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Partial Characterization of Phospholipase A2 from the Erythrocytic Stage of Plasmodium berghei

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Author(s): M.A. Ibrahim | A.B. Sallau | A. Salihu | K.C. Onwube

Journal: Asian Journal of Biochemistry
ISSN 1815-9923

Volume: 6;
Issue: 2;
Start page: 208;
Date: 2011;
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Keywords: kinetics | parasite | Plasmodium berghei | Phospholipase A2 | enzyme

ABSTRACT
2 (EC. 3.1.1.4) was isolated and partially characterized from the erythrocytic stage of Plasmodium berghei (NK-65) obtained from experimentally infected mice with the objective of studying its kinetic properties and its possible role in the pathogenesis of malaria. The parasite collected by sucrose gradient centrifugation was subjected to lysis to obtain the crude phospholipase A2 which was assayed and subjected to some biochemical characterizations . The enzyme had broad pH and temperature ranges with optima of 7.5 and 37C, respectively. Initial velocity studies for the determination of kinetic parameters with L-a lecithin as substrate revealed a KM and VMAX of 0.68 mg mL-1 and 52.60 mol min-1, respectively. The P. berghei PLA2 was slightly activated by Ca2+ while Cu2+, Zn2+and Mn2+ were inhibitory to the enzyme. However, no enzyme activity was detected in the presence of Mg2+ and Hg2+. Considering the findings of this work, P. berghei can be said to contain PLA2 which has similar properties with some other parasites PLA2 and could be involved in cellular invasion and/or aneamia development during cerebral malaria.]]>
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