ArticleParasitology research2007
Purification and biochemical characterization of cytosolic glutathione-S-transferase from malarial parasites Plasmodium yoelii.
Article in Parasitology research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- The role of antioxidants treatment on the pathogenesis of malarial infections: a review.Parasitology research · 2014Review
- The serological diagnosis of human clonorchiasis by time-resolved fluoroimmunoassay based on GST2-specific IgG4 detection.Parasitology research · 2014Article
- Virtual screening and in vitro assay of potential drug like inhibitors from spices against glutathione-S-transferase of filarial nematodes.Journal of molecular modeling · 2012Article
- Biochemical studies on glutathione S-transferase from the bovine filarial worm Setaria digitata.Parasitology research · 2011Article
- In vitro antifilarial activity of glutathione S-transferase inhibitors.Parasitology research · 2009Article
- Inhibition of glutathione-S-transferase from Plasmodium yoelii by protoporphyrin IX, cibacron blue and menadione: implications and therapeutic benefits.Parasitology research · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Glutathione (GSH) metabolism represents a potential target for antiparasitic drug design. Glutathione-S-transferase (GST), an important enzyme of the GSH cycle, is considered to be an essential detoxification enzyme in parasitic species. Soluble GST from rodent malarial parasites Plasmodium yoelii was purified to homogeneity using a combination of salt precipitation, affinity chromatography on GSH-sepharose 6B and ultrafiltration. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed a single band and activity staining was also detected on PAGE gels. Kinetic studies on the purified enzyme revealed significant differences between the parasitic and mammalian enzymes. The purified enzyme exhibited an optimum pH of 8.2 and K (m) values of 0.2+/-0.213 and 3.3+/-0.056 mM with respect to co-substrate GSH and substrate 1-chloro-2, 4-dinitrobenzene (CDNB), respectively. Hemin, the known mammalian GST inhibitor was found to be a potent inhibitor of P. yoelii GST, with a K (i) of 4.0 microM.
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