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. 1983 Mar;9(3):315-29.

[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]

[Article in Russian]
  • PMID: 6385998

[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]

[Article in Russian]
Iu B Alakhov et al. Bioorg Khim. 1983 Mar.

Abstract

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.

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