Catalytic activity of three variants (Ile, Leu, and Thr) at amino acid residue 359 in human CYP2C9 gene and simultaneous detection using single-strand conformation polymorphism analysis.

@article{Ieiri2000CatalyticAO,
  title={Catalytic activity of three variants (Ile, Leu, and Thr) at amino acid residue 359 in human CYP2C9 gene and simultaneous detection using single-strand conformation polymorphism analysis.},
  author={Ichiro Ieiri and Hitoshi Tainaka and Toshisuke Morita and A. Hadama and Kiminori Mamiya and Masatoshi Hayashibara and Hideaki Ninomiya and Shigeru Ohmori and Mitsukazu Kitada and Norimichi Tashiro and Shun Higuchi and Kenji Otsubo},
  journal={Therapeutic drug monitoring},
  year={2000},
  volume={22 3},
  pages={
          237-44
        }
}
This study evaluated the catalytic activity of three variants (Ile, Leu, and Thr) at codon 359 of CYP2C9 enzymes expressed in a yeast cDNA expression system, and then established single-strand conformation polymorphism (PCR-SSCP) analysis for simultaneous detection as a screening method. Diclofenac was used for the in vitro experiment, and its hydroxy metabolite (4'-hydroxydiclofenac) was measured by HPLC. To discuss the in vivo effect of the Thr359 variant on the pharmacokinetics of phenytoin… CONTINUE READING
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