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
Alakhov, I.B.; Bundule, M.A.; Bundulis, I.P.; Vinokurov, L.M.; Kozlov, V.P.
Bioorganicheskaia Khimiia 9(3): 330-342
1983
ISSN/ISBN: 0132-3423 PMID: 6385999 Document Number: 197511
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.