Formation and Identification of Naphthoquinone Glutathione Conjugates Following Microsomal Metabolism of 1-Naphthol
Previous studies have indicated that 1-naphthol is metabolised by the cytochrome P-450 mixed function oxidase enzyme system to form a reactive species capable of covalently binding to microsomal protein (1,2). Furthermore, Hesse and Mezger (1) suggested the involvement of quinones and/or semiquinones in 1-naphthol-dependent covalent binding. In more recent studies, 1,4-naphthoquinone formed from 1-naphthol has been directly measured with both rat liver microsomes (2,3) and a reconstituted cytochrome P-450 enzyme system (4). From this, it was hypothesised that the toxicity of 1-naphthol, previously reported in isolated hepatocytes (5), may be mediated by naphthoquinone metabolites of l-naphthol.
KeywordsCovalent Binding Fast Atom Bombardment Microsomal Protein Proton Nuclear Magnetic Resonance Glutathione Conjugate
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