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KMID : 0374019800030010009
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Ewha Medical Journal
1980 Volume.3 No. 1 p.9 ~ p.14
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Cytochrome P-450 Dependent N-and Ring-Hydroxylation of AAF of Various Fish Liver Compare with Rat Liver
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Abstract
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2-Acetylaminofluorene (AAF) is a useful model compound for studying the biochemical mechanisms of hydroxylation since it could undergo hydroxylation at several carbon atoms in the ring as well as on the nitrogen atom.
These hydroxylation reactions are important due to the fact that N-hydroxylation is an activation step in the carcinogenic process whereas ring-hydroxylation is an inactivation step. Both N-and ring-hydroxylation of AAF occur in the liver microsomes in the presence of NADPH and molecular oxygen.
The present studies were undertaken to investigate the hepatic micrasomal hemoproteins P-450 and the N-and ring hydroxylation of AAF in vitro in the rat, rabbit and carp, crucian and sea bass. Nhydroxylation of 2-acetylaminofluorene in liver microsomes from carp, crucian and sea bass was formed 5%, 9% or 42% respectively.
These results indicate that N-acetylarylamines can be N-oxidized by a cytochrome P-450 dependent mixed function oxidase in fish liver microsomes.
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