75 -715
3
1
10
0
12 1
3
4
6
10
21
4
13
7
11
148
7
120
31
-15
7
5
12
11
18 4
13
13
15
14
27
7
16
14
15
12
150
1
121
1 -76
1 1” 123
-
1
0
0
0
2
0
0
124
1”
1
1111111111
1
111111
10
0
0
0
0
10
11111111111
0
1
1111111
0
0
0
1111111
0
0
12
153
1”
1
1
0
0
0
0
2
0
0
0
0
154
126
-
of protein
111111 0 0
152
weight
11111
0
10
0
2 0
151
per molecular
Residues 147
2 (Continued)
TABLE
127
1”
1
1
0
0
0
0
2
0
0
0
0
155
128
-
-78
1
1
2
0
0
0
2
2
0
0
0
0
156
-” 129
1 1
1
0
0
0
0
2
13
0
0
0
0
157
2.7 131
066
1
1
2
3
1111
0
3
2
0
12
0
0
0
2 10
158
2.1 132
066
1
1
111
2
0
11
2
0
3
0
0
0
2
159
127
2.1
066
1
1
2
0
2
0
2
3
0
0
0
2 0
160
2.1 133
066
1
1
2
0
2
2
0
1
3
0
0
0
2 0
161
0
0
0
0
0
2
1
0
2
acid
acid
Alanine Valine
Leucine
Isoleucine
Proline
Serine
Threonine
Aspartic
Glutamic
1
1
1
1
066
Histidine
Phenylalanine
Tyrosine
Tryptophan
Amide
Reference
x lo+
134
2.1
2
Arginine
MW
2
Lysine
ammonia
0 1
Half-cystine Methionine
2
2
0
2
Glycine
129
2.1
0%
1
1
1
1
3
1
0 1
2
2
0
1
2
0
0
163
acid
162”
Amino
128
1.9
066
1
1
2
1
1
1
0 0
0
3
0
1
1
0
1
1
0
2
164
128
2.1
066
1
1
1
1
1
2
0 2
0
3
0
0
1
1
0
1 0
3
165
135
1’9
2
0
1
0
0
0
0
2 0
0
2
0
0
1
1
1
0 0
1
166
136, 137
1.0
380
0
1
0
0
0
0
2 0
1
1
0
1
1
1
0
0 0
1
167-170 1
1
138- 142
1.0
28’
0
1
0
0 0
143-
1.0
382
0
1
0
0 0
0
0
0 0
2
1
1
0
0
1
0 2
0
0
2
0
1
0
1
1
0 2
0
0
149
180-190
per molecular
Residues 171-179
2 (Continued)
TABLE
150-
1.0
382
0
1
0
0 0
0
0
2
1
1
0
0
1
1 1
0
0
1
157
191-198
weight
1.0 -ma
382
0
1
0
1 0
0
0
2
1
1
0
0
1
0 1
0
0
1
199-214
of protein
135
1.0
3”
0
1
0
0 0
0
2 0
1
1
0
0
1
1
1 0
0
1
215
1.0 -84b
3”
0
1
1
1 0
0
2 0
1
1
0
0
1
0
0
0 0
1
216-222
1.0 -Sk
0 382
1
1
0 0
1
2 0
1
1
0
0
1
0
0
0 0
1
223-225
Table
164
-
-
0
2
5
5
9
2
0
10
10
1
6
2
10 1
8
7
5
226
166
-
8”
1
1
2
5 4
9
2
0
11
9
1
8
2
8 3
7
7
4
228
continued
165
-
8=
1 1
2
4
5
9
2
0
11
9
0
8
2
8 3
8
7
4
227
229”
8 0
8
acid
acid
Isoleucine
Serine Threonine
Aspartic
Glutamic
41
5
22
19
9
23
11
17
20
4
1
0
1
10
0
Reference
x 1O-3
-
170
-
168
8
171
4
172
0.9
173
-
286 -87
MW
l--
110
P
Tryptophan Amide ammonia
3
0
0
Tyrosine
14
15
7
12
0
0
6
0
121
6=
0 3
12
13
0 1
1 0
12
10
1
173
-88
-87
3
5
7
11
10
6
15
17
9
15
7
24
0
12
12
234
13
11
233
0
1
232
Histidine Phenylalanine
Arginine
12 6
9 5
Lysine
0
2
1
4 0
6
1 2
1
3
3
1
231
11 0
9
9 0
3 24
8
9
42 7
230
Methionine
Half-cystine
1 0
3 2
Leucine
Proline
9
10
Valine
5 6
acid
Alanine
Glycine
Amino
2
174
-
-
8
6
7
11
9
7
6
22
22
9
15
11
11
23=
9
10
11
235
177
23
1899
2
7
6
8
11
9
7
6
22
22
9
15
11
11
23”
10
9
11
236
2--20
178
23
2091
7
6
9
13
9
4
6
24
22
5
16
7
15
26
11
9
8
237
913
29
20
15 9
10
181
-
65604
66714
11 10 77512
101011
181
-
11
10
240
182
-
8
603
28
22
12 6
12
910 24 22
13
11
239
44202
28 6-
19
15 9
9
10
25
12 9
9
238
per
Residues
molecular
2 (Continued)
TABLE
183
-
184
185
-
-95
-95
0
1
2
2
3
495
395
2
0
2 5
2
3
244
186
-
1 0 494 -
2
2
1 11
1
2 10
1
4
4 2
2
0
1 3
1
3
243
of protein
193 28
-93
9
7
13
242
392 -
4
06
311
213
416 212
0
0
19 610
113
2
241
weight
187
-
496
0
0 1
1 1
2
2 0
3
2
4
3
2
0
2 5
1
3
245
189
_
59’
0
1
1 3
0
1
1
2
2
3
5
1
2
1
1 2
2
4
246
190
-
1 5=
1
1 3
2
0
1
2
1
4
4 2
2
0
3
1
1
3
247
192
59’
1 0
0
1
1
2
0
2
3
2
5
4
2
0
5
1
0
3
248
193
597
1 0
2
1
0
1
1
2
2
3
5
2
2
1
3
1
1
4
249
194
494
3 1
I
1
1
1
1
2
1
4
2
4
2
0
3
1
1
3
250
5.6 195
699
0
2
1
0
2
5
0
0
8
4
4
3
2
0
8
6
3
1
251
8
9
7
17
11
16
14 15
Leucine
Isoleucine
Proline
Serine
Threonine
Aspartic Glutamic
3
3
7
5
Arginine Histidine
ammonia
MW x lO-3 Reference
Amide
Tryptophan
Phenylalanine Tyrosine
28 1%
4
10 -
-197
0
4
7
5
13
Lysine
Methionine
9 2
15 5
9
6
8
1
4
7
Half-cystine
acid acid
6
11
Valine
5
5
14
253
11
252”
Alanine
Acid
Glycine
Amino
198
11 o-
4
3
5
7
12 2
9 7
11
5
7
9
6
4
6
4
254
199
200
5 0
5
3
3
10
10 4
6 8
9
6
7
2
2
5
7
4
256
30 _
18
11
8
10
16
21 5
22 23
24
18
17
13
14
15
17
16
255
200
_
11 0
4
3
4
9
12 5
9 7
11
5
7
6
4
6
6
4
257
204
-103
1
1
1
0
1
1
0
0
1 0
0
0
1
1
1 0
0
0
2
258
205
-103
1
10
10
0
10
10
0
0
10 0
0
0
10
1
1 0
0
0
2
259 1
206
*103 -104
0
0
0
0
0
0
1
1 0
0
0
207
0 0 ,103 -104
0
0
0
0 0
0
0 0
0
0
1
1 0
0
0
1
261
207
1 1105
0
3
0
0
0 2
2
0
1
2
1
0
0 0
0
1
1
262
209
-
0 1103
0
0
1
0
0 0
0
1
0
0
0
1
0 0
0
0
0
263
per molecular
Residues 260
2 (Continued)
TABLE
210
-
13
6
58 12
11
12
76
81
24
26
26
38 39
22
37
32
265
59’06 212
24
23
57
14 26
14
101
86
43
48
39
76 48
61
85 120
266
98 213
19 13 -107
of protein
0 11 0 1103 -
0
1
0
0 0
0
1
0
0
0
1
0 0
0
0
0
264
weight
---
5
11
14
7
15
7 25
4
44
33
19
26
0 16
30
23
31
30
268
5
9
14
7
20
6 24
5
38
34
18
24
16
36 0
23
34
25
269
4
9
11
6
15
10 16
6
29
26
18r09
23’09
12
22 11’09
191°9
24
23
270
98’OS 40 40 32 213 214 214 213
-
19 13
24
22
57
15 27
12
101
87
44
45
38
76 50
63
83 132
267
33 217
-
65
9
219
-
16
12 19
20
61
8
9
61
54
37
43
22 40
46
44
43
39
274
continued
218
59
74
6
17
7 0
4 15
33
15
4
13
12 8
6
12
4
13
74
54
15 20
25 34
12 23
24 30
60
44
52
31
273
7 57
17
22
0
23
272
Table
49 216
5 59
17
24
14
19
31
8
57 -109a
22 44
25
19
18
36
27 31
33
271
35
33
30
22
13
19
21
27
acid
acid
Valine
Leucine
Isoleucine
Proline
Serine
Threonine
Aspartic
Glutamic
x 10-s
Reference
MW
Amide
165
221
220
7
93
38
-
25
6
Tyrosine
ammonia
32
8
Histidine Phenylalanine
-
2.5
7
Arginine
