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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Dec;74(12):5477–5481. doi: 10.1073/pnas.74.12.5477

Hepatic mitochondrial cytochrome P-450: Isolation and functional characterization

R Sato *, Y Atsuta †, Y Imai *, S Taniguchi †, K Okuda †
PMCID: PMC431771  PMID: 271969

Abstract

A CO-binding heme protein was solubilized and partially purified from the inner membrane fraction of rat liver mitochondria by a modification of a method [Imai, Y. & Sato, R. (1974) Biochem. Biophys. Res. Commun. 60, 8-14] developed to purify cytochrome P-450 from liver microsomes. The partially purified preparation contained protoheme and its spectral properties are characteristic of the heme proteins of the cytochrome P-450 family. The isolated cytochrome P-450 preparation could reconstitute a CO-sensitive, NADPH-dependent 26-hydroxylation activity for 5β-cholestane-3α,7α,-12α-triol when supplemented with NADPH-adrenodoxin reductase and adrenodoxin, both purified from bovine adrenocortical mitochondria. Unlike a cytochrome P-450 purified from liver microsomes of drug-untreated rats, however, the liver mitochondrial cytochrome P-450 could not catalyze NADPH-dependent benzphetamine N-demethylation in the presence of adrenodoxin reductase and adrenodoxin or function with the purified microsomal NADPH-cytochrome c reductase plus Emulgen 913 as an electron-donating system. It is concluded that the rat liver inner mitochondrial membrane houses a species of cytochrome P-450 functional in 5β-cholestane-3α,7α,12α-triol 26-hydroxylation.

Keywords: heme protein, liver mitochondria, bile acid, cholestanetriol 26-hydroxylase

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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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