キノコプロテアーゼの精製と性質 : 1. シイタケ Letinus edodes

概要

論文の詳細を見る
A chymotrypsin-like endoprotease was purified from shiitake mushroom (Lentinus edodes) homogenate by ammonium sulfate precipitation, gel filtration on Sephadex G-100,hydrophobic chromatography on Butyl-Toyopearl and ion-exchange chromatography on DEAE-Toyopearl using t-butyloxycarbonyl-Ala-Ala-Pro-Phe p-nitroanilide as a substrate. The final preparation was homogeneous by polyacrylamide gel electrophoresis. Studies on the substrate specificity with peptide p-nitroanilides revealed that this protease preferentially hydrolyzed peptide bonds on the carboxyl-terminal side of phenylalanine and leucine. It was most active at pH 9-10 for the hydrolysis of Boc-Ala-Ala-Pro-Phe-pNA. The activity was strongly inhibited by diisopropyl phosphofluoridate, indicating the serine protease nature of the enzyme. The enzyme was also inactivated by chymostatin, and partially inhibited by tosyl-_L-phenylalanine chloromethylketone and elastatinal.
福岡女子大学の論文
1998-02-25