Properties and Inhibition Spectrum of a New Human Pancreatic Protease

Abstract

In our laboratory we have isolated to this date two forms of trypsin and three forms of chymotrypsin from homogenates of human pancreatic tissue [1-4]. However, we have been unable to detect the presence of any specific enzyme which hydrolyzes elastin. Nevertheless, a proteolytic enzyme (Protease E), which hydrolyses all of the conventional synthetic substrates used for identification of elastase activity (benzyloxycarbonyl-L-alanine p-nitrophenyl ester, N-tert-butyl-oxycarbonyl-L-alanine p-nitrophenyl ester and acetyl-L-alanyl-L-alanyl-L-alanine methyl ester) has been identified and purified to homogeneity. This enzyme is referred to elsewhere as a second proteolytic component isolated during the purification of anionic trypsin [2].

This research was supported in part by grants from the National Institute of Health and the Council for Tobacco Research, USA.