Dimethylnitrosamine demethylation by reconstituted liver microsomal cytochrome P-450 enzyme system
| Autor: | E N Dwyer, W J Baldy, Prabhakar D. Lotlikar |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Male
Nitrosamines Cytochrome Hamster Biochemistry Dimethylnitrosamine Cytochrome P-450 Enzyme System Enzyme system Cricetinae Animals Molecular Biology NADPH-Ferrihemoprotein Reductase Demethylation chemistry.chemical_classification biology Cytochrome c peroxidase Cytochrome P450 reductase Cell Biology Molecular biology Rats Enzyme chemistry Microsomes Liver Microsome biology.protein Research Article |
| Zdroj: | Biochemical Journal. 152:705-708 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj1520705 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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