Liver microsomal epoxide hydrase.

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Liver microsomal epoxide hydrase.

1. The substrate specificity of membrane-bound and purified epoxide hydrase from rat liver microsomes has been studied. Both enzyme preparations catalyzed the hydration of a variety of alkene oxidase as well as arene oxides of several polycyclic aromatic hydrocarbons. 2. Unlike the membrane-bound enzyme, the rate of hydration for most of the substrates catalyzed by the purified epoxide hydrase ...

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Hepatic Microsomal Epoxide Hydrase

The effects of a wide variety of chemical modification reagents on the activity of purified rat liver microsomal epoxide hydrase have been investigated. Alkylating agents, such as the phenacyl bromides and benzyl bromide are potent inhibitors of epoxide hydrase. Z-Bromo-4’-nitroacetophenone @-nitrophenacyl bromide) specifically and irreversibly inactivates epoxide hydrase. Pseudo-first order ki...

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Identification of epoxide hydrase as the preneoplastic antigen in rat liver hyperplastic nodules.

A liver microsomal protein, previously referred to as preneoplastic antigen, from hyperplastic nodules of rats fed a diet containing 2-acetylaminofluorene has been identified as the enzyme epoxide hydrase [glycol hydro-lyase (epoxideforming), EC 4.2.1.63]. Purified preneoplastic antigen from hyperplastic nodules and purified rat liver microsomal epoxide hydrase are immunochemically identical on...

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Cytosolic and microsomal epoxide hydrolases: differential properties in mammalian liver.

The epoxide hydrolase activities of the 100,000 g pellet (microsomal) and 100,00 g soluble (cystosolic) fractions of mouse, rat, and guinea pig liver were measured with three closely related compounds used as substrates. Differences between the species in the distribution of the cytosolic and microsomal hydrolases and in their substrate specificities and pH optima demonstrate why epoxide hydrol...

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Distribution and properties of a mammalian soluble epoxide hydrase.

Two substrates, 1-(4’-ethylphenoxy)-3,7-dimethyl-6,7-epoxy-trans-2-octene and cis-epoxymethyl stearate were used to determine the distribution of epoxide hydrase activity in mammals. The highest epoxide hydrase activity in liver subcellular fractions was found in the 100,000 g supernatant and the mitochondrial fraction, while activity in washed microsomes is lower. The 100,000 g supernatant epo...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1977

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)40311-5