Hepatic mitochondrial cytochrome P-450: Isolation and functional characterization

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 pur...

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Bibliografische gegevens

Gepubliceerd in:	Proc Natl Acad Sci U S A
Hoofdauteurs:	Sato, R., Atsuta, Y., Imai, Y., Taniguchi, S., Okuda, K.
Formaat:	Artigo
Taal:	Inglês
Gepubliceerd in:	National Academy of Sciences 1977
Onderwerpen:	Biological Sciences: Biochemistry
Online toegang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC431771/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/271969/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.74.12.5477
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