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. 1981 Sep;78(9):5362–5366. doi: 10.1073/pnas.78.9.5362

Liver microsomal cytochrome P-450 and the oxidative metabolism of arachidonic acid.

J Capdevila, N Chacos, J Werringloer, R A Prough, R W Estabrook
PMCID: PMC348745  PMID: 6795631

Abstract

Arachidonic acid is oxidatively metabolized by rat liver microsomes at a rate of approximately 5 nmol per min per mg of protein at 25 degrees C. This reaction is dependent on the presence of NADPH and oxygen. Studies with various inhibitors indicate a role for membrane-bound cytochrome P-450 in the transformation of arachidonic acid to a mixture of hydroxy acid derivatives. The stoichiometry of the reaction conforms to that of a monooxygenase reaction--i.e., one mole of NADPH is oxidized per mole of oxygen utilized--suggesting a reaction mechanism different from that proposed for lipid peroxidation reactions. No evidence for the formation of prostaglandin-like metabolites was obtained. The diene character of some of the metabolites formed suggests another role for cytochrome P-450--i.e., participation in hydrogen abstraction reactions for the activation of various substrates.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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