Dissociation of catalytic activity and neurotoxicity of a basic phospholipase A2 from Russell's viper (Vipera russelli) venom.

A neurotoxic phospholipase A2, VRV PL-V was purified from Vipera russelli venom in a single step by CM-Sephadex C-25 column chromatography. VRV PL-V is a basic PLA2 with a mol. wt of approximately 10,000. The lethal potency of VRV PL-V was greater than that of the crude V. russelli venom. VRV PL-V showed anticoagulant activity and induced edema in the foot pad of the mouse. VRV PL-V undergoes aggregation at pH 4.8. The size of the aggregate increased as the temperature at which the enzyme was incubated was raised. A highly aggregated form with a mol. wt of 53,100 was formed at 96 degrees C. This aggregate showed a two-fold increase in its catalytic activity, while its neurotoxic activity disappeared. The aggregate also showed a significant increase in its anticoagulant activity when compared to the monomeric form. Edema-inducing activity decreased upon association to higher molecular form.