ブリ幽門垂のジアミンオキシダ-ゼの精製および性状〔英文〕

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Diamine oxidase was purified from acetone powder of pyloric caeca of yellowtail by chroma-tography on DEAE-cellulose (stepwise), DEAE-cellulose (linear gradient) and hydroxyapatite. The purified diamine oxidase showed a single protein band on disc electrophoresis, and its molecular weight was estimated to be 140, 000 by gel filtration. The enzyme was separated into two subunits by SDS-polyacrylamide gel electrophoresis, and molecular weights of each subunits were estimated to be 80, 000 and 60, 000, respectively. The optimal pH's of the enzyme for oxidation of cadaverine and histamine, were 7.5 and 7.0 respectively, and the enzyme was stable between pH values 7.0 to 8.0. The enzyme was most active at 50°C, but unstable at 60°C. The enzyme was strongly inactivated by Hg2+, Ni2+, and Cu2+, and activated by Al3+ and Zn2+, and more strongly by Mn2+ and Co2+. The enzyme activity completely disappeared by the gel filtration on Bio-gel P-2, and the simultaneous addition of Mn2+ and Cu2+ into the reaction mixture recovered nearly all of the activity. The enzyme activity was strongly inhibited by iproniazid and 2-mercaptoethanol, and completely by amino-guanidine and KMnO4. The enzyme activity was more prominent for C3-C6 aliphatic diamines, such as putrescine and cadaverine, than histamine and agmatine. The Km value of diamine oxidase for cadaverine was found to be 1.46×10-5M.
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