Inhibition of desipramine hydroxylation (Cytochrome P450-2D6) in vitro by quinidine and by viral protease inhibitors: relation to drug interactions in vivo.

@article{Moltke1998InhibitionOD,
  title={Inhibition of desipramine hydroxylation (Cytochrome P450-2D6) in vitro by quinidine and by viral protease inhibitors: relation to drug interactions in vivo.},
  author={Lisa L. von Moltke and David J Greenblatt and Su Xiang Duan and Johanna Daily and Jerold S. Harmatz and Richard I. Shader},
  journal={Journal of pharmaceutical sciences},
  year={1998},
  volume={87 10},
  pages={1184-9}
}
Pharmacokinetic drug interactions with viral protease inhibitors are of potential clinical importance. An in vitro model was applied to the quantitative identification of possible interactions of protease inhibitors with substrates of cytochrome P450-2D6. Biotransformation of desipramine (DMI) to hydroxydesipramine (OH-DMI), an index reaction used to profile activity of human cytochrome P450-2D6, was studied in vitro using human liver microsomes. Quinidine and four viral protease inhibitors… CONTINUE READING
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