Molecular characterization of dihydrofolate reductase in relation to antifolate resistance in Plasmodium vivax.

Journal article

The genes encoding the wild-type and six (five single and one double) mutant dihydrofolate reductase (DHFR) domains of the human malaria parasite, Plasmodium vivax (Pv), were cloned and expressed in Escherichia coli. The catalytic activities and the kinetic parameters of the purified recombinant wild-type and the mutant PvDHFRs were determined. Generally, all the PvDHFR mutants yielded enzymes with poorer catalytic activities when compared to the wild type enzyme. The widely used antifolates,...

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Authors: Leartsakulpanich, U; Imwong, M; Pukrittayakamee, S; White, N; Snounou, G

• Publication status: Published
• Journal: Molecular and biochemical parasitology
• Volume: 119
• Issue: 1
• Pages: 63-73
• Publication date: 2002-01-01
• DOI: 10.1016/s0166-6851(01)00402-9
• EISSN: 1872-9428
• ISSN: 0166-6851
• Language: English
• Keywords: Kinetics; Potassium Chloride; Osmolar Concentration; Tetrahydrofolate Dehydrogenase; Folic Acid Antagonists; Sodium Chloride; Thermodynamics; Hydrogen-Ion Concentration; Urea; Drug Resistance; Animals; Plasmodium vivax; Catalysis