title: [Primary structure of the elongation factor G from Escherichia coli. V. Amino acid sequence of the C-terminal domain].
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.
mesh_terms: D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000235:genetics*; D006868:Hydrolysis; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000032:analysis*
chemical_list: D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors
vernacular_title: Pervichnaia struktura faktora élongatsii G iz Escherichia coli. V. Aminokislotnaia posledovatel'nost' C-kontsevogo domena.