弱アルカリ性域で作用するプロテイナーゼの精製とその性質 (魚筋肉のプロテアーゼに関する研究-2,3-〔英文〕)

概要

論文の詳細を見る
A muscle proteinase acting at alkaline pH has been purified about 100 fold from carp ordinary muscle by the following procedure: (1) heat-treatment of 0.5% KCl extract, (2) (NH4)2SO4 fractionation, and (3) Sephadex G-200 chromatography. Crude preparation exhibited very little or no activity below 55°C, but showed fair activity at 50°C and 55°C when heated at 65°C before assay. The proteinase had a pH optimum at 8.0 and a temperature optimum for two hour reaction at 65°C. It was fairly stable at 60°C. It was active on casein, hemoglobin and somewhat active on endogenous protein. The enzyme was inhibited by Zn++, Co++ and Ni++ but not by Na+ and K+. DETA and KCN activated the enzyme. It was activated by 2-mercaptoethanol and cysteine but inhibited by p-CMB.
社団法人日本水産学会の論文