[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]

Autor:	Iu A, Ovchinnikov, Iu B, Alakhov, Iu P, Bundulis, M A, Bundule, L M, Vinokurov
Rok vydání:	1983
Předmět:	Hydrolysis Sulfhydryl Reagents Chromatography Gel Escherichia coli Amino Acid Sequence Cyanogen Bromide Chromatography Agarose Peptide Elongation Factor G Peptide Elongation Factors Chromatography High Pressure Liquid Peptide Fragments
Zdroj:	Bioorganicheskaia khimiia. 9(3)
ISSN:	0132-3423
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::224e88b3cae5de46e5366991aef22b1d https://pubmed.ncbi.nlm.nih.gov/6386000 Zobrazit plný text záznamu