Purification and some properties of DCPA hydrolyzing enzyme in microsomal fraction of pig liver.
1991
Kimura T. | Kodama O. | Akatsuka T.
DCPA hydrolyzing enzyme was solubilized by Triton X-100 from the microsomal fraction prepared from pig liver. After removal of Triton X-100 from solubilized fraction by Bio-Beads SM-2 treatment, solubilized DCPA hydrolyzing enzyme was purified by Sephadex G-200 gel filtration and column chromatography on hydroxylapatite. The final preparation was homogenous in polyacrylamide gel electrophoresis at pH 8.3 and purified approximately 200-fold in a 28% yield. The molecular weight of the enzyme was estimated to be approximately 200,000 by gel filtration and the weight of the subunits enzyme was determined to be 60,000 by SDS-PAGE. These results suggested that the enzyme may be homooligomeric enzyme. The enzyme was inhibited by DFP. Among the pesticides tested, carbamate pesticides such as Sevin and organophosphorus pesticides such as Sumioxon and IMP completely inhibited the enzyme activities. The enzyme hydrolyzed not only DCPA but also ethyl n-butyrate and p-nitrophenyl acetate. Therefore, this enzyme may belong to carboxylesterase.
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