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

Abstract:

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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Publication status:
Published

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Authors


Leartsakulpanich, U More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Thailand/Laos MOP
Pukrittayakamee, S More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Thailand/Laos MOP
Snounou, G More by this author
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Journal:
Molecular and biochemical parasitology
Volume:
119
Issue:
1
Pages:
63-73
Publication date:
2002-01-05
DOI:
EISSN:
1872-9428
ISSN:
0166-6851
URN:
uuid:bbaa2f8b-c6d5-4ca9-9b00-29385940146b
Source identifiers:
38113
Local pid:
pubs:38113

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