These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Characterization of Plasmodium berghei glutathione synthetase.
    Author: Sharma SK, Banyal HS.
    Journal: Parasitol Int; 2011 Sep; 60(3):321-3. PubMed ID: 21377539.
    Abstract:
    Plasmodium berghei contained 0.454±0.031 U/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 70 kDa and its Km for γ-glutamylcysteine, glycine and ATP being 0.33 mM, 8.3 mM and 0.43 mM 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.
    [Abstract] [Full Text] [Related] [New Search]