HYDROLYSIS OF ε-AMINOCAPROYL COMPOUNDS BY TRYPSIN

Abstract

In studies on the action of trypsin to ε-aminocaproyl compounds it has been shown that the peptides, amide or esters of ε-aminocaproic acid can be partly hydrolysed by the enzyme action. It seems that an enzyme which catalyzes the hydrolysis of these compounds is trypsin itself from the ex-amination of the stability, inhibitions of the enzymes responsible. Optimum pH, Km, and proteolytic coefficient k₃, were also determined for the hydrolysis. Several w-amino-n-fatty acid (C₅-C₃) derivatives, ornithine ethyl ester ε-caprolactarn and adipamide, structurally related to ε-aminocaproic acid derivatives, made completely resistance to the hydrolytic action of the enzyme.
The authors wish to express their hearty thanks to Prof. F. Egami of Nagoya University, Prof. J. Noguchi of this University, and Dr. R. Sato, Osaka University for their kind encouragements throughout the course of this work. The authors are also grateful to Mr. T. Nojiri for his technical assistances.
The expense of this study was defrayed in part by a grant from the Ministry of Education.