Venom of P. persicus dissolved in 200 mM ammonium acetate, was applied to column of Sephadex G-50 at 4 C temperature. The column was eluted in the same buffer at the flow rate of 60 ml/hr. 5 ml fractions were collected and analyzed via UV spectrometer. Fractions containing components of lower than 15 kDa were pooled and lyophilized for further purification by ion-exchange chromatography. Fractions analyzed by a C4 column and results show the presence of some peaks in each fraction. Also lyophylized crude venom in 200 mM ammonium acetate (1 mg/ml) was applied to a SEC 2000 column of HPLC. The results revealed the presence of proteins with molecular weights of less than 15 kDa. The result of our purification attemps via ion-exchange chromatography and IEF will be described.