406
Biochimica et Biophysica Acta,
485 (1977) 406--416 © Elsevier/North-Holland Biomedical Press
BBA 68282
PURIFICATION OF AN ACID PROTEINASE FROM ASPERGILLUS SAITOI AND DETERMINATION OF PEPTIDE BOND SPECIFICITY
NORIO TANAKA,
MICHIO TAKEUCHI
and EIJI ICHISHIMA *
Laboratory of Enzymology and Microbial Chemistry, Tokyo Noko University, Fuchu, Tokyo 183 (Japan) (Received April 21st, 1977)
Summary The specificity and mode of action of an acid proteinase ** (EC 3.4.23.6) from Aspergillus saitoi were investigated with oxidized B-chain of insulin, angiotensin II and bradykinin. Further purification of acid proteinase was performed with N, O-dibenzyloxycarbonyl-tyrosine hexamethylene
Biochimica et Biophysica Acta,
485 (1977) 406--416 © Elsevier/North-Holland Biomedical Press
BBA 68282
PURIFICATION OF AN ACID PROTEINASE FROM ASPERGILLUS SAITOI AND DETERMINATION OF PEPTIDE BOND SPECIFICITY
NORIO TANAKA,
MICHIO TAKEUCHI
and EIJI ICHISHIMA *
Laboratory of Enzymology and Microbial Chemistry, Tokyo Noko University, Fuchu, Tokyo 183 (Japan) (Received April 21st, 1977)
Summary The specificity and mode of action of an acid proteinase ** (EC 3.4.23.6) from Aspergillus saitoi were investigated with oxidized B-chain of insulin, angiotensin II and bradykinin. Further purification of acid proteinase was performed with N, O-dibenzyloxycarbonyl-tyrosine hexamethylene
