The hydrolysis of N-benzoyl-DL-tyrosylglycinamide, N-acetyl-L-tyrosylglycinamide, and N-acetyl-DL-tyrosylglycinamide by chymotrypsin

Abstract

Contrary to the report of Bergmann and Fruton (1) the L peptide present in aqueous solutions of N-benzoyl-DL-tyrosylglycinamide, prepared by two independent methods, is rapidly hydrolyzed by crystalline chymotrypsin. At 40° and pH 7.8 in a 0.00344 M solution of the DL mixture the L component is hydrolyzed as rapidly as in a 0.00172 M solution of the L peptide (Table I). Because of the relative insolubility of N-benzoyl-DL-tyrosylglycinamide, it was not possible to study the reaction at higher substrate concentrations, and attention was directed to the much more soluble N-acetyl-DL-tyrosylglycinamide.

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