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- W104217360 abstract "Epoxide hydrolase activities have been found to be enriched in three different intracellular compartments of liver cells, i.e., the endoplasmic reticulum, peroxisomes, and cytosol. While the activity at the first of these locations is membrane bound, the other two acitivities are catalyzed by soluble proteins (Oesch 1973; Gill and Hammock 1981). The cytosolic and peroxisomal forms of epoxide hydrolase are very similar in several respects, as judged from experiments with crude subcellular fractions (see, e.g., Pichare and Gill 1985). In order to further investigate the structural relatedness of these soluble forms of epoxide hydrolase, they have been purified to homogeneity using immunoaffinity chromatography and the pure proteins characterized physicochemically." @default.
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- W104217360 date "1988-01-01" @default.
- W104217360 modified "2023-09-23" @default.
- W104217360 title "Immunoaffinity Purification and Comparison of Epoxide Hydrolases from Liver Cytosol and Peroxisomes of Untreated and Clofibrate-Treated Mice" @default.
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- W104217360 doi "https://doi.org/10.1007/978-3-642-73113-6_47" @default.
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