Oxidation of n-hydroxyphentermine to 2-methyl-2-nitro-1-phenylpropane by liver microsomes
| Autor: | Arthur K. Cho, Michael S. Maynard |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Male
Azides Phentermine Xanthine Oxidase Nitro compound Biochemistry Medicinal chemistry Superoxide dismutase Hydroxylation Glucose Oxidase chemistry.chemical_compound Cytochrome P-450 Enzyme System Animals Xanthine oxidase Hydrogen peroxide Demethylation Pharmacology chemistry.chemical_classification Reactive oxygen species biology Superoxide Hydrogen Peroxide Catalase Rats Kinetics chemistry Microsomes Liver biology.protein Rabbits |
| Zdroj: | Biochemical Pharmacology. 30:1115-1119 |
| ISSN: | 0006-2952 |
| DOI: | 10.1016/0006-2952(81)90450-0 |
| Popis: | The role of cytochrome(s) P-450 in the oxidation of N -hydroxyphentermine to 2-methyl-2-nitro-1-phenylpropane by liver microsomes was examined using inhibitors of this heme system. The reaction resembled the N -hydroxylation of phentermine and the N -demethylation of benzphetamine in its sensitivity to carbon monoxide, metyrapone, and 2,4-dichloro-6-phenylphenoxy-ethylamine, but it differed from these reactions in its inhibition by Superoxide dismutase. Superoxide, generated by xanthine oxidase, was also capable of oxidizing N -hydroxyphentermine, but glucose oxidase generated hydrogen peroxide was not. Superoxide dismutase completely blocked nitro compound formation when substantial levels of hydrogen peroxide were present in the incubation mixture. These observations suggest that this hydroxylamine-nitro oxidation is mediated by microsome-generated Superoxide. |
| Databáze: | OpenAIRE |
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