[Primary structure of the elongation factor G from Escherichia coli. VI. Structure of peptides of cyanogen bromide cleavage of the G-factor molecule]. / Pervichnaia struktura faktora élongatsii G iz Escherichia coli. VI. Struktura peptidov bromtsianovogo rasshchepleniia molekuly G-faktora.

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.

[Primary structure of the elongation factor G from Escherichia coli. VII. Study of peptides generated during hydrolysis of the T4 fragment by glutamic proteinase from Staphylococcus aureus]. / Pervichnaia struktura faktora élongatsii G iz Escherichia coli. VII. Issledovanie peptidov, poluchennykh pri gidrolize fragmenta T4 glutaminovoi proteinazoi Staphylococcus aureus.

For fragment T4, obtained on limited trypsinolysis of the G-factor, the amino acid sequence embracing 76% of its structure has been determined by analysis of peptides resulting from the fragment T4 cleavage with staphylococcal glutamic protease. These data permitted to assemble into one polypeptide chain 7 out of 12 earlier characterized cyanogen bromide peptides contained in the fragment T4.

[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]. / Pervichnaia struktura faktora élongatsii G iz Escherichia coli. VIII. Issledovanie struktury peptidov tripticheskogo gidroliza, vkhodiashchikh v sostav fragmenta T4 ogranichennogo tripsinolizata G-faktora.

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.

[Primary structure of the elongation factor G from Escherichia coli. IX. Structure of peptides generated by cyanogen bromide cleavage of the G-factor isolated on thiol-activated sepharose and of the products of the G-factor cleavage at Asp-Pro bonds. Complete primary structure]. / Pervichnaia struktura faktora élongatsii G iz Escherichia coli. IX. Issledovanie struktury peptidov bromtsianovogo rasshchepleniia G faktora, vydelennykh na tiol-aktivirovannoi sefaroze, i produktov rasshepleniia G-faktora po sviaziam Asp-Pro. Polnaia pervichnaia struktura.

The amino acid sequence of cysteine- and cystine-containing peptides resulting from cleavage of the G-factor by cyanogen bromide has been determined. For structure analysis cyanogen bromide peptides were further degradated using trypsin, chymotrypsin, thermolysin, staphylococcal glutamic protease, or limited acid hydrolysis. The products of the G-factor cleavage at Asp-Pro bonds were also studied. The obtained data together with those published earlier permitted to establish the complete primary structure of the elongation factor G. The polypeptide chain consists of 701 amino acid residues and has molecular mass of 77321,46.