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[Native and modified subtilisin Karlsberg as an effective catalyst of peptide bond formation in organic media].

作者信息

Anikina O M, Semashko T A, Oksenoĭt E S, Lysogorskaia E N, Filippova I Iu

出版信息

Bioorg Khim. 2006 Mar-Apr;32(2):130-6. doi: 10.1134/s1068162006020026.

DOI:10.1134/s1068162006020026
PMID:16637283
Abstract

The activity and stability of native subtilisin Karlsberg and subtilisin 72 and their complexes with sodium dodecyl sulfate (SDS) in organic solvents were studied. The kinetic constants of the hydrolysis of specific chromogenic peptide substrates Z- ALA-Ala-Leu-pNA and Glp-Ala-Ala-Leu-pNA by the subtilisins were determined. It was found that the subtilisin Karlsberg complex with SDS in anhydrous organic solvents is an effective catalyst of peptide synthesis with multifunctional amino acids in positions P1 and P'1 (Glu, Arg, and Asp) containing unprotected side ionogenic groups.

摘要

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