SNAKE VENOM

Abstract

Introduction: Viperidae