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.
Research Article|December 01 1975
Dimethylnitrosamine demethylation by reconstituted liver microsomal cytochrome P-450 enzyme system
P D Lotlikar;
W J Baldy, Jr;
Biochem J (1975) 152 (3): 705-708.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
P D Lotlikar, W J Baldy, E N Dwyer; Dimethylnitrosamine demethylation by reconstituted liver microsomal cytochrome P-450 enzyme system. Biochem J 1 December 1975; 152 (3): 705–708. doi: https://doi.org/10.1042/bj1520705
Download citation file: