Dimethylnitrosamine demethylation by reconstituted liver microsomal cytochrome P-450 enzyme system
- 1 December 1975
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 152 (3), 705-708
- https://doi.org/10.1042/bj1520705
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.Keywords
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