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Int. Journal of Clinical Pharmacology and Therapeutics, Volume 43 - July (327 - 334)

Rate-limiting biotransformation of triamterene is mediated by CYP1A2
U. Fuhr, S. Kober, M. Zaigler, E. Mutschler, H. Spahn-Langguth
1 Institute for Pharmacology, Clinical Pharmacology, University of Cologne, 2 Department of Pharmacology, Biocenter Niederursel N 2  6  0 , Frankfurt/Main, and 3 Department of Pharmaceutical Chemistry, Martin Luther University Halle-Wittenberg, Halle/Saale, German

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DOI 10.5414/CPP43327

Abstract

Objective: Triamterene (TA), a potassium-sparing diuretic, is extensively metabolized by hydroxylation in 4?-position and subsequent conjugation by cytosolic sulfotransferases. To identify the cytochrome P450 enzyme(s) catalyzing hydroxylation of triamterene (the rate-limiting step in the formation of the sulfate ester (STA)), in vitro incubation studies were performed with human liver microsomes. Methods: Initial rates of TA hydroxylation (0 ? 300

Author Details

Authors

Departments

  • 1 Institute for Pharmacology, Clinical Pharmacology, University of Cologne,
  • 2 Department of Pharmacology, Biocenter Niederursel N
  • 2 
  • 6 
  • 0 , Frankfurt/Main, and
  • 3 Department of Pharmaceutical Chemistry, Martin Luther University Halle-Wittenberg, Halle/Saale, German

Address

Prof. Dr. H. Spahn-Langguth Spessartstra
Email: [email protected]

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Citation

U. Fuhr, S. Kober, M. Zaigler, E. Mutschler and H. Spahn-Langguth. Rate-limiting biotransformation of triamterene is mediated by CYP1A2. 2005; 43: 327-334. doi: 10.5414/CPP43327.

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