Ethanol Oxidation and Toxicity: Role of Alcohol P-450 Oxygenase
نویسندگان
چکیده
منابع مشابه
Role of alcohol P-450-oxygenase (APO) in microsomal ethanol oxidation.
The form of liver microsomal cytochrome P-450 induced by chronic administration of ethanol to rabbits, designated as P-450ALC or P-450 isozyme 3a, has been purified to homogeneity as judged by several criteria, including NH2- and COOH-terminal amino acid sequence determination. The reconstituted alcohol-P-450 oxygenase (APO) system containing P-450ALC and NADPH-cytochrome P-450 reductase cataly...
متن کاملAlcohol metabolism and toxicity: role of cytochrome P-450.
A new isozyme of cytochrome P-450, designated from 3a on the basis of its relative electrophoretic mobility, has been purified to homogeneity from liver microsomes of rabbits treated chronically with ethanol. This cytochrome has the highest activity of the known rabbit P-450 isozymes in the oxidation of ethanol to acetaldehyde. In view of the reports of others that the hepatotoxicity of acetami...
متن کاملImmunochemical evidence for a role of cytochrome P-450 in liver microsomal ethanol oxidation.
Antibodies to cytochrome P-450 isozyme 3a, the ethanol-inducible isozyme in rabbit liver, were used to determine the role of this enzyme in the microsomal oxidation of alcohols and the p-hydroxylation of aniline. P-450 isozymes, 2, 3b, 3c, 4, and 6 did not crossreact with anti-3a IgG as judged by Ouchterlony double diffusion, and radioimmunoassays indicated a crossreactivity of less than 1%. Gr...
متن کاملEthanol oxidation by a component of liver microsomes rich in cytochrome P-450.
A cytochrome P-450-rich fraction free of alcohol dehydrogenase activity and containing only small amounts of catalase was prepared from rat liver microsomes and shown to catalyze the NADPH-dependent oxidation of ethanol. The recoveries of cytochrome P-450 and the activity of the NADPH-dependent ethanol oxidation were 15.6% and 14.0%, respectively. The addition of separated cytochrome c reductas...
متن کاملAlcohol oxidation by isozyme 3a of liver microsomal cytochrome P-450.
Liver microsomes from rabbits treated chronically with ethanol were solubilized and fractionated to yield a new isozyme of cytochrome P-450 in a homogeneous state. This cytochrome, designated as isozyme 3a on the basis of its relative electrophoretic mobility, is distinct from the known terminal amino acid sequences. In addition, peptide mapping by high performance liquid chromatography followi...
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ژورنال
عنوان ژورنال: Alcoholism: Clinical and Experimental Research
سال: 1986
ISSN: 0145-6008,1530-0277
DOI: 10.1111/j.1530-0277.1986.tb05179.x