Identification of ethanol-inducible P-450 isozyme 3a as the acetone and acetol monooxygenase of rabbit microsomes.

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Identification of ethanol-inducible P-450 isozyme 3a as the acetone and acetol monooxygenase of rabbit microsomes.

Treatment of rabbits with 1% (v/v) acetone for 1 week resulted in the appearance in blood serum of 88 +/- 14 14 nmol/ml 1-hydroxyacetone (acetol) and 70 +/- 9 nmol/ml 1,2-propanediol. Untreated rabbits had no detectable 1,2-propanediol or acetol. Hepatic microsomes from control, ethanol-, and acetone-treated rabbits catalyzed the hydroxylation of acetone at rates of 0.32 +/- 0.01, 2.01 +/- 0.43...

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Benzene metabolism by ethanol-, acetone-, and benzene-inducible cytochrome P-450 (IIE1) in rat and rabbit liver microsomes.

Ethanol is known to exert a synergistic effect on the toxicity of benzene. In the present investigation it was found that benzene was metabolized at a rate 20-65-fold higher in liver microsomes from ethanol- or acetone-treated rats than in microsomes from control animals. One high affinity site [Km = 19 +/- 5 (SD) microM] and one low affinity site [Km = 0.3 +/- 0.1 mM] for benzene metabolism we...

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Catalytic activity of cytochrome P-450 isozyme 3a isolated from liver microsomes of ethanol-treated rabbits. Oxidation of alcohols.

Cytochrome P-450 isozyme 3a, isolated from hepatic microsomes of rabbits treated chronically with ethanol, was found to have a unique substrate specificity when compared with isozymes 2, 3b, 3c, and 4. Form 3a has unusually high activity in the p-hydroxylation of aniline and in the oxidation of alcohols to aldehydes. These properties are reflected in the increased activities of these substrates...

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On the amino acid sequence of cytochrome P-450 isozyme 4 from rabbit liver microsomes.

Isozyme 4 of rabbit liver microsomal cytochrome P-450 was shown earlier in this laboratory to contain multiple NH2-terminal residues, whereas isozymes 2, 3a, 3b, and 3c have single, unique NH2-terminal sequences. Similar results were obtained with isozyme 4 obtained from animals that were untreated, treated with phenobarbital (which does not induce this isozyme), or induced with beta-naphthofla...

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Benzene Metabolism by Ethanol-, Acetone-, and Benzene-inducible Cytochrome P-450 (IIE1) in Rat and Rabbit Liver Microsomes1

Ethanol is known to exert a synergistic effect on the toxicity of benzene. In the present investigation it was found that benzene was metabolized at a rate 20-65-fold higher in liver microsomes from ethanolor acetonetreated rats than in microsomes from control animals. One high affinity site \Ka = 19 ±5 (SD) urn] and one low affinity site [K„ = 0.3 ±0.1 IIIM| for benzene metabolism were pre...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1985

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)38768-9