[Primary structure of the elongation factor G from Escherichia coli. VIII. Structure of tryptic peptides comprising the T4 fragment of limited trypsinolysis of the G-factor].
Products of tryptic hydrolysis of the maleic anhydride modified fragment Th3 from limited thermolytic hydrolysis of the G-factor have been studied. Some short peptides which result from the trypsin action on the native G-factor molecule and belong to the fragment T4 obtained on limited trypsinolysis of the G-factor have been separated and their structure has been studied. As a result amino acid sequence has been determined by tryptic peptides containing 322 amino acid residues of the fragment T4 which makes up about 94% of its polypeptide chain.
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D006868:Hydrolysis; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D014357:Trypsin
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D014357:Trypsin
Pervichnaia struktura faktora élongatsii G iz Escherichia coli. VIII. Issledovanie struktury peptidov tripticheskogo gidroliza, vkhodiashchikh v sostav fragmenta T4 ogranichennogo tripsinolizata G-faktora.