Aim - to search fibrinogenolytic enzymes among protein components of Vipera renardi snake venom. Methods - Venom of V. renardi as the lyophilized powder was supplied by Trypillia serpentarium. It was dissolved in 0,05 M Tris-HCl buffer pH 8,3 and fractionated on Superdex G-75 using FPLC system Acta Prime. Peaks were tested for their ability to directly cleave fibrinogen. Hydrolytic products were analyzed by SDS-PAGE. Enzyme-electrophoresis with fibrinogen co-polymerized in 12 % polyacrylamide gel was used for the identification of protein that can cleave fibrinogen. Venom of V. renardi was fractionated on 4 fractions using size-exclusion chromatography. SDS-PAGE of fibrinogen hydrolysis products showed the presence of fibrinogen-specific protease in the 1st and 2nd fractions of venom. 2<^>nd fraction was much more active and according to the data of enzyme electrophoresis contained protease with molecular mass 25 kDa. Conclusions: fractionation of V. renardi snake venom allowed to detect a protease with apparent molecular mass 25 kDa that can cleave fibrinogen molecule.

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