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 language | English (US) |
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Pages (from-to) | 23-26 |
Number of pages | 4 |
Journal | Alcohol |
Volume | 2 |
Issue number | 1 |
DOIs | |
State | Published - 1985 |
Externally published | Yes |
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