Epoxide hydrolase activity in isolated peroxisomes of mouse liver.

نویسندگان

  • F Waechter
  • P Bentley
  • F Bieri
  • W Stäubli
  • A Völkl
  • H D Fahimi
چکیده

Using trans-stilbene oxide as substrate, the subcellular distribution of epoxide hydrolase was investigated in livers from DBA/2 mice. The highest specific activities were found in cytosolic and light mitochondrial fractions. Isopycnic subfractionation of the light mitochondrial fraction showed that the organelle-bound trans-stilbene oxide hydrolase is localized in peroxisomes.

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منابع مشابه

Differential subcellular localization of endogenous and transfected soluble epoxide hydrolase in mammalian cells: evidence for isozyme variants.

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Design, Synthesis and Biological Activity of 4,6-disubstituted Pyridin-2(1H)-ones as Novel Inhibitors of Soluble Epoxide Hydrolase

Soluble epoxide hydrolase enzyme is a promising therapeutic target for hypertension, vascular inflammation, pain and some other risk factors of cardiovascular diseases. The most potent sEH inhibitors reported in the literature are urea-based ones which often have poor bioavailability. In this study, in a quest for finding potent inhibitors of soluble epoxide hydrolase, some 4,6-disubstituted py...

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Epoxide hydrolase in human and rat peroxisomes: implication for disorders of peroxisomal biogenesis.

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Molecular cloning and expression of murine liver soluble epoxide hydrolase.

A clofibrate-induced mouse liver cDNA library was prepared and used to isolate the coding sequence for soluble epoxide hydrolase. A 1668-base pair (bp) clone was isolated and found to contain a 1269-bp open reading frame coding for 423 amino acids. Subsequent RNA polymerase chain reaction resulted in the isolation of 396 bp of additional 5'-sequence. Translation of the resulting 1659-bp open re...

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عنوان ژورنال:
  • FEBS letters

دوره 158 2  شماره 

صفحات  -

تاریخ انتشار 1983