Role of alcohol P-450-oxygenase (APO) in microsomal ethanol oxidation

Dennis R. Koop, Minor J. Coon

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

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 catalyzes the oxidation of a variety of primary and secondary alcohols to aldehydes and ketones, including methanol, ethanol, n-propanol, n-butanol, 2-butanol, n-pentanol, and cyclohexanol. Other purified P-450 cytochromes, including isozymes 2, 3b, 3c, 4, and 6, are much less active than P-450alc in the oxidation of alcohols. That P-450alc functions in ethanol oxidation in liver microsomal membranes as well as in the reconstituted system was shown by immunochemical experiments involving inhibition by sheep anti-P-450alc antibodies. We conclude that P-450alc is the predominant ethanol-oxidizing cytochrome present after induction by chronic alcohol administration and that the other P-450 cytochromes have low but significant activity in both control and ethanol-induced animals.

Original languageEnglish (US)
Pages (from-to)23-26
Number of pages4
JournalAlcohol
Volume2
Issue number1
DOIs
StatePublished - Jan 1 1985

Keywords

  • Alcohol P-450-oxygenase (APO)
  • Antibodies to P-450alc
  • Cytochrome P-450, role in ethanol oxidation
  • Microsomal ethanol oxidation
  • P-450 isozyme 3a
  • P-450alc

ASJC Scopus subject areas

  • Health(social science)
  • Biochemistry
  • Toxicology
  • Neurology
  • Behavioral Neuroscience

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