| Literature DB >> 819003 |
P D Lotlikar, W J Baldy, E N Dwyer.
Abstract
Oxidative demethylation of dimethylnitosamine was studied with both reconstituted and unresolved liver microsomal cytochrome P-450 enzyme systems from rats and hamsters. Proteinase treatment of liver microsomal preparations yielded cytochrome P-450 particulate fractions. Both cytochrome P-450 and NADPH- cytochrome c reductase fractions were required for optimum demethylation activity. Particulate cytochrome P-450 fractions were more effecient than either Triton X-100- or cholatesolubilized preparations of these particles in demethylation activity with rat and hamster liver preparations appear to be due to differences in specificity in their cytochrome P-450 fractions.Entities:
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Year: 1975 PMID: 819003 PMCID: PMC1172528 DOI: 10.1042/bj1520705
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857