N-hydroxylation of the antiprotozoal drug pentamidine catalyzed by rabbit liver cytochrome P-450 2C3 or human liver microsomes, microsomal retroreduction, and further oxidative transformation of the formed amidoximes. Possible relationship to the biological oxidation of arginine to NG-hydroxyarginin

@article{Clement1994NhydroxylationOT,
  title={N-hydroxylation of the antiprotozoal drug pentamidine catalyzed by rabbit liver cytochrome P-450 2C3 or human liver microsomes, microsomal retroreduction, and further oxidative transformation of the formed amidoximes. Possible relationship to the biological oxidation of arginine to NG-hydroxyarginin},
  author={B. E. P. Clement and Fernanda Jung},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={1994},
  volume={22 3},
  pages={486-97}
}
Previous investigations have shown that the antiprotozoal drug pentamidine is N-hydroxylated by rabbit and rat liver microsomal fractions. Indirect evidence for the participation of the cytochrome P-450 enzyme system was obtained. In this study, rabbit liver cytochrome P-450 2C3 is shown by reconstitution experiments with highly purified variants of P-450 2C3 isolated from rabbit liver and purified variants of P-450 2C3 expressed by recombinant Escherichia coli to be a microsomal pentamidine N… CONTINUE READING

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