Purification and characterization of dog liver microsomal epoxide hydrolase

Noritaka Ariyoshi, Mitsuko Tanaka, Yuji Ishii, Kazuta Oguri

研究成果: ジャーナルへの寄稿学術誌査読

13 被引用数 (Scopus)


An epoxide hydrolase (mEH) in liver microsomes was purified to apparent homogeneity from a dog treated with phenobarbital. The purified enzyme had a minimum molecular weight of 47,000 as determined by SDS-PAGE. The dog mEH activity was characterized by use of a substrate, 7-glycidoxycoumarin (GOC), and some effectors of this enzyme. In vitro activators, metyrapone, and isoquinoline, stimulated the microsomal activity, but the former had no such effect on the purified enzyme in case of this substrate. All mEH inhibitors, 1,1,1-trichloropropene 2,3-oxide (TCPO), cyclohexene oxide, and 2-bromo-4'-nitroacetophenone (BrNAP), suppressed hydrolase activity. The NH2-terminal amino acid sequence of the purified enzyme was highly homologous (90%) to the sequences deduced from a cDNA clone of rat enzyme. Antiserum to the purified enzyme raised in rabbits cross-reacted with rat and Guinea pig epoxide hydrolases. No gender-difference in this enzyme in liver microsomes was observed in dogs.

ジャーナルJournal of biochemistry
出版ステータス出版済み - 1月 1 1994

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学


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