Tryptophan
63
19
25
Lysine
47
8
Methionine
14
3
139
105
96
74
62
86
81
111
116
143
216
Half-cystine
41
38
275a
Alanine
acid
Glycine
Amino
-
222
54
8
8
12
8
24
20
8
4
48
32
-110
17 -110
20
33
32
44
40
277
45 223
-
2
14
14
10
21
16
5
6
52
44
13
23
15
22
45
34
55
29
278
224
270
1501”
33
65
80
16
27
60
21
5
115
178
84
114
65
40
83
69
68
71
279
Residues
TABLE
25
135
30
31
77
29
32
85
14
0
124
165
80
151
63
38
77
73
84
115
280
per
40 226
-
3
9
12
9
16
24
5
2
38 31
30
27
18
29
32
27
30
32
281
molecular
2 (Continued)
50 227
-
5
14
17
8
18
26
11
5
38
42
26
18 23
25
35
28
43
42
282
weight
228
93
10 -112
2.5
32
10
37
66
18
101 -
76
4728
2528
41
69
51
63
88
76
283
of protein
80 229
-
-
24
14 23
28
57
8 10
75 84
36
31 34
51
58 66
75
62
284
230
-
-
2
12 9
12
17
26
13
6
43 39
22
19
17
23 26
31
36
32
285
78 231
-
-
-
13
16
23
63
9
3
90
69
39
87
28
30
48
35
80
81
286
80 232
-
7
19
17
13
24
52
8
3
70 61
39
33 42
39
60
42
76
45
287
40
9
233
-
-
12
10
15
26
11
7
37
41
19
19
17
24
32
30
34
32
288
21
158
Tryptophan
Amide
x lo+
-
19
32
102
84
Tyrosine
31
26
235
71
Phenylalanine
234
47
Histidine
61 45
23
14
91
88
46
44
48 47
222
114 94
Lysine Arginine
MW
43
Methionine
ammonia
21
Half-cystine
240
acid
Glutamic
Serine
197
90
Isoleucine Proline
120
83 80
Leucine
acid
59
156 140
Aspartic
93
Threonine
72
176
266
Glycine
Alanine Valine
83
290
acid
289”
Amino
237
114
236
112
33 -
-
30
24
67 44
21
7
83
101
55
55
43 44
83
81
107
82
292
-
25
33
32
25
65 49
25
15
99
99
48
46
49 47
77 80
82 100
291
41
21 46
25 43
12
96
238
100
-
-
114
68
42
48 50
65
50
42
50
293
Residues
TABLE
13
3
7
6
-
239
240
57
6
17
17
8
22
5
33
15
17
56 5
50
22
12
3
33 4
26
29
-
19 24
11 12
28
49
33
57
49
295
15
27
29
27
28
294
per molecular
2 (Continued) weight
17 241
-
4
4
10
3
5
8
4
8 0
8
8
8
4
23
23
11
14
9
296
of protein
70 242
-
17 7
13 22
37
28
15
9
67
22 68
37
42 33
58
33
74
58
297
48
11
243
-
13 13
25
28
9
5
50
23 49
24
25 14
28
31
39
30
298
48
9
243
-
12 13
21
26
11
5
51
21 48
22
22 16
30
28
37
31
299
-
14 66
Table
244
143
-
18
35
22 47
79 71
16
21
140
143
continued
245
48
11
11
13 13
28 2.5
9
5
50
49
23
24
75 82
28 25
31
39
30
301
100 62
94
107
97
300
to Table
2
o!See Table 1 for identification of protein, polypeptide, or peptide. 1 - Not done. 2 tr, Trace. 3 From sequence; plus 1 residue e-N-methyllysine. * Amino acid analyses and a previously suggested sequence may be found in Refs. (7b,c). 5 Includes 1 residue of methyllysine with dimethyllysine predominating; some trimethyllysine detected. 8 Includes 1 residue of methyllysine. ’ Plus 2 residues of methyllysine, with the monomethyl derivative predominating and a small amount of dimethyl derivative. * From sequence; the amide ammonia is distributed as 1 asparagine and 9 glutamine residues. 9 Plus 2 residues of methyllysine. lo From sequence; the amide ammonia is distributed as 1 asparagine and 8 glutamine residues. ” Plus 2 residues of methyllysine. From the sequence; the amide ammonia is distributed as 2 asparagine and 8 glutamine residues. i* Plus 1 residue of methyllysine. From the sequence; the amide ammonia is distributed as 2 asparagine and 2 glutamine residues. There are also 2 acetyl groups present; one is on the N-terminal amino acid. See also Ref. (12b). I3 From sequence; the amide ammonia is distributed as 3 asparagine and 3 glutamine residues. I4 There are 6 or 7 residues of isoleucine, 6 or 7 residues of proline, 4 or 5 residues of serine, 1 or 2 residues of half-cystine and 1 or 2 residues of methyllysine. i5 From sequence; the amide ammonia is distributed as 6 asparagine and 5 glutamine residues. The N-terminus is acetylated.
Footnotes
I6 5 or 6 residues of proline. i7 From sequence; the amide ammonia is distributed as 6 asparegine and 7 glutamine residues. There is an N-terminal acetyl group. is From sequence; there is an N-terminal acetyl group. The same composition is obtained from analysis of 24- and 72-hr hydrolysates. I9 See Ref. (24). 2oSee Ref. (26). *I From sequence: the amide ammonia is distributed as 1 asparagine residue, 1 glutamine residue, and 1 C-terminal amide. One tyrosine exists as a phenolic sulfate ester. 22There are 9 residues of galactose, 9 residues of mannose, 1 residue of fucose, 11 residues of N-acetylglucosamine, 3 residues of N-acetylgalactosamine, and 8 sialic acid residues (29). *3 From sequence; the amide ammonia is distributed as 5 glutamine and 3 asparagine residues. *4 From sequence; the amide ammonia is distributed as 5 glutamine and 4 asparagine residues. 25 From sequence; the amide ammonia is distributed as 7 asparagine and 12 glutamine residues or as 6 asparagine and 12 glutamine residues (31). 266 or 7 residues of isoleucine. 27From sequence; there is 1 asparagine residue and 1 terminal amide. 28Analyses uncorrected for incomplete hydrolysis or destruction during hydrolysis. 29There are 20 or 21 residues of hexoses, 1 residue of fucose, 15 residues of glucosamine, and 5 residues of sialic acid. Galactosamine is absent (35). 3o Carbohydrate content in percentage: total hexose, 9.7; mannose, 3.1; galactose, 3.6; total hexosamine, 4.5; glucosamine, 3.1; galactosamine, 1.4; fucose, 0.6; sialic acid, 5.4.
