Characterization of Plasmodium berghei glutathione synthetase
2011
Sharma, S.K. | Banyal, H.S.
Plasmodium berghei contained 0.454±0.031U/mg of glutathione synthetyase (GS). GS was purified using solid ammonium sulfate and Sephadex G-200 from P. berghei infected mouse erythrocytes. SDS-PAGE showed purified GS as a single band protein of 70kDa and its Km for γ-glutamylcysteine, glycine and ATP being 0.33mM, 8.3mM and 0.43mM respectively with noncompetitive inhibition by GSH. The malaria parasite enzyme was optimally active at 37°C and pH 8.0–8.5. Heavy metals significantly inhibited parasite GS activity.
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