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Purification Characterization and Inhibition Studies on Phospholipase C From Opisthacanthus Capensis (Black Scorpion) Venom

Yahaya Tijani, Hassan Zanna, Aji Bukar Sadiq, Babagana Modu, Madu Adamu Gadaka, Binta Baba Shehu, Ali Ali Abdulrahman.




Abstract

Phospholipase C from Opisthacanthus capensis venom was partially purified and characterized. The enzyme was purified 105.2 fold with an overall yield of 13% using various steps involving ammonium sulphate precipitation, protamine sulphate treatment, sephadex G-75 fractionation and DE-52 anion exchange chromatography. The purified enzyme was homogeneous by the criteria of SDS polyacrylamide gel electrophoresis with a molecular weight of 29 kDa. The phospholipase C has pH and temperature optima of 7.2 and 600C, respectively with activation energy of 25KJ/mol and t1/2 of 1.50 hr. Initial velocity studies on Opisthacanthus capensis venom phospholipase C revealed a KM of 0.02 mM and Vmax of 0.015 µmol/min respectively. Studies on the effect of pH on KM and Vmax gave PKa1 of 6.9 and PKa2 of 7.4 with enthalpy of ionization of 20 KJ/mol suggesting histidine in the active site. The enzyme was positively modulated by Mg2+, Zn2+ and Ca2+ and negatively by Fe2+. While Hg2+ produced complete inhibition. Various concentrations of leaf aqueous extract of Momordica charantia also inhibited the activity of Opisthacanthus capensis venom phospholipase C in vitro with a display of competitive

Key words: : Phospholipase C; Opisthacanthus capensis; Momordica charantia; venom






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