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  • Title: Thiolsubtilisin as an instrument for peptide synthesis. Preparation and properties.
    Author: Kolobanova SV, Lysogorskaya EN, Filippova IYu, Anisimova VV, Oksenoit ES, Stepanov VM.
    Journal: Biochemistry (Mosc); 1997 Mar; 62(3):329-36. PubMed ID: 9275305.
    Abstract:
    A convenient procedure for thiolsubtilisin purification from an admixture of subtilisin involving affinity chromatography on bacitracin-Sepharose is presented. Thiolsubtilisin activity was measured by hydrolysis of p-nitrophenyl acetate, p-nitroanilide-peptide (Glp-Ala-Ala-Leu-pNA), and azocasein. The thiolenzyme catalyzes peptide synthesis. Under these conditions only activated peptide esters, e.g., p-chlorophenyl, N-hydroxysuccinimide, or p-nitrophenyl esters form peptide bonds during interaction with appropriate nucleophiles such as peptides and their derivatives and amino acid amides.
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