キノコプロテアーゼの精製と性質 : 2. シロタモギタケ Lyophyllum ulmarium

概要

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Two endoproteases, proteases I and II, were purified to apparent homogeneity from fruit body of shirotamogitake mushroom, Lyophyllum ulmarium, by a series of column chromatography on Toyopearl, Butyl-Toyopearl and DEAE-Toyopearl using Boc-Ala-Ala-Leu-Phe-pNA and Boc-Ala-Ala-Pro-Phe-pNA as the substrates. Protease I was most active at pH 9-10,and protease II at pH 7. Studies on the substrate specificity with synthetic peptide p-nitroanilides revealed that protease I preferentially hydrolyzed peptide bond on the carboxyl-terminal side of phenylalanine, while protease II efficiently cleaved the peptide bonds of phenylalanine, leucine and alanine. Protease I was strongly inactivated by p-chloromercuribenzoate, and protease II by diisopropyl fluorophosphate. Based on the reactivity toward substrates and behaviors against the protease inhibitors, protease I was shown to be a thiol enzyme with chymotrypsin-like specificity, and protease II was a serine protease hydrolyzing the peptide bonds of hydrophobic amino acids.
福岡女子大学の論文
1999-02-25