[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].
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.
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003488:Cyanogen Bromide; D010450:Endopeptidases / Q000494:pharmacology*; D004926:Escherichia coli / Q000235:genetics*; D006868:Hydrolysis; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis*
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D010450:Endopeptidases; C042769:Staphylococcus aureus glutamic protease; D003488:Cyanogen Bromide
Pervichnaia struktura faktora élongatsii G iz Escherichia coli. VII. Issledovanie peptidov, poluchennykh pri gidrolize fragmenta T4 glutaminovoĭ proteinazoĭ Staphylococcus aureus.