Identification of human cytochrome P450 isoforms involved in the 3-hydroxylation of quinine by human live microsomes and nine recombinant human cytochromes P450.

@article{Zhao1996IdentificationOH,
  title={Identification of human cytochrome P450 isoforms involved in the 3-hydroxylation of quinine by human live microsomes and nine recombinant human cytochromes P450.},
  author={Xue Jin Zhao and Hirokazu Yokoyama and Kan Chiba and Sompon Wanwimolruk and Takashi Kariya Ishizaki},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1996},
  volume={279 3},
  pages={
          1327-34
        }
}
Studies using human liver microsomes and nine recombinant human cytochrome P450 (CYP) isoforms (CYP1A1, 1A2, 2A6, 2B6, 2C9, 2C19, 2D6, 2E1 and 3A4) were performed to identify the CYP isoform(s) involved in the major metabolic pathway (3-hydroxylation) of quinine in humans. Eadie-Hofstee plots for the formation of 3-hydroxyquinine exhibited apparently monophasic behavior for all of the 10 different microsomal samples studies. There was interindividual variability in the kinetic parameters, as… CONTINUE READING

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