Action of Carbon Tetrachloride in the Reconstituted Monooxygenase System Using Partially Purified Cytochrome P-450 and P-448

In the cytochrome P-450-reconstituted system, CCI4 stimulated NADPH-dependent lipid peroxidation of the system containing the P-450 form to a much greater extent than that of the system containing the P-448 form. When the P-450-reconstituted system was preincubated in the presence of both NADPH and...

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Bibliographic Details
Published in:Japanese Journal of Pharmacology 1987, Vol.43 (2), p.226-229
Main Authors: MASUDA, Yasusuke, YASOSHIMA, Mitsue
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Carbon Tetrachloride - pharmacology
Chemical and industrial products toxicology. Toxic occupational diseases
Cytochrome P-450 CYP1A2
Cytochrome P-450 Enzyme System - metabolism
Cytochromes - metabolism
In Vitro Techniques
Lipid Peroxides - metabolism
Liver - drug effects
Liver - enzymology
Male
Medical sciences
Methylcholanthrene - pharmacology
Mixed Function Oxygenases - metabolism
Pentobarbital - pharmacology
Rats
Rats, Inbred Strains
Solvents
Toxicology
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Summary:In the cytochrome P-450-reconstituted system, CCI4 stimulated NADPH-dependent lipid peroxidation of the system containing the P-450 form to a much greater extent than that of the system containing the P-448 form. When the P-450-reconstituted system was preincubated in the presence of both NADPH and CCI4, 7-ethoxycoumarin O-deethylase, aminopyrine N-demethylase and aniline hydroxylase activities were decreased by 40–60%, whereas, with P-448 form reconstituted system, no suppression was observed in these enzyme activities or in 7-ethoxyresorufin O-deethylase activity. These observations suggest that the P-450 form, but not the P-448 form, is active in metabolizing CCI4 to a reactive species that subsequently impairs the hemoprotein.
ISSN:0021-5198
1347-3506
DOI:10.1016/S0021-5198(19)43543-9