8 3
g 2 E; s x s g
WI 22
3123,000 is the amino acid portion of the total weight of FSH which is considered to weigh 33,000 (38). 32Carbohydrate content in residues per mole: glucosamine, 14; galactosamine, 2; fucose, 2; mannose, 10; galactose, 5; sialic acid, 6. 3aCarbohydrate content in residues per mole: glucosamine, 7; galactosamine, 1; fucose, 0.4; mannose, 5; galactose, 2; sialic acid, 2. 34Carbohydrate content in residues per mole: glucosamine, 9: galactosamine, 1; fucose, 2; mannose, 5; galactose, 4; sialic acid, 5. 3sAnother amino acid analysis can be found in Ref. (42). 36 From sequence; carbohydrate is present. 3’ From sequence; the amide ammonia is distributed as 4 glutamine and 4 asparagine residues. Amino acid analyses by column chromatographic method can be found in Ref. (46). s8From sequence, the amide ammonia is distributed as 3 glutamine and 4 asparagine residues. Amino acid analysis by column chromatographic method can be found in Ref. (46). ** Zollinger-Ellison tumor fractions analyzed [Gregory, R. A., Tracy, H. J., Agarwal, K. L., and Grossman, M. I. (1969) Gut 10, 603-6081. 40From sequence; the amide ammonia is distributed as 3 glutamine and 1 asparagine residues. From electrophoretic examination of other glucagons it would appear that all have the same number of amide groups (54-58). 41 From sequence; column chromatographic analysis can be found in Ref. (60). 12 From sequence; the amide ammonia is distributed as 9 asparagine and 13 glutamine residues. Column chromato~aphic analysis can be found in Ref. (62). 43 From sequence; the amide ammonia is distributed as 9 asparagine and 14 glutamine residues. 44 Thirty percent of the molecules have leucine replaced by vahne (65). Reported here is the amino acid analysis of the leucine sequence. *5 From sequence; the amide ammonia is distributed as 6 asparagine and 11 glutamine residues. The analysis of the leucine sequence is cited here (see footnote 44). Column chromatographic analyses cited in Ref. (67). * From sequence; the amide ammonia is distributed as 5 asparagine and 11 glutamine residues. 47 Amino acid analyses by column chromatography cited in Ref. (71). 48 Arginine, 3 or 4 residues: threonine, 2 or 3 residues; serine, 4 or 5 residues; glycine, 5 or 6 residues; alanine, 4 or 5 residues; half-cystine, 1 or 2 residues; methionine, 2 or more residues. 4g From sequence; the amide ammonia is distributed as 2 asparagine and 2 glutamine residues. Jo From sequence; the amide ammonia is distributed as 1 asparagine residue and 1 glutamine residue. 51 From sequence; the amide ammonia is distributed as 1 glutamine residue. In Ref. (78) can be found the analysis of insulin from SpragueDawley rat. s2 See Ref. (79) for additional analyses of mouse insulins. 53 From sequence; the amide ammonia is distributed as 3 asparagine and 2 glutamine residues. 54 The data for the p-chain is not correctly described in Ref. (83). 65 From sequence; the amide ammonia is distributed as 3 glutamine and 1 asparagine residues; see also Ref. (86). SeFrom sequence; the amide ammonia is distributed as 1 asparagine and 2 glutamine residues. I7 From sequence; the amide ammonia is distributed as 2 asparagine residues and 1 C-terminal amide. Table continued
s z s E 2
;I E
2 $
b E;
0
Footnotes to Table 2 continued s8 From sequence; the amide ammonia is distributed as 3 ~utamine and 2 asparagine residues. 59 From sequence; the amide ammonia is distributed as 3 glutamine and 5 asparagine residues. See also Ref. (95). W From sequence; the amide ammonia is distributed as 4 glutamine and 2 asparagine residues. See also Refs. (99) and (100) for column chromatographic amino acid analyses and revision of previous structure. E1From sequence; the amide ammonia is assigned to 1 residue of glutamine. OzFrom sequence; the amide ammonia is assigned to 2 residues of glutamine. es From sequence; an N-terminal acyl group is present. The amide ammonia is distributed as 2 glutamine and 1 asparagine residues. Carbohydrate has been reported as follows (values expressed per milligram without correction for moisture and ash). Subunit CI: sugars, totalamount, 152 pg; fucose 0.037 pmol; mannose, 0.46 Kmol; galactose, trace; glucose, trace; N-acetylglucosamine, 0.288 or 0.112 pmol (an error was made in printing and one of these values refers to something else) (102). Subunit CII: sugars, total amount, 109 pg; fucose, 0.060 pmol; mannose, 0.232 pmol; Nacetylglucosamine, 0.191 or 0.120 (an error was made in printing and one of these values refers to something else) (102). Carbohydrate has also been reported as follows (103) in relative numbers of residues and the assumption of 10% moisture. Subunit CI: fucose, 0.4; mannose, 6.8; galactose, 0.1; glucosamine, 5.3; galactosamine, 1.6. Subunit CII: fucose, 0.7; mannose, 2.5; galactose, 0; glucosamine, 3.6; g~actosamine, 1.4. Intact luteinizing hormone; fucose, 1.6; mannose, 8.7; glucosamine, 8.7; galactosamine, 3.6. Amino acid analyses done by column chromatography may be found in Refs. (102) and (103).
61 Carbohydrate reported as grams per 100 g (piven in order of a-subunit, psubunit, and hormone): fucose, 0.34,0.67,0.60; mannose, 5.37,2.62,4.32; galactose, 1.75, 3.65, 3.31; glucosamine, 5.73, 4.82, 4.72; galactosamine, 1.59, 1.64, 2.90; sialic acid, 4.97, 9.47, 7.70 (104). An earlier carbohydrate analysis can be found in Ref. (105). 85 From sequence. Column chromatographic amino acid analyses can be found in Refs. (106) and (107). Carbohydrate analyses (reported as residues per mole assuming 5.0 residues of valine): fucose, 0.5; mannose, 4.3; galactose, 2.2; glucosamine, 7.2; galactosamine, 1.1; sialic acid, 0.2 (107). W From sequence. w From sequence; an N-terminal acyl group is also reported (109). Column chromatographic analyses can be found in Ref. (107). Carbohydrate analysis (reported as residues per mole assuming 9 residues of valine): fucose, 0.6; mannose, 2.0; galactose, 0.9; glucosamine, 3.3; galactosamine, 0.5; sialic acid, 0 (107). W Amino acid analyses were reported for three different times of hydrolysis: 24, 48, and 72 hr. I have taken the 72-hr results for aIJ amino acids, except that the 26hr result was used for threonine, serine, and methionine. The value for tyrosine is 5 or 6 residues. All results are uncorrected for hydrolytic destruction, moisture, and ash. Carbohydrate results, reported as residues per 27,OOOg, are: sialic acid, 1.6; hexoses, 18.1; hexosamine, 7.5. See also Refs. (110) and (111). m Column chromatographic analysis can be found in Refs. (112), (113), and (114). Carbohydrate analyses for subunits A and B prepared by countercurrent distribution and by sulfitolysis and chromatography can be found in Ref. (113). ‘O From sequence; the amide ammonia is distributed as 2 glutamine residues and 1 carbohydrate-blocked asparagine residue. Column chromatographic analysis can be found in Ref. (115).
