ブリ肝臓Carboxylesteraseの性状について〔ハマチ脂質分解酵素に関する研究-1-〕

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Carboxylesterase (EC 3.1.1.1) in the liver extract of young yellowtail, Seriola quinqueradiata, was purified by ammonium sulfate precipitation, followed by chromatographies on columns of DEAE cellulose and Sephadex G-100. The final preparation (S-2) was found to be homogeneous in polyacrylamide gel disc electrophoresis at pH9.4. The molecular weight and the isoelectric point of the enzyme were estimated to be about 67, 000 (by gel filtration method) and pH4.5 (by isoelectric focusing method), respectively. The enzyme had the optimum pH at 8.0 and showed the highest enzyme activity at 40°C. It was stable over the pH range of pH7.0 to 9.5, and below 35°C. Km of the enzyme was estimated to be 2.5×10-4 M. The enzyme was inhibited by such metal ions as Zn2+, Pb2+, Fe2+, Cd2+, Al2+, Hg2+, Sn2+, but not by p-chloromercuribenzoate and EDTA.
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