Major role of the CYP2C isozymes in deamination of amphetamine and benzphetamine: evidence for the quinidine-specific inhibition of the reactions catalysed by rabbit enzyme.

@article{Shiiyama1997MajorRO,
  title={Major role of the CYP2C isozymes in deamination of amphetamine and benzphetamine: evidence for the quinidine-specific inhibition of the reactions catalysed by rabbit enzyme.},
  author={S. Shiiyama and T. Soejima-Ohkuma and S. Honda and Y. Kumagai and A. Cho and H. Yamada and K. Oguri and H. Yoshimura},
  journal={Xenobiotica; the fate of foreign compounds in biological systems},
  year={1997},
  volume={27 4},
  pages={
          379-87
        }
}
  • S. Shiiyama, T. Soejima-Ohkuma, +5 authors H. Yoshimura
  • Published 1997
  • Chemistry, Medicine
  • Xenobiotica; the fate of foreign compounds in biological systems
  • 1. The cytochrome P450 isozymes involved in the deamination of amphetamine (AP) and benzphetamine (BZP) have been studied in liver microsomes from rabbit and rat using isozyme-specific inhibitors. 2. Metabolism of BZP in rat yielding phenylacetone and formaldehyde was moderately inhibited by testosterone and chloramphenicol. N-Debenzylation was thought to be P450-dependent, but all inhibitors except for a non-specific inhibitor, SKF-525A, failed to inhibit this reaction. 3. In rabbit, quinidine… CONTINUE READING
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