Participation of superoxide,hydrogen peroxide and hydroxyl radicals in NADPH-cytochrome P-450 reductase-catalyzed peroxidation of methyl linolenate |
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| Affiliation: | The Department of Biochemistry, School of Medicine, Hokkaido University, Sapporo 060 Japan;Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI, 48201, USA;Rutgers New Jersey Medical School Department of Cell Biology and Molecular Medicine, Rutgers Biomedical and Health Sciences, Newark, NJ, 07101, USA |
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| Abstract: | - 1.1. NADPH-cytochrome P-450 reductase-catalyzed peroxidation of methyl linolenate is inhibited by superoxide dismutase, catalase, ethanol and mannitol and is potentiated by H2O2.
- 2.2. H2O2 is shown to be generated in the incubation mixture in the presence of NADPH and NADPH-cytochrome P-450 reductase. If the system contains Fe-EDTA complex, H2O2 is not formed. In the presence of the enzyme and Fe-EDTA complex, added H2O2 is consumed.
- 3.3. In the presence of Fe-EDTA complex, NADPH-cytochrome P-450 reductase is shown to generate O2− at a slow rate.These results suggest that H2O2 produced from O2− is decomposed to form OH· by the action of Fe-EDTA complex in the lipid peroxidation system and that OH· is a trigger of lipid peroxidation.
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