400
Biochimica et Biophysica Acta, 577 (1979) 400--409
© Elsevier/North-Holland Biomedical Press
BBA 38162 COMPARATIVE STUDY BETWEEN P R O K A R Y O T E S AND E U K A R Y O T E S BY CHEMICAL IODINATION OF RIBOSOMAL PROTEINS
C. BERNABEU, D. V/kZQUEZ and F.P. CONDE Instituto de Bioqu[mica de MacromoMculas, Centro de Biolog{a Molecular, C.S.I.C. and U.A.M. Canto Blanco, Madrid-34 (Spain)
(Received July 14th, 1978) (Revised manuscript received October 16th, 1978)
Key words: Ribosomal protein; Lactoperoxidase; Iodination
Summary Escherichia coli and S a c c h a r o m y c e s cerevisiae ribosomal proteins were chemically iodinated with 12sI by chloramine T under conditions in which the proteins were denatured. The labelled proteins were subsequently separated by two-dimensional gel electrophoresis with an excess of untreated ribosomal proteins from the same species. The iodination did not change the electrophoretic mobility of the proteins as shown by the pattern of spots in the stained gel slabs and their autoradiography. The 12sI radioactivity incorporated in the proteins was estimated by cutting o u t the gel spots from the two
Biochimica et Biophysica Acta, 577 (1979) 400--409
© Elsevier/North-Holland Biomedical Press
BBA 38162 COMPARATIVE STUDY BETWEEN P R O K A R Y O T E S AND E U K A R Y O T E S BY CHEMICAL IODINATION OF RIBOSOMAL PROTEINS
C. BERNABEU, D. V/kZQUEZ and F.P. CONDE Instituto de Bioqu[mica de MacromoMculas, Centro de Biolog{a Molecular, C.S.I.C. and U.A.M. Canto Blanco, Madrid-34 (Spain)
(Received July 14th, 1978) (Revised manuscript received October 16th, 1978)
Key words: Ribosomal protein; Lactoperoxidase; Iodination
Summary Escherichia coli and S a c c h a r o m y c e s cerevisiae ribosomal proteins were chemically iodinated with 12sI by chloramine T under conditions in which the proteins were denatured. The labelled proteins were subsequently separated by two-dimensional gel electrophoresis with an excess of untreated ribosomal proteins from the same species. The iodination did not change the electrophoretic mobility of the proteins as shown by the pattern of spots in the stained gel slabs and their autoradiography. The 12sI radioactivity incorporated in the proteins was estimated by cutting o u t the gel spots from the two
