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Het cytochroom P450 enzymsysteem: wat is de relevantie voor de praktijk? Deel II, interacties.

Published online by Cambridge University Press:  18 September 2015

D.J. Touw ,
W.M.A. Verhoeven  and
J.B.G.M. Noten
D.J. Touw
Affiliation:
Apotheek, Academisch ziekenhuis Vrije Universiteit
W.M.A. Verhoeven
Affiliation:
Zenuwarts, Vincent van Gogh Instituut voor Geestelijke, Gezondheid
J.B.G.M. Noten
Affiliation:
Stichting Ziekenhuisapotheek en Klinisch Laboratorium Venray
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Summary

In man a great interindividual variability exists in the oxidative capacity to metabolize drugs. A major factor contributing to this phenomenon is the genetically determined hydroxyla-tion-capacity of the cytochrome P450 enzyme system. The cytochrome P450 system comprises of several isozymes. For several isozymes (CYP2D6, CYP2C) a genetically based hydroxylation capacity has been demonstrated. A frequency distribution of the clearance shows a bimodal distribution with poor and extensive metabolizers. Applying standard dosing schemes of the drugs that are predominantly metabolised by these isozymes, a considerable number of patients will be intoxicated because of poor metabolism. In general, cytochrome P450 capacity is limited and substrate-affinity is high. Henceforth cytochrome P450 isozymes are likely targets for pharmacokinetic interactions.

Keywords

Cytochrome P450genetic polymorfismhydroxylation capacitymetabolismdrug metabolismliver enzymessubstrate affinityCytochroom P450genetisch polymorfismehydroxyleringscapaciteitmetabolismegeneesmiddelmetabolismelever enzymensubstraat affiniteit
Type
Research Article
Information
Acta Neuropsychiatrica , Volume 10 , Issue 3 , September 1998 , pp. 58 - 62
Copyright
Copyright © Scandinavian College of Neuropsychopharmacology 1998

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References

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