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Species differences in the hydroxylation of aniline and N-ethylaniline by liver microsomes

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Summary

The velocity of the N- and p-hydroxylation of aniline and N-ethylaniline by NADPH-dependent hydroxylases in guinea pig liver microsomes was found to be as high as in rabbit liver microsomes. Microsomes prepared from cat livers were less active.

The effect of 2,4-dichlorophenol, p-chloromercuribenzoate, semicarbazide, and 8-hydroxyquinoline on the microsomal hydroxylations was observed to be not uniform in the microsomes of the species studied.

Carbon monoxide inhibited the p-hydroxylation of N-ethylaniline by the microsomes prepared from the livers of rabbits, guinea pigs, dogs, and rats. The N-hydroxylation of N-ethylaniline by microsomes from rat's liver was inhibited like the p-hydroxylation by carbon monoxide. The N-hydroxylation by dog and guinea pig microsomes was scarcely, if at all, inhibited by the same carbon monoxide pressure. These enzymes showed a lower affinity for oxygen than the N-hydroxylating enzyme in rat microsomes and the p-hydroxylating enzymes.

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Appel, W., Graffe, W., Kampffmeyer, H. et al. Species differences in the hydroxylation of aniline and N-ethylaniline by liver microsomes. Naunyn - Schmiedebergs Arch 251, 88–94 (1965). https://doi.org/10.1007/BF00245732

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