Studying alkaline phosphatase activity in isolation fractions from Iranian snake Vipera lebetina venom

Snake venom is a complex mixture of different components including proteins and peptides that mostly has enzymatic properties. In this study, the alkaline phosphatase (ALP) activity is measured in Iranian Vipera lebetina, venomous snake on sephadex G-100 to investigate the suitability of this procedure. The method of this study is experimental. 100 mg of the crude venom of Vipera lebetina by gel filtration chromatography on sephadex G-100, that equilibrated with 20mM ammonium acetate buffer pH 7.6, was fractionated into 6 fractions. ALP enzyme activity was determined using Sulkowski et al method and using paranitrophenylphosphate as substrate. Ninety mg (approximately 79%) of crude venom of Iranian vipera lebetina is protein. Crude venom produced 6 distinct fractions. These fractions were labeled peak I to peak VI (PI-PVI), in order of their dilution. Specific activity in crude venom and PI were 4×10-4 and 1×10-3 unit/mg, respectively. Other peaks didn’t show any activity of ALP enzyme. The results indicated that the Iranian vipera lebetina venom has ALP enzyme activity and that their total activity belongs to PI. Other peaks didn’t show any ALP activity.