コイ肉5-ヌクレオチダーゼの性質

概要

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The purified 5-nucleotidase from carp muscle showed the optimum activity at about pH7.5 At above this pH, Mg2+ affected the 5-nucleotidase activity in a complex manner, showing a second optimum at pH 9 in the presence of some buffer ions. ADP and ATP were effective inhibitors of the enzyme in a manner of competitive inhibition. ADP was a far more powerful inhibitor than ATP. The enzyme activity was also inhibited by the addition of EDTA and the inhibition was dependent on the time of incubation with chelating agent. The inhibition of the enzyme by EDTA apparently followed a second order equation, logVt/Vo=-k[EDTA]t. The apoenzyme which was prepared by treatment with EDTA restored the original activity effectively by the addition of Zn2+, and was more unstable on heating than the intact enzyme.
公益社団法人日本水産学会の論文