Results 151 to 160 of about 2,725 (177)
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Microsomal and cytosolic epoxide hydrolase in Drosophila melanogaster
Biochemical Pharmacology, 1986Subcellular fractions from Drosophila melanogaster and rat liver were investigated on their epoxide hydrolase activity. Both microsomes and the post-microsomal supernatant of Drosophila appeared to contain epoxide hydrolase activity using styrene-7,8-oxide as the substrate. Based on body weight, these activities were in the same order of magnitude. Rat
A.J. Baars, M. Jansen, Douwe D. Breimer
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Microsomal epoxide hydrolase in different rat strains
Biochemical Pharmacology, 1983Epoxide hydrolase activity was determined in hepatic microsomes of adult males of 22 rat strains. The specific activity varied between 4.3 and 12.7 nmole styrene glycol/mg protein per min. The enzyme in F344, DA and Sprague--Dawley rats, strains with low, high and intermediate activity, respectively, was studied in more detail.
Franz Oesch, Hansruedi Glatt, A. Zimmer
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Epoxide Metabolites of Opiates and Their Interaction with the Hepatic Microsomal Epoxide Hydrolase [PDF]
, 1988 The biotransformation of a variety of chemicals indicates that the epoxide-diol pathway is important in the formation of active intermediates that cause damage to cellular components. The chemical structure of morphine alkaloids shows a double bond in the 7,8 position susceptible to epoxidation (Fig. 1).
A. Arnoldi, D. Cova, L. Rossini
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Biochemical and Biophysical Research Communications, 1996
We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp227-His428-Asp350 in
Glenn D. Prestwich, Hubert Wojtasek
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We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp227-His428-Asp350 in
Glenn D. Prestwich, Hubert Wojtasek
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[46] Microsomal epoxide hydrolase
1981Publisher Summary Microsomal epoxide hydrolase catalyzes the conversionof epoxides to glycols. The microsomal enzyme should not be confused with another epoxide hydrolase activity, found primarily in the cytosolic fraction, which differs greatly from membrane-bound enzyme in substrate specificity and immunological properties.
Thomas M. Guenthner +2 more
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Inhibition of Microsomal Epoxide Hydrolases by Ureas, Amides, and Amines
Chemical Research in Toxicology, 2001The microsomal epoxide hydrolase (mEH) plays a significant role in the metabolism of xenobiotics such as polyaromatic toxicants. Additionally, polymorphism studies have underlined a potential role of this enzyme in relation to several diseases, such as emphysema, spontaneous abortion, and several forms of cancer.
John W. Newman +4 more
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Post-transcriptional regulation of human microsomal epoxide hydrolase
Pharmacogenetics, 1998Microsomal epoxide hydrolase (mEH) is a key biotransformation enzyme that is variably expressed in humans. Genetic polymorphisms in the mEH gene have been identified that result in amino acid substitutions in the corresponding enzyme. Results of expression analyses of the mEH allelic variants in vitro suggest that the mutations do not affect the ...
Curtis J. Omiecinski +2 more
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A study of the hepatic microsomal epoxide hydrolase in sea birds
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 19821. Epoxide hydrolase activities were measured in six species of sea birds using the chlorinated epoxide HEOM as substrate. 2. The activities found fell within the general range for birds, and there were no clear sex or species differences. 3. Relatively low activities were found in liver microsomes of female puffins early in the breeding season, but ...
G.C. Knight, C.H. Walker
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Microsomal epoxide hydrolase polymorphism and susceptibility to ovarian cancer
Cancer Letters, 2002Polymorphic variants of microsomal epoxide hydrolase (mEPHX) with altered enzyme activity have been associated with an increased risk for ovarian cancer. We assessed the frequency of exon 3 and exon 4 variants of mEPHX among 291 ovarian cancers and 257 controls from a UK-based population. The distribution of the exon 3 alleles among both the cancer and
Ian G. Campbell +2 more
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Developmental expression of human microsomal epoxide hydrolase.
The Journal of Pharmacology and Experimental Therapeutics, 1994Microsomal epoxide hydrolase (mEH) is a critical biotransformation enzyme that catalyzes the hydrolysis of a large number of epoxide intermediates, which arise frequently from the oxidation of pharmaceutical and environmental compounds by the cytochrome P450 mixed function oxygenase system.
C J, Omiecinski, L, Aicher, L, Swenson
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