2 s $
z
k E
” AR N-terminal acyl group is present. 72 Hydrolysis in 6 N HCl for 24 hr. No corrections made for decomposition losses. Carbohydrate: (6hr hydrolysis in 4 N HCl; reported as residues per 28,300 daltons): glucosamine, 7; galactosamine, 3.2. Additional chromatographic analyses may be found in Refs. (117), (118), and (113) and additional carbohydrate results in Ref. (117). t3 From sequence; the amide ammonia is distributed as 2 glutamine and 4 asparagine residues of which 2 asparagine residues have carbohydrate attached. 74From sequence; the amide ammonia is distributed as 2 glutamine and 1 asparagine residues of which 1asparagine has carbohydrate attached. There is an N-terminal acyl group. There is a possible form with 1 arginine residue replaced by a glutamyl residue. r5 Carbohydrate (reported as residues per mole in the order C-t, C-2, intact hormone): giucosamine, 8, 4, 13; galactosamine 1, 1, 3; galactose, I, I, 2; mannose, 3, 2, 6; fucose, 1, 1, 2. 78 From sequence. See Ref. (122) for column chromatographic analysis. 77 From sequence. There is an N-terminal acyl group and the amide is C-terminal. See Ref. (125). 78 Some 50% of the molecules are C-terminal amidated. A tyrosyl dogfish hormone is mentioned here; it has 1 tyrosine residue in addition to the other residues of the a-MSH (130). From sequence. rB From sequence; amide ammonia is distributed as an asparagine residue and a C-terminal glycine amide. so From sequence; the amide ammonia is distributed as 1 asparagine residue, 1 glutamine residue, and 1 C-terminal glycine amide. *I From sequence; the amide ammonia is distributed as 1 asparagine residue and 1 C-terminal glycine amide. Table
continued
8ZFrom sequence; the amide ammonia is distributed as 1 asparagine residue, 1 glutamine residue, and 1 C-terminal glycine amide. *3 From enzymatic hydrolysis and from sequence; the amide ammonia is distributed as 5 glutamine residues and 3 asparagine residues (165,166). Amino acid analyses of interest can be found in Ref. (167). BdFrom enzymatic digestion (169) and sequence (168); the amide ammonia is distributed as 5 glutamine residues and 3 asparagine residues. 84itReferences (139,140,142-145,147,149,158-1~). WJ References (152-156,161,162). ** References (155,162,163). 85 From sequence; the amide ammonia is distributed as 3 glutamine residues, 2 asparagine residues, and 1 C-terminal amide. SfiFrom sequence; the amide ammonia is distributed as 1 asparagine residue and 1 C-terminal amide. a1 Uncorrected for hydrolytic destruction; results calculated on basis of 196 residues per mole, excluding tryptophan. BBThis preparation contains carbohydrate. 89 In the amino acid content, Ref. (175) reports one less leucine residue in the sequence. Column chromatographic analysis can be found in Ref. (176). e0 From sequence; the amide ammonia is distributed as 11 asparagine residues and 7 glutamine residues. Although 22 leucine residues are reported in Ref. (177), the correct number is 23 residues (178). 111From sequence; the amide ammonia is distributed as 12 asparagine residues and 8 glutamine residues. Column chromatographic analysis can be found in Refs. (178-180). 92 From sequence; the amide ammonia is distributed as 2 glutamine residues and 1 C-terminal amide.
Ln z
% 9 3 ffZ p x E
5 g v,
ki?
b F3
Liz
$2
to Table
2 continued
s3Results based on 2 residues of histidine per 15,000 MW. There are 8 or 9 arginine residues, and the presence of tryptophan is questionable. Carbohydrate analysis gave the fobllowing results (in percentages): arabinose, 6.6; xylose, 25.5; mannose, 15.6; galactose, 4.4; glucose, 32.5; acetylglucosamine, 3.9; unknown peak, 11.3. s4 From sequence; the amide ammonia is dist~buted as 3 asparagine residues and I C-terminal amide. g5Aspartic acid; 1 or 2 residues; tyrosine, 0 or 1 residue; serine and threonine values not corrected for losses during hydrolysis. BBFrom sequence: amide ammonia is distributed as 1 asparagine residue, 2 glutamine residues, and 1 C-terminal amide. Column chromatographic analyses can be found in Ref. (188). *’ Prom sequence; amide ammonia is dist~buted as 2 asparagine residues, 2 glutamine residues, and t C-terminal amide. s8 From sequence; amide ammonia is dist~buted as 4 asparagine residues and I C-terminal amide, In Ref. (191) the structure of porcine calcitonin-I is reported. The analysis is exactly the same as No. 247. O9From sequence; the amide ammonia is distributed as 4 glutamine and 2 asparagine residues. There is an error on p. 362 of Ref. (19.5) in the paragraph “amino acid composition of TPII:” 4 proline residues are reported as present in the sequence but there are only 2 residues. loo No correction made for moisture or ash. Values adjusted to 14.4 residues of aspartic acid which has been rounded off to I4 residues; 3.3 residues of glucosamine and 1.0 residue of galactosamine present. lo* From sequence; column chromatographic analysis can be found in Ref. (197).
Fooinotes
lo2 From sequence; amino acid analyses and carbohydrate analyses can also be found in Refs. (202) and (203). Carbohydrate analyses from Ref. (201): a-subunit, p-subunit (residues per molecule): fucose, 0.3, 0.9; mannose, 5.8, 2.5; galactose, 0.2, 0; glucosamine, 6.4,3.1; galactosamine, 2.5, 1.5. rM From sequence; there is a C-terminal amide. See Ref. (211). lo4 A recent report states that this is inactive (208). ‘05 From sequence; there is 1 asparaghte residue. *06This molecular weight includes 12 atoms of iron and sulfur. lo7 There are 3.7 atoms of iron and 4.0 atoms of sulfide in 4.2 form. ‘OSThere are 3.6 atoms of iron and 3.9 atoms of sulfide in 4.4 form. log These values have not been corrected for low recoveries due to degradation or nonrelease during hydrolysis. rosa3 half-cystine residues found upon amino acid analysis, and 4 residues found by pCMB titration. Ilo Threonine, 24 or 2.5 residues; serine, 19-21 residues. ‘I* 38 residues of glucosamine. rl* In addition to these results from a 20-hr hydrolysate the results of a 22-hr hydrolysate are also reported in Ref. (228). ‘I3 Following reported as residues per 100,000 MW: glucosamine (as N-acetyl derivative), 21; galactosamine (as N-acetyi derivative), 4; glucose, 3; fucose, 5; mannose, 6, galactose, 6 (238). ‘I* From sequence. Column chromatographic amino acid analyses may be found in Refs. (246-248). There is one sulfite group attached to a tyrosine residue.
!iL
!2
13 3 6 s: jr; 9 g
AMINO
ACID ANALYSES
REFERENCES
OF PROTEINS.
XII
513
FOR TABLE 2
1. Fliegerova, O., Salvetova, A., Ticha, M., and Kocourek, J. (1974) B&him. Biophys. Acta 351, 416-426. 2. Petersen, T. E., Roberts, H. R., Sottrup-Jensen, L., and Magnusson, S. (1976) Protides Biol. Fluids 23, 145- 149. 3. Strickland, W. N., Strickland, M., Brandt, W. F., Morgan, M., and Von Holt, C. (1974) FEES Lett. 40, 161-166. 4. Bailey, G. S., and Dixon, G. H. (1973) J. Biol. Chem. 248, 5463-5472. 5. Brandt, W. F., Strickland, W. N., and Von Holt, C. (1974) FEES Lett. 40, 349-352. 6. Brandt, W. F., Strickland, W. N., Morgan, M., and Von Holt, C. (1974) FEES Lett. 40, 167-172. 7. (a) Brandt, W. F., and Von Holt, C. (1974) Eur. J. Biochem. 46, 419; (b) (1971) FEES Lett. 14, 338-340; (c) (1972) FEES Lett. 23, 357-360. 8. Marzluff, Jr., W. F., Sanders, L. A., Miller, D. M.. and McCarthy, K. S. (1972) J. Biol.
Chem.
247, 2026-2033.
9. Patthy. L., Smith, E. L., and Johnson, J. (1973) J. Biol. Chem. 248, 6834-6840. 10. Hooper, J. A., Smith, E. L., Sommer, K. R., and Chalkley, R. (1973) J. Biol. Chem. 248,
3275-3279.
11. De Lange, R. J., Hooper, J. A., and Smith, E. L. (1973) J. Biol. Chem. 248, 3261-3274. 12. (a) De Lange, R. J., Fambrough, D. M., Smith, E. L., and Bonner, J. (1969) J. Bid. Chem. 244, 319-334; (b) Ogawa, Y., Quagliarotti, G., Jordan, J., Taylor, C. W., Starbuck, W. C., and Busch, H. (1969) J. Biol. Chem. 244, 4387-4392. 13. Sautiere, P.. Tyrou, D., Moschetto, Y., and Biserte, G. (1971) Biochimie 53, 479-483. 14. Sautiere, P., Lambelin-Breynaert, M. D., Moschetto, Y., and Biserte, G. (1971) Biochimie 53, 711-715. 15. Ishikawa, K., Hayashi, H., and Iwai, K. (1972) J. Biochem. (Tokyo) 72, 299-326. 16. Yokotsuka, K., Kikuchi, A., and Shimura, K. (1972) J. Biochem. (Tokyo) 71, 133-146. 17. Sautiere, P., Tyrou, D., Laine, B., Mizon, J., Ruffin, P., and Biserte, G. (1974) Eur. J. Biochem. 41, 563-576. 18. Wouters-Tyrou, D., Sautiere, P., and Biserte, G. (1974) Biochim. Biophys. Acta 342, 360-366.
