[Primary structure of the elongation factor G from Escherichia coli. VI. Structure of peptides of cyanogen bromide cleavage of the G-factor molecule].
Iu B Alakhov, M A Bundule, Iu P Bundulis, Vinokurov Lm, Kozlov Vp
Abstract
Iu B Alakhov, M A Bundule, Iu P Bundulis, Vinokurov Lm, Kozlov Vp
Abstract
Peptides obtained as a result of cyanogen bromide cleavage of the G-factor have been studied. All 12 peptides embracing the whole structure of fragment T4 have been isolated. For their amino acid sequence determination, cyanogen bromide peptides have been further cleaved with trypsin, chymotrypsin, thermolysin, staphylococcal glutamic protease and BNPS-skatole. The complete primary structure of 9 from 12 cyanogen bromide peptides has been determined.
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Peptides obtained as a result of cyanogen bromide cleavage of the G-factor have been studied. All 12 peptides embracing the whole structure of fragment T4 have been isolated. For their amino acid sequence determination, cyanogen bromide peptides have been further cleaved with trypsin, chymotrypsin, thermolysin, staphylococcal glutamic protease and BNPS-skatole. The complete primary structure of 9 from 12 cyanogen bromide peptides has been determined.
Key concepts: Cyanogen bromide, Thermolysin, Chemistry, Cyanogen, Protein primary structure, Cleavage (geology), Trypsin, Chymotrypsin