Glutathione and peroxide metabolism in malaria-parasitized erythrocytes.

Abstract

The glutathione metabolism of Plasmodium falciparum, P. vinckei and P. berghei has been investigated. Human erythrocytes with low glutathione reductase and synthetase activity are still capable of harbouring P. falciparum. Both enzymes have been demonstrated in Plasmodium spp. Moreover, evidence is given for a selenium-independent glutathione peroxidase in malaria parasites.

• Authors: B Fritsch, A Dieckmann, B Menz, E Hempelmann, K G Fritsch, G Fritsch, A Jung
• Journal: Parasitology research (Parasitol Res) Vol. 73 Issue 6 Pg. 515-7 ( 1987) ISSN: 0932-0113 [Print] Germany
• PMID: 3321043 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Peroxides
• Glutathione Peroxidase
• Glutathione Reductase
• Glutathione Synthase
• Glutathione
• Selenium

Topics

• Animals
• Erythrocytes (enzymology, metabolism, parasitology)
• Glutathione (metabolism)
• Glutathione Peroxidase (metabolism)
• Glutathione Reductase (metabolism)
• Glutathione Synthase (metabolism)
• Humans
• Mice
• Oxidation-Reduction
• Peroxides (metabolism)
• Plasmodium (enzymology, metabolism)
• Plasmodium berghei (enzymology, metabolism)
• Plasmodium falciparum (enzymology, metabolism)
• Selenium (blood)
• Substrate Specificity