19. Yeoman, L. C., Olson, M. 0. J., Sugano, N., Jordan, J., Taylor, C. W., Starbuck, W. C., and Busch, H. (1972) J. Biol. Chem. 247, 6018-6023. 20. Sautiere, P., Tyrou, D., Laine, B., Mizon, J., Lambelin-Breynaert, M. D., Ruffin, P., and Biserte, G. (1972) C’. R. Acad. Sci. Paris 274D, 1422-1425. 21. Champagne, M., Pouyet, J., Ouellet, L.. and Garel, A. (1970) Bull. Sot. Chim. Bioj. 52, 377-390. 22.
23. 24. 25. 26.
27. 28. 29. 30. 31. 32. 33. 34.
Sonnenbichler, J., and Nobis, P. C. (1970) Eur. J. Biochem. 16, 60-65. Graf, L., Bajusz, S., Patthy, A., Barat, E., and Cseh, C. (1971) Acta Biochim. Biophys. 6, 415-418. Riniker, B., Sieber, P., Rittel, W., and Zuber, H. (1972) Nature New Biol. 235, 114- 116. Johl, A., Riniker, B., and Schenkel-Hulliger, L. (1974) FEES Lett. 45, 172-174. Li. C. H. (1972) Biochem. Biophys. Res. Commun. 49, 835-839. Mutt, V., and Jorpes, J. E. (1971) Biochem. J. 125, 57p-58~. Morgan, F. J., Birken, S., and Canfield, R. E. (1975) J. Biol. Chem. 250, 5247-5258. Bahl, 0. P. (1969) J. Biol. Chem. 244, 567-574. Li, C. H., Dixon, J. S., and Chung, D. (1973) Arch. Biochem. Biophys. 155, 95- 110. Niall, N. D., Hogan, M. L., Tregear, G. W., Segre, G. V., Hwang, P., and Friesen, H. (1973) Rec. Progr. Harm. Res. 29, 387-416. Shome, B., and Friesen, H. G. (1971) Endocrinology 89, 631-641. Fernlund, P., and Josefsson, L. (1972) Science 177, 173-175. Femlund, P. (1971) Biochim. Biophys. Acta 237, 519-529.
514
DONALD
M. KIRSCHENBAUM
35. De La Llosa, P., Hermier, C., De La Llosa, P., and Jutisz, M. (1965) Bull. Sot. Chim. Biol. 47, 1073- 1078. 36. Papkoff, H., Gospodarowicz, D., and Li, C. H. (1967) Arch. Biochem. Biophys. 120,434-439.
37. Cahill, C. L., Shetlar, M. R., Payne, R. W., Endecott, B., and Li, Y. T. (1968) Biochim. Biophys.
Acta
154, 40-52.
38. Sherwood, 0. D., Grimek, H. J., and McShan, W. H. (1970) J. Biol. Chem. 245, 2328-2336. 39. Grimek, H. J., and McShan, W. H. (1974) J. Biol. Chem. 249, 5725-5732. 40. Papkoff, H., Mahlmann, L. J., and Li, C. H. (1967) Biochemistry 6, 3976-3982. 41. Saxena, B. B., and Rathnam, P. (1971) J. Biol. Chem. 246, 3549-3554. 42. Amir, S. M., and Parlow, A. F. (1972) Proc. Sot. Exp. Biol. Med. 139, 1120-1122. 43. Shome, B., and Parlow, A. F. (1974) J. Clin. Endocrinol. Metabol. 39, 199-202. 44. Rathnam, P., and Saxena, B. B. (1975) .I. Biol. Chem. 250, 6735-6746. 45. Shome, B., and Parlow, A. F. (1974) J. Clin. Endocrinol. Metabol. 39, 203-205. 46. Saxena, B. B., and Rathnam, P. (1976) J. Biol. Chem. 251, 993-1005. 47. Gregory, H., Hardy, P. M., Jones, D. S., Kenner, G. W., and Sheppard, R. C. (1964) Nature (London) 204,93 l-933. 48. Bentley, P. H., Kenner, G. W., and Sheppard, R. C. (1966) Nature (London) 209, 583-585. 49. Gregory, R. A., and Tracy, H. J. (1973) Mt. Sinai J. Med. 40, 359-364. 50. Agarwal, K. L., Beacham, J., Bentley, P. H., Gregory, R. A., Kenner, G. W., Sheppard, R. C., and Tracy, H. J. (1968) Nature (London) 219, 614-615. 51. Agarwal, K. L., Kenner, G. W., and Sheppard, R. C. (1969) Experientia 25,346-348. 52. Agarwal, K. L., Kenner, G. W., and Sheppard, R. C. (1969) J. Amer. Chem. Sot. 91, 3096-3097.
53. (a) Bromer, W. W., Staub, A., Diller, E. R., Bird, H. L., Sinn, L. G., and Behrens, 0. K. (1957) J. Amer. Chem. Sot. 79, 2794-2798; (b) Bromer, W. W., Sinn, L. G., and Behrens, 0. K. (1957) J. Amer. Chem. Sot. 79, 2807-2810. 54. Sundby, F., and Markussen, J. (1971) Horm. Metabol. Res. 3, 184-187. 55. Bromer, W. W., Boucher, M. E., and Koffenberger, J. E., Jr. (1971) J. Biol. Chem. 246, 2822-2827. 56. Sundby, F., and Markussen, J. (1972) Harm. Metabol. Res. 4, 56. 57. Thomsen, J., Kristiansen, K., and Brunfeldt, K. (1972) FEBS Lett. 21, 315-319. 58. Sundby, F., Markussen, J., and Danko, W. (1974) Horm. Metabol. Res. 6, 425. 59. Zakin, M. M., Paskus, E., Dellacha, J. M., Paladini, A. C., and Santome, J. A. (1973) FEBS Left. 34, 353-355. 60. Conde, R. D., Paladini, A. C., Santome, J. A., and Dellacha, J. M. (1973) Eur.
J. Biochem.
32, 563-568.
61. Li, C. H., and Dixon, J. S. (1971) Arch. Biochem. Biophys. 146, 233-236. 62. (a) Dixon, J. S., and Li, C. H. (1962) J. Gen. Physiol. Suppl. 45, 169-178; (b) Meisinger, M. A. P., Cirillo, V. J., Davis, G. E., and Reisfeld, R. A. (1964) Nature (London) 201, 820-821; (c) Bewley, T. A., Brovetto-Cruz, J., and Li, C. H. (1969)
Biochemistry
8, 4701-4708.
63. Niall, H. D., Hogan, M. L., Tregear, G. W., Segre, G. V., Hwang, P., and Friesen, H. (1973) Rec. Progr. Horm. Res. 29, 387-416. 64. Santome, J. A., Dellacha, J. M., Paladini, A. C., Wolfenstein, C. E. M., Pena, C., Poskus, E., Daurat, S. T., Biscoglio, M. J., De Sese, Z. M. M., and De Sanguesa, A. V. F. (1971) FEBS Lett. 16, 198-200. 65. Daurat, S. T., Femandez, H. N., Dellacha, J. M., Paladini, A. C., and Santome, J. A. (1970) 6th Nat. Meet. Sot. Arg. Inves. Bioquim., abstract P 39; cited in Ref. (64). 66. Wallis, M. (1973) FEBS Lett. 35, 11-14.
AMINO
ACID ANALYSES
OF PROTEINS.
XII
51.5
67. (a) Parcells, A. J. (1961) Nature (London) 192, 971-972; (b) Glaser, C. B., and Li, C. H. (1974) Biochemistry 13, 1044-1047. 68. Li, C. H., Gordon, D., and Knorr, J. (1973) Arch. Biochem. Biophys. 156, 493-508. 69. Fernandez, H. N., Pena, C., Poskus, E., Biscoglio, M. J., Paladini, A. C., Dellacha, J. M., and Santome, J. A. (1972) FEBS Lett. 25, 265-270. 70. Bellair, J. T. (1972) Biochem. Biophys. Res. Commun. 46, 1128-1134. 71. Dellacha, J. M., Enero, M. A., Santome, J. A., and Paladini, A. C. (1970) Eur. J. Biochem.
