[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].
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.
D000595:Amino Acid Sequence; D002847:Chromatography, Agarose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D004926:Escherichia coli / Q000235:genetics*; D006868:Hydrolysis; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*; D013439:Sulfhydryl Reagents
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D013439:Sulfhydryl Reagents; D003488:Cyanogen Bromide
Pervichnaia struktura faktora élongatsii G iz Escherichia coli. IX. Issledovanie struktury peptidov bromtsianovogo rasshchepleniia G faktora, vydelennykh na tiol-aktivirovannoĭ sefaroze, i produktov rasshepleniia G-faktora po sviaziam Asp-Pro. Polnaia pervichnaia struktura.