PURIFICATION AND CHARACTERIZATION OF DOG LIVER MICROSOMAL EPOXIDE HYDROLASE

被引:13
|
作者
ARIYOSHI, N [1 ]
TANAKA, M [1 ]
ISHII, Y [1 ]
OGURI, K [1 ]
机构
[1] KYUSHU UNIV 62,FAC PHARMACEUT SCI,HIGASHI KU,FUKUOKA 812,JAPAN
来源
JOURNAL OF BIOCHEMISTRY | 1994年 / 115卷 / 05期
关键词
DOG; MICROSOMAL EPOXIDE HYDROLASE; PURIFICATION;
D O I
10.1093/oxfordjournals.jbchem.a124449
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 effecters 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.
引用
收藏
页码:985 / 990
页数:6
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