酸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〕)

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A muscle proteinase acting at acid pH has been purified about 200 fold from carp ordinary muscle by the following procedure: (1) acid heat treatment of 0.5% KCl extract, (2) (NH4)2SO4 fractionation, (3) acetone fractionation, and (4) Sephadex G-200 chromatography. The proteinase has a pH optimum at 2.8-3.0 and a temperature optimum for 1 hour reaction at near 50°C. It was stable at 37°C but lost its activity at 55°C rapidly. The proteinase was active on acid denatured hemoglobin, casein and myosin fraction protein. The enzyme did not hydrolyze synthetic substrate, CBZ-L-glu-L-tyr., BZ-L-arg-NH2 and gly-L-tyr-NH2 Na+, K+, Zn++, Co++, EDTA, KCN, cysteine and p-CMB did not affect the activity. Ni++, glutathione and 2-mercaptoethanol activated the enzyme.
社団法人日本水産学会の論文