Lack of relationship between quinidine pharmacokinetics and the sparteine oxidation polymorphism

Eur J Clin Pharmacol. 1995;48(6):501-4. doi: 10.1007/BF00194341.


Quinidine is a very potent inhibitor of CYP2D6, but the role of the enzyme in the biotransformation of quinidine has only been investigated in a single in vitro study and in two small in vivo experiments, with contradictory results. The present investigation was designed to present definite evaluation of whether quinidine is metabolised by CYP2D6. Eight poor metabolizers (PM) and 8 extensive metabolizers (EM) of sparteine each took one oral dose of 200 mg quinidine. In the EM, the total clearance, the clearance via 3-hydroxylation and the clearance via N-oxidation, were 33, 3.7 and 0.23 l.h-1, respectively. In the PM, the corresponding values were 29, 3.1 and 0.18 l.h-1, respectively. There were no statistically significant differences between EM and PM in any of these pharmacokinetic parameters. It is concluded that CYP2D6 is not an important enzyme for the oxidation of quinidine.

Publication types

  • Clinical Trial
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Antimalarials / blood
  • Antimalarials / pharmacokinetics*
  • Biotransformation
  • Cytochrome P-450 CYP2D6
  • Cytochrome P-450 Enzyme System / metabolism
  • Female
  • Half-Life
  • Humans
  • Male
  • Mixed Function Oxygenases / metabolism
  • Oxidation-Reduction
  • Phenotype
  • Polymorphism, Genetic
  • Quinidine / analogs & derivatives
  • Quinidine / analysis
  • Quinidine / blood
  • Quinidine / pharmacokinetics*
  • Sparteine / metabolism*


  • Antimalarials
  • Sparteine
  • hydroquinidine
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • Cytochrome P-450 CYP2D6
  • Quinidine