Affiliation:
1. Department of Chemistry, Moscow State University, 117234, Moscow, Russia
Abstract
Calf chymosin was shown to catalyse peptide synthesis optimally over the range pH 4-5, giving satisfactory yields of methyl esters or p-nitroanilides of benzyloxycarbonyl tetra- to hexa-peptides, provided that hydrophobic amino-acid residues form the new peptide bonds. The effectiveness of the enzyme depends also on the nature of adjacent amino-acid residues. As an aspartate-proteinase with a characteristic specificity pattern chymosin would be useful for the synthesis of middle-length peptides.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
8 articles.
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