- 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,...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/s0166-6851(01)00402-9
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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
- Copyright date:
- 2002
Journal article
Molecular characterization of dihydrofolate reductase in relation to antifolate resistance in Plasmodium vivax.
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