PMID: 16637283Apr 28, 2006Paper

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

Bioorganicheskaia khimiia
O M AnikinaI Iu Filippova

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.

References

Apr 20, 1967·Biochemical and Biophysical Research Communications·I Schechter, A Berger
Mar 1, 1995·Protein Science : a Publication of the Protein Society·J J Perona, C S Craik
Mar 1, 1996·International Journal of Peptide and Protein Research·J D MeyerM C Manning
Dec 9, 2003·The Plant Cell·Nina V ChichkovaAndrey B Vartapetian

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