72. 73. 74. 75. 76. 77. 78. 79. 80. 81. 82. 83. 84. 85. 86. 87. 88. 89. 90. 91. 92. 93. 94. 95. 96. 97. 98. 99. 100. 101. 102.
12, 289-295.
Kleinholz, L. H. (1975) Nature (London) 258, 256-257. Kotaki, A. (1962) J. Biochem. (Tokyo) 51, 301-309. Kotahi, A. (1963) J. Biochem. (Tokyo) 53, 61-70. Hama, H., Titani, K., Sakaki, S., and Narita. K. (1964) J. Biochem. (Tokyo) 56, 285-293. Smith, L. F. (1966) Amer. J. Med. 40, 662-666. Bunzli, H. F., and Humbel, R. E. (1972) Hoppe-Seyler’s Z. Physiol. Chem. 353, 444-450. Steiner, D. F., Clark, J. L., Nolan, C., Rubenstein, A. H., Margoliash, E., Aten, B., and Oyer, P. E. (1969) Rec. Progr. Norm. Res. 25, 207-282. Markussen, J. (1971) Int. J. Protein Res. 3, 149-155. Ishihara, Y., Saito, T., Ito, Y., and Fujino, M. (1958) Nature(London) 181, 1468-1469. Harris, J. I., Sanger, F., and Naughton, M. A. (1956) Arch. Biochem. Biophys. 65, 427-438. Markussen, J., and Sundby, F. (1973) Int. J. Protein Res. 5, 37-48. Vensel, W. H., Pollock, H. G., and Kimmel, J. R. (1974) Fed. Proc. 33, Abstract No. 413. (a) Sanger, F., and Tuppy, H. (1951) Biochem. J. 49, 463-481, 481-490; (b) Sanger, F., and Thompson, E. 0. P. (1953) Biochem. J. 53, 353-366, 366-374. Nicol, D. S. H. W., and Smith, L. F. (1960) Nature (London) 187, 483-485. Smith, L. F. (1972) Diabetes 21, 457-460. Neumann, P., and Humbel, R. E. (1969) Int. J. Protein Res. 1, 125-140. Reid, K. B. M., Grant, P. T., and Youngson, A. (1968) Biochem. J. 110, 289-296. Neumann, P. A., Koldenhof, M., and Humbel, R. E. (1969) Hoppe-Seyler’s Z. Physiol. Chem. 350, 1286- 1288. Brown, H., Sanger, F., and Kitai, R. (1953) Biochem. J. 60, 556-565. Fernlund, P. (1976) Biochim. Biophys. Acta 439, 17-25. Graf, L., Barat, E., Cseh, C., and Sajgo, M. (1971) Biochim. Biophys. Acta 229, 276-278. Gilardeau, C., and Chretien, M. (1972) in Chemistry and Biology of Peptides (Meienhofer, J., ed.), pp. 609-611. Ann Arbor Science, Ann Arbor, Mich. Li, C. H., and Chung, D. (1976) Nature (London) 260, 622-624. Chretien, M., Gilardeau, C., Seidah, N., and Lis, M. (1976) Canad. J. Biochem. 54, 778-782. Graf, L., and Li, C. H. (1973) Biochem. Biophys. Res. Commun. 53, 1304-1309. Graf, L., Cseh, G., and Sajgo, M. (1971) in Polypeptide Hormones (Goth, E., and Forenyi, J., eds.), pp., 185-189. Akademiai Kiado, Budapest. Chretien, M., and Li, C. H. (1967) Canad. J. Biochem. 45, 1163-1174. Li, C. H., Barnafi, L., Chretien, M., and Chung, D. (1965) Nature (London) 208, 1093-1094. Chretien, M., Gilardeau, C., and Li, C. H. (1972) Int. J. Peptide Protein Res. 4, 263-265. Maghuin-Rogister, G., and Hennen, G. (1973) Eur. J. Biochem. 39, 235-253. Hennen, G., Maghuin-Rogister, G., and Mamoir, G. (1970) FEBS Lett. 9, 20-26.
516
DONALD
M. KIRSCHENBAUM
103. Pierce, J. G., Liao, T. H., Howard, S. M., Shome, B., and Cornell, J. S. (1971) Rec. Progr. Horm. Res. 27, 165-212. 104. Landefeld, T. D., and McShan, W. H. (1974) Biochemistry 13, 1389-1393. 105. Landefeld, T. D., Grimek, H. J., and McShan, W. H. (1972) Biochem. Biophys. Res. Commun. 46, 463-469. 106. Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem. Biophys. Res. Commun. 48, 530-537.
107. Hartree, A. S., Thomas. M., Braikevitch, M., Bell, E. T., Christie, D. W., Spaull, G. V., Taylor, R., and Pierce, J. G. (1971) J. Endocrinol. 51, 169-180. 108. (a) Shome, B., and Parlow, A. F. (1973) Fed. Proc. 32, 281, abstract No. 372; (b) Closset, J., Henner, G., and Lequim, R. M. (1973) FEBS Lerr. 29, 97-100. 109. Rathnam, P., and Saxena, B. B. (1970) J. Biol. Chem. 245, 3725-3731. 110. Rathnam, P., and Saxena, B. B. (1971) J. Biol. Chem. 246, 7087-7094. 111. Ward, D. N., Reichert, L. E., Liu, W-K., Nahm, H. S., Hsia, J., Lamkin, W. M., and Jones, N. S. (1973) Rec. Progr. Horm. Res. 29, 533-561. 112. Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Arch. Biochem. Biophys. 153, 554-572.
113. Lamkin, W. M., Fujino, M., Mayfield, J. D., Holcomb, G. H., and Ward, D. N. (1970) Biochim. Biophys. Acta 214, 290-298. 114. Sairam, M. R., and Li, C. H. (1974) Arch. Biochem. Biophys. 165, 709-714. 115. Sairam, M. R., Samy, T. S. A., Papkoff, H., and Li, C. H. (1972) Arch. Biochem. Biophys. 153, 572-586. 116. Gospodarowicz, D. (1972) J. Biol. Chem. 247, 6491-6498. 117. Papkoff, H., Gospodarowicz, D., Candiotti, A., and Li, C. H. (1965) Arch. Biochem. Biophys. 111, 431-438. 118. Ward, D. N., Walborg, E. F., and Adams-Mayne, M. (1961) Biochim. Biophys. Acta 50, 224-232.
119. Maghuin-Rogister,
G., Combamous,
Y., and Hennen, G. (1973) Eur. J. Biochem.
39, 255-263.
120. Ward, D. N., Reichert, L. E., Jr., Fitach, B. A., Nahm, H. S., Sweeney, C. M., and Neill, J. D. (1971) Biochemistry 10, 1796-1802. 121. Matsuo, H., Baba, Y., Nair, R. M. G., Arimura, A., and Schally, A. V. (1971) Biochem. Biophys. Res. Commun. 43, 1334-1339. 122. Schally, A. V., Nair, R. M. G., Redding, T. W., and Arimura, A. (1971) J. Biol. Chem. 246, 7230-7236. 123. Lo, T. B., Dixon, J. S., and Li, C. H. (1961) Biochim. Biophys. Acra 53, 584-586. 124. Harris, J. I., and Lerner, A. B. (1957) Nature (London) 179, 1346-1347. 125. Harris, J. I. (1959) Biochem. J. 71, 451-459. 126. Dixon, J. S., and Li, C. H. (1960) J. Amer. Chem. Sot. 82, 4568-4572. 127. Lee, T. H., Lerner, A. B., and Buettner-Janusch, V. (1963) Biochim. Biophys. Acta 71, 706-709. 128. Lowry, P. J., Bennett, H. P. J., McMartin, C., and Scott, A. P. (1974) Biochem. J. 141,439-444.
