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. 1975 Dec;152(3):705–708. doi: 10.1042/bj1520705

Dimethylnitrosamine demethylation by reconstituted liver microsomal cytochrome P-450 enzyme system.

P D Lotlikar, W J Baldy Jr, E N Dwyer
PMCID: PMC1172528  PMID: 819003

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.

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Selected References

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