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

Background:

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.

Material and methods:

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.

Results:

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 delution. Specific activity in crude venom and PI were 410-4 and 110-3 unit/mg,

respectively. Other peaks didnt show any activity of ALP enzyme.