129. Lee, T. N., Lerner, A. B., and Buettner-Janusch, V., (1961) J. Biol. Chem. 236, 1390-1394. 130. Lowry, P. J., and Chadwick, A. (1970) Biochem. J. 118, 713-718. 131. Harris, J. I. (1959) Nature (London) 184, 167-169. 132. Geschwind, I. I., Li, C. H., and Barnafi, L. (1957) J. Amer. Chem. Sot. 79, 1003- 1004. 133. (a) Harris, J. I., and Roos, P. (1956) Nature (London) 178, 90; (b) Geschwind, I. I., Li, C. H., and Barna8, L. (1957) J. Amer. Chem. Sot. 79, 620-625.
AMINO
ACID
ANALYSES
OF PROTEINS.
517
XII
134. Dixon, J. S., and Li, C. H. (1961) Gen. Camp. Endocrinol. 1, 161-169. 135. Acher, R., Chauvet, J., and Chauvet, M. T. (1972) Eur. J. Biochem. 29, 12-19. 136. Chauvet, J., Chauvet, M. T., Beaupain, D., and Acher, R. (1965) C. R. Acad. Sci. Paris
261, 4234-4236.
137. Acher, R., Chauvet, J., and Chauvet, M. T. (1967) Nature (London) 216, 1037-1038. 138. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1962) B&him. Biophys. Acta
58, 624-625.
139. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1968) Gen. Camp. Endocrinol. 11, 535-538.
140. Acher, R., Chauvet, J., Chauvet. M. T., and Crepy, D. (1965) Comp. Physiol.
Biochem.
14, 245-254.
141. Acher, R., Chauvet, J., and Chauvet, M. T. (1970) FEB.9 Lerr. 11, 332-335. 142. Wilson, N., and Smith, M. (1969) Gen. Comp. Endocrinol. 13, 412-424. 143. Acher, R., Chauvet. J., and Chauvet, M. T. (1968) Biochim. Biophys. Acra 154, 255-257. 144. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1964) Biochim. Biophys. Acra 90, 613-615. 145. Acher, R., Chauvet, J., and Chauvet, M. T. (1970) Eur. J. Biochim. 17, 509-513. 146. Acher, R., Chauvet, J., and Chauvet, M. T. (1969) Nature (London) 221, 759-760. 147. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1967) Gen. Camp. Endocrinol.
8, 337-343.
148. Acher, R., Chauvet, J., and Chauvet, M. T. (1970) Nature (London) 227, 186-187. 149. Acher, R., Chauvet, J., and Chauvet, M. T. (1969) Gen. Camp. Endocrinol. 13, 357-360. 150. (a) Du Vigneaud, V., Ressler, C., and Trippett, S. (1953) J. Biol. Chem. 205, 949-957; (b) Tuppy, H., and Michl, H. (1953) Monarsh. Chemie 84, 1011-1020. 151. Pierce, J. G., Gordon, S., and Du Vigneaud, V. (1952) J. Biol. Chem. 199, 929-940. 152. Light, A., and Du Vigneaud, V. (1958) Proc. Sot. Exp. Biol. Med. 98, 692-696. 153. Acher, R., Chauvet, J., and Lenci, M. T. (1958) Bull. Sot. Chim. Biol. 40, 2005-2018. 154. Acher, R., Chauvet, J., and Chauvet. M. T. (1964) Nature (London) 201, 191-192. 155. Ferguson, D. R., and Pickering, B. T. (1969) Gen. Camp. Endocrinol. 13, 425-429. 156. Acher, R., Chauvet, J., and Lenci, M. T. (1959) C. R. Acad. Sci. 248, 1435-1438. 157. Pickering, B. T.. and Heller, H. (1969) J. Endocrinol. 45, 597-606. 158. Acher, R., Chauvet, J., Lenci, M. T., Morel, F., and Maetz, J. (1960)Biochim. Biophys. Acfa
42, 379-380.
159. Heller, H.. and Pickering, B. T. (1961) J. Physiol. 155, 98-114. 160. Acher, R., Chauvet, J., Chauvet, M. T., and Crepy, D. (1961) Biochim. Acra
Biophys.
51, 419-420.
161. (a) Du Vigneaud, V., Lawler, H. C., and Popenoe, E. A. (1953) J. Amer. Chem. Sot. 75, 4880-4881; (b) Acher, R., and Chauvet, J. (1953) Biochim. Biophys. Acra 12, 487-488. 162. Stewart, A. D. (1968) J. Endocrinol. 44, XIX-XX. 163. Popenoe, E. A., Lawler, H. C., and Du Vigneaud, V. (1952) J. Amer. Chem. Sot. 74, 3713. 164. Keutmann, H. T., Barling, P. M., Hendy, G. N., Segre, G. V., Niall, H. D., Aurbach, G. D., Potts, J. T.. and O’Riordan, J. L. H. (1974) Biochemistry 13, 1646-1652.
165. Niall, H. D.. Keutmann, H., Sauer, Potts, J., Jr. (1970) Hoppe-Seyler’s 166. Keutmann, H. T., Aurbach, G. D., Potts, J. T., Jr. (1971) Biochemistry
R., Hogan, M., Dawson, B., Aurbach, 2. Physiol.
Chem.
351,
G., and
1586-1588.
Dawson, B. F., Niall, H. D., Deftos, L. J., and 10, 2779-2787.
518
DONALD
M. KIRSCHENBAUM
167. Tashjian, A., Ontjes, D., and Munson, P. L. (1964) Biochemistry 3, 1175-1182. 168. Sauer, R. T., Niall, H. D., Hogan, M. L., Keutmann, H. T., O’Riordan, J. L. H., and Potts, J. T., Jr. (1974) Biochemistry 13, 1994-1999. 169. Woodhead, J. S., O’Riordan, J. L. H., Keutmann, H. T., Stoltz, M. L., Dawson, B. F., Niall, H. D., Robinson, C. J., and Potts, J. T., Jr. (1971) Biochemistry 10,2787-2792. 170. Hamilton, J. W., Niah, H. D., Keutmann, H. T., Potts, J. T., Jr., and Cohn, D. V. (1973) Fed. Proc. 32, 269, abstract No. 315. 171. Kimmel, J. R., Hayden, L. J., and Pollock, H. G. (1975) J. Biol. Chem. 250, 9369-9376.
172. Fernlund, P. (1974) Biochim. Biophys. Acta 371, 304-311. 173. Farmer, S. W., Clarke, W. C., Papkoff, H., Nishioka, R. S., Bern, H. A., and Li, C. H. (1975) Life Sci. 16, 149-158. 174. Wallis, M. (1974) FEBS Lett. 44, 205-208. 175. Graf, L. (1971) in Polypeptide Hormones (Goth, E., and Forenyi, J., eds.), pp. 255-262, Akademiai Kiado, Budapest. 176. Yudaev, N. A., Pankov, Y. A., Elizarova, G. P., Han, Z., and Nikolaeva, 0. P. (1975) Bioorg. Chem. 1, 97-112. 177. Li, C. H., Dixon, J. S., Lo, T. B., Schmidt, K. D., and Pankov, Y. A. (1970) Arch. 178.
Biochem. Biophys. 141, 705-737. Li, C. H. (1976) Znt. J. Peptide Protein Res. 8, 205-224. Eppstein, S. (1964) Nature (London) 202, 899-900. Clarke, W. C., and Li, C. H. (1974)Arch. Biochem. Biophys.
179. 180. 181. Hwang, P., Murray, Biochemistry
161, 313-318.
J. B., Jacobs, J. W., Niall, H. D., and Friesen, H. (1974)
13, 2354-2358.
182. Ellis, S., Grindeland,
R. E., Nuenke, J. M., and Callahan, P. X. (1969) Endocrinology
85, 886-894.
183. 184. 185. 186. 187. 188. 189. 190. 191. 192.
