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[Primary structure of the elongation factor G from Escherichia coli. V. Amino acid sequence of the C-terminal domain].

作者信息

Alakhov Iu B, Vinokurov L M, Dovgas N V, Motuz L P

出版信息

Bioorg Khim. 1983 Mar;9(3):293-303.

PMID:6385996
Abstract

The amino acid sequence of the C-terminal domain of the elongation factor G (EF-G) has been studied. The polypeptide chain of the domain consists of 228 amino acid residues, and contains no tryptophan or cysteine residues. To determine its structure, the peptides obtained as a result of the fragment digestion by staphylococcal glutamic protease, cyanogen bromide cleavage, and tryptic hydrolysis of the fragment modified by maleic anhydride have been analyzed, as well as peptides obtained after hydrolyses of cyanogen bromide fragments with chymotrypsin, thermolysin and trypsin.

摘要

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