Phospholipase A2 activity in crude venom and fractions separated from Iranian Vipera Lebetina venom

Snake venoms are complex mixtures containing many different biologically active proteins and peptides. Vipera lebetina is one of the most poisonous snakes in Iran. The aim of the present study was to test the existence of phospholipaseA2 activity in the crude venom of the snake. One hundred mg of the crude venom of Vipera lebetina was resolved into five fractions using gel filtration chromatography on sephadex G-100, equilibrated with 20mM ammonium acetate buffer pH 6.8. Protein concentration of crude venom and fractions was assayed by Bovin serum albumin as a standard. Phospholipase A2 (PLA2) activity was determined using suspension of egg yolk as substrate. The preliminary results showed that the 89% of lyophilized venom was protein. Crude venom produced five fractions. These fractions were labeled as peak I to peak V (PI-P V), in order of their elution. Specific activity in crude venom, peak I, peak II and peak III were 2.25, 0.078, 2.76 and 1.04 U/mg. High PLA2 activity was detected in crude venom, which was more prominent in peak II and was not considerable in peak I of the fractions.