The Mode of Action of Trypsin upon Synthetic Poly-ε-aminocaproyl-α-Alanines*

Abstract

In previous papers (1, 2) we reported that the synthetic linear polymers, poly-ε-aminocaproyl-α-alanines, can be partly hydrolysed by the action of trypsin if relatively high concentrations of the enzyme are employed. This finding is important in connection to the problem of substrate specificity of trypsin. The present study was undertaken to identify the products of tryptic hydrolysis of poly-ε-aminocaproyl-α-alanines and to examine the behavior of trypsin upon several synthetic substrates for the aim of finding a clue to the substrate specificity of the enzyme.