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Published February 1949 | public
Journal Article

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.

Additional Information

© 1949 American Society for Biochemistry and Molecular Biology. (Received for publication, August 16, 1948) From the Gates and Crellin Laboratories of Chemistry, California Institute of Technology, Pasadena, Contribution No. 1236.

Additional details

Created:
August 19, 2023
Modified:
October 23, 2023