Sallau, A.B., Ibrahim, M. A., Salihu, A. and Patrick, F.U
Phospholipase A2 (EC. 220.127.116.11) was isolated and partially characterized from the venom of Echis ocellatus. The enzyme was purified 13.5-fold with a yield of 86.69% on DEAE-Sephadex G-75 column. The PLA2 from E. ocellatus venom had broad pH and temperature ranges with optima of 7.5 and 40o C respectively. Initial velocity studies for the determination of kinetic constants with L- - lecithin as substrate revealed a Km and Vmax of 1mg/ml and 0.35 ?moles/min respectively. The enzyme activity was enhanced by Ca2+ and strongly inhibited by Mg2+ and Co2+. Cu2+ was fairly inhibitory to the enzyme. The relevance of these findings towards understanding the biochemistry of E. ocellatus envenomation and development of antivenom for E. ocellatus venom is discussed.
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