Elsevier

Alcohol

Volume 2, Issue 1, January–February 1985, Pages 23-26
Alcohol

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

https://doi.org/10.1016/0741-8329(85)90008-4Get rights and content

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.

References (30)

Cited by (9)

  • Purification and characterization of human liver cytochrome P-450-ALC

    1987, Biochemical and Biophysical Research Communications
  • Alcohol’s promotion of gastrointestinal carcinogenesis

    2017, Alcohol and the Gastrointestinal Tract
  • Interaction study of curcumin with 1-butanol binary mixture

    2013, Research Journal of Pharmaceutical, Biological and Chemical Sciences
View all citing articles on Scopus

This research was supported by Grant AA-06221 from the National Institute on Alcohol Abuse and Alcoholism.

View full text