THE MODE OF ACTION OF TRYPSIN UPON SYNTHETIC POLY-ε-AMINOCAPROYL-α-ALANINES

Abstract

Hydrolysis products of synthetic linear polymers, both poly-ε-amino-caproyl-DL-alanine and poly-ε-aminocaproyl-L-alanine by the action of trypsin were investigated by paper chromatographic analysis. Small amounts of free alanine and ε-aminocaproic acid together with large amount of dialysable peptides were found as the dialysable hydrolysis products. Sometimes traces of free ε-aminocaproyl-L-alanine could be observed in the case of poly-ε-aminocaproyl-L-alanine. Furthermore, some studies on the substrate specificity of the enzyme were carried out using a number of synthetic substrates related to the polymer, and a possible mode of action of trypsin upon the poly-ε-aminocaproyl-α-alanines was discussed.
The author wished to express his hearty thanks to Prof. F. Egami of Nagoya University, Prof. J. Noguchi of this university, Dr. R. Sato, Osaka University and to Dr. N. Sakota, Dainippon Zoki Laboratory, for their kind encouragements throughout the course of this work. The author is also grateful to Mr. K. Morita for his technical assistances.
The expense of this study was defrayed in part by a grant from the Ministry of Education