Identification of Fibrinolytic Activity in Iranian Vipera Lebetina Venom

Background and purpose: Vipera lebetina lives in different areas in Iran, and its venom contains a variety of proteins with coagulant and anticoagulant activities. Fibrinolytic enzymes could have a therapeutic role in dissolution of blood clots, so, this study aimed at separating the venom components of Iranian V. lebetina and detecting its anticoagulant activity. Materials and methods: In this experimental study, crude venom components were isolated by gel filtration chromatography on sephadex G-100. We investigated the endopeptidase, arginine ester hydrolase, coagulant, anticoagulant, and fibrinolytic activities in crude venom and separated fractions. Results: The crude venom was separated into five fractions (PI-PV). 200 mg of crude venom contained 187 mg protein and 11.75 mg protein was recovered from 187 mg protein used on the column. The venom showed coagulant activity at low concentrations and anticoagulant activity at high concentrations. Endopeptidase activity was detected in crude venom and all fractions except PV. Also, arginine ester hydrolase activity was seen in crude venom, PI, and PII. Fibrinolytic activity was found in crude venom and only in PIII. Conclusion: According to this study, the venom of Iranian V. lebetina has strong proteolytic activities including fibrinolytic that dissolve blood clots by lysis fibrin directly in laboratory conditions.