VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Higher microsomal monooxygenase activity in chloroquine-resistant strains of malarial plasmodium as a possible cause of drug stability

   
Pankova T.G., Igonina T.M., Chekhonadskikh T.V., Salganik R.I., Rabinovich S.A.
PubMed Id: 6316663
Year: 1983  Volume: 29  Issue: 5  Pages: 63-65
Ability to hydroxylate benz(alpha)pyrene--a substrate of arylhydrocarbone hydroxylase (AHH) was distinctly increased in lysates of erythrocytes containing malarial plasmodium. Hydroxylation of benz(alpha)pyrene was inhibited by methyrapone--an inhibitor of microsomal monooxygenases. Activity of AHH was increased from 2- to 3-fold in chloroquine-resistant plasmodium strains as compared with the drug-sensitive strains. Resistance of Plasmodium berghei to chloroquine appears to involve an activation of the monooxygenases system in the parasite.
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Pankova, T. G., Igonina, T. M., Chekhonadskikh, T. V., Salganik, R. I., Rabinovich, S. A. (1983). Higher microsomal monooxygenase activity in chloroquine-resistant strains of malarial plasmodium as a possible cause of drug stability. Voprosy Meditsinskoi Khimii, 29(5), 63-65.
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