Malarial parasite metabolism: The glutamic acid dehydrogenase of Plasmodium berghei

Langer, Bernhardt W.; Phisphumvidhi, Pirom; Jiampermpoon, Duangduen

doi:10.1016/0014-4894(70)90100-1

Cited by 12 publications

(2 citation statements)

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“…Babesia possesses a GluDH activity. This activity is of the same order as that observed in Plasmodium (Langer et al 1970;Vander Jagt et al 1989). This enzyme is capable of providing reduced nicotinamide adenine dinucleotide phosphate (NADPH), which is necessary both for regeneration of the reduced glutathione and for maintenance of the catalase in its active form (Hillar et al 1994).…”

Section: Resultssupporting

confidence: 68%

Babesia hylomysci and B. divergens : presence of antioxidant enzymes destroying hydrogen peroxide

Clarebout

Gamain

Précigout³

et al. 1997

Parasitology Research

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Catalase and glutathione peroxidase (Gpx), two enzymes destroying hydrogen peroxide, were reported in two Babesia species: B. divergens cultivated in vitro and B. hylomysci obtained in vivo. On the use of specific substrate and inhibitor, we confirmed that the Gpx activity detected was selenium-dependent. Moreover, the two Babesia species contain glutamate dehydrogenase activity. This enzyme is capable of providing to the cell the reduced nicotinamide adenine dinucleotide phosphate (NADPH) necessary for regeneration of the reduced glutathione. Gpx activity is weaker in B. divergens than in B. hylomysci and seems to be compensated by higher levels of catalase activity. Such a balance between the two enzymes may depend on the selenium concentration available for the parasite.

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