Abstract
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.
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References
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© 1986 Plenum Press, New York
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Miller, M.G., Powell, J., Cohen, G.M. (1986). Formation and Identification of Naphthoquinone Glutathione Conjugates Following Microsomal Metabolism of 1-Naphthol. In: Kocsis, J.J., Jollow, D.J., Witmer, C.M., Nelson, J.O., Snyder, R. (eds) Biological Reactive Intermediates III. Advances in Experimental Medicine and Biology, vol 197. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5134-4_37
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DOI: https://doi.org/10.1007/978-1-4684-5134-4_37
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