Mutt, V., Jorpes, J. E., and Magnusson, S. (1970) Eur. J. Biochem. 15, 513-519. Starr, R. C., and Jaenicke, L. (1974) Proc. Nat. Acad. Sci. USA 71, 1050-1054. Brewer, H. B., Jr., and Ronan, R. (1969) Proc. Nat. Acad. Sci. USA 63, 940-947. Nieto, A., Moya, F., and Candela, J. L. R. (1973) Biochim. Biophys. Acra 322, 383-391. Noda, T., and Narita, K. (1976) J. Biochem. (Tokyo) 79, 353-359. Otani, M., Yamauchi, H., Meguro, T., Kitazawa, S., Watanabe, S., and Orimo, H. (1976) J. Biochem. (Tokyo) 79, 345-352. Neher, R., Riniker, B., Rittel, W., and Zuber, H. (1968) Helv. Chim. Acta 51, 1900-1905. Potts, J. T., Jr., Niall, H. D., Keutmann, H. T., Brewer, H. B., and Deftos, L. J. (1968) Proc. Nat. Acad. Sci. USA 59, 1320-1328. Barg, W., Jr., Englert, M. E., Davies, M. C., Colucci, D. F., Snedeker, E. H., Dziobkowski, C., and Bell, P. H. (1970) Biochemistry 9, 1671-1676. Niall, H. D., Keutmann, H. T., Copp, D. H., and Potts, J. T., Jr. (1969) Proc. Nat. Acad.
Sci.
USA
64, 771-778.
193. Raulais, D., Hagaman, J., Ontjes, D. A., Lundblad, R. L., and Kingdon, H. S. (1976) Eur. J. Biochem. 64, 607-611. 194. Sauer, R., Niall, H. D., and Potts, J. T., Jr. (1970) Fed. Proc. 29,728 abstract No. 2723. 195. Schlesinger, D. H., and Goldstein, G. (1975) Cell 5, 361-365. 196. Pierce, J. G., and Wynston, L. L. (1960) Biochim. Biophys. Acta 43, 538-540. 197. Sairam, M. R., and Li, C. H. (1973) Biochem. Biophys. Res. Commun. 51, 336-342. 198. Sairam, M. R., and Li, C. H. (1973) Biochem. Biophys. Res. Commun. 54, 426-431. 199. Roos, P., Jacobson, G., and Wide, L. (1975) Biochim. Biophys. Acra 379, 247-261. 200. Liao, T. H., and Pierce, J. G. (1971) J. Biol. Chem. 246, 850-865. 201. Pierce, J. G. (1971) Endocrinology 89, 1331-1344.
AMINO
ACID ANALYSES
OF PROTEINS.
519
XII
202. Hennen, G., Maghuin-Rogister, G., and Mamoir, G. (1970) FEBS Lett. 9, 20-26. 203. Carsten, M. E., and Pierce, J. G. (1960) J. Biol. Chem. 235, 78-84. 204. Burgus, R., Butcher, M., Amoss, M., Ling, N., Monahan, M., Rivier, J., Fellows, R., Blackwell, R., Vale, W., and Guillemin, R. C. (1972) Proc. Nat. Acad. Sci. USA 69, 278-282. 205.
Baba, Y., Matsuo, H., and Schally, A. V. (1971) Biochem.
Biophys.
Res.
Commun.
44, 459-468.
Celis, M. E., Taleisnik, S., and Walter, R. (1971) Proc. Nat. Acad. Sci. USA 68, 1428- 1433. 207. Nair, R. M. G., Kastin, A. J., and Schally, A. V. (1971) Biochem. Biophys. Res. Commun. 43, 1376- 1381. 208. Grant, N. H., Clark, D. E., and Rosanoff (1973) Biochem. Biophys. Res. Commun. 51, lOO- 106. 209. Brazeau, P., Vale, W., Burugs, R., Ling, N., Butcher, M.. Rivier, J., and Guillemin
206.
(1973)
Science
179, 77-79.
210. Burgus, R., Dunn, T. F., Desiderio, D., and Guillemin, Paris
269D,
R. (1969) C. R. Acad.
Sci.
1870-1873.
211. Nair, R. M. G., Barrett, J. F., Bowers, C. Y., and Schally, A. V. (1970) Biochemistry 9, 1103-1106. 212. Chen, J. S., and Mortenson, E. (1974) B&him. Biophys. Acta 371, 283-298. 213. Gitlitz, P. H., and Krasna, A. I. (1970) Biochemistry 14, 2564-2568. 214. Duley, J. A., and Holmes, R. S. (1976) Eur. J. Biochem. 63, 163-173. 215. Bock, H. G., and Fleischer, S. (1975)J. Biol. Chem. 250, 5774-5781. 216. Wada, G. H., Fellman, J. H., Fujita, T. S., and Roth, E. S. (1975) J. Biol. Chem. 250, 6720-6726.
217. 218. 219. 220. 221.
Uwajima, T., Yagi, H., and Terada, 0. (1974) Agr. Biol. Chem. 38, 1149-I 153. Martin, R. G., Voll, M. J., and Appella, E. (1967)J. Biol. Chem. 242, 1175-1181. Merrick. W. C.. and Anderson, W. F. (1975)J. Biol. Chem. 250, 1197-1206. Heyde, E., and Morrison, J. F. (1976) Biochim. Biophys. Acra 429, 635-644. Yokosawa, H., Tobita, T., and Yamada, T. (1971) Biochim. Biophys. Acta 227,
222.
Krishnaiah, K. V. (1975) Arch. Biochem. Biophys. 170, 567-575. Creighton, T. E., and Yanofsky, C. (1966) J. Biol. Chem. 241, 4616-4624. Neumann, N. P., and Lampen, J. 0. (1967) Biochemisfry 6,468-475. Gascon, S., Neumann, N. P., and Lampen, J. 0. (1968)J. Biol. Chem. 243, 1573- 1577. Illingworth, J. A. (1972) Biochem. J. 129, 1119-1124. Buzdygon, B. E.. Braginski, J. E., and Chung, A. E. (1973) Arch. Biochem. Biophys.
538-553.
223. 224. 225. 226.
227.
159, 400-408.
228. Howard, R. L., and Becker, R. R. (197O)J. Biol. Chem. 245, 3186-3194. 229. Reeves, H. C., Daumy, G. O., Lin, C. C., and Houston. M. (1972) Biochim. Biophys.
Acta
258, 27-39.
230. Fan, C. C., and Plaut, G. W. E. (1974) J. Biol. Chem. 249, 4839-4845. 231. Barrera, C. R., and Jurtshuk. P. (1970) Biochim. Biophys. Acta 220, 416-429. 232. Chung, A. E.. and Franzen, J. S. (1969) Biochemisfry 8, 3175-3184. 233. Shen, W. C., Mauck, L., and Colman, R. F. (1974) J. Biol. Chem. 249, 7942-7949. 234. Shiio, I., Shiio, T., and McFadden, B. A. (1965) Biochim. Biophys. Acta 96, 114- 122. 235. Durekovic, A., Flossdorf, J., and Kula, M. R. (1973) Eur. J. Biochem. 36, 528-533. 236. Baldwin, A., and Berg, P. (1966) J. Biol. Chem. 241, 831-838. 237. Piszkiewicz. D., and Goitein. R. K. (1974) Biochemistry 13, 2505-2511. 238. Cogoli, A., Eberle, A., Sigrist, H., Joss, C., Robinson, E., Mosimann, H., and Semenza, G. (1973) Eur. J. Biochem. 33, 40-48. 239. Margolies, M. N., and Goldberger, R. F. (1967) J. Biol. Chem. 242, 256-264.
520
DONALD
M. KIRSCHENBAUM
240. Hofler, J. G., Decedue, C. J., Luginbuhl, G. H., Reynolds, J. A., and Burns, R. 0. (1975) J. Bid. Chem. 250, 877-882. 241. Sandermann, H., Jr., and Strominger, J. L. (1971) Proc. Nat. Acad. Sci. USA 68, 2441-2443. 242. Parsons, S. J., and Burns, R. 0. (1969) J. Eiol. Chem. 244, 996- 1003. 243. Bartholemew, J. C., and Calve, J. M. (1971) Biochim. Biophys. Acta 250, 568-576. 244. Webster, R. E., and Nelson, C. A., and Gross, S. R. (1965) Biochemistry 4,2319-2327. 245. Bartholomew, J. C., and Calvo, J. M. (1971) Biochim. Biophys. Acta 250, 577-587. 246. Bagdy, D., Barabas, E., and Graf, L. (1973) Thromb. Res. 2, 229-238. 247. Markwardt, F., and Walsmann, P. (1967) Hoppe-Seyler’s Z. Physiol. Chem. 348, 1381-1386. 248. De La Llosa, P., Tertrin, C., and Jutisz, M. (1963) Bull. Sot. Chim. Biol. 45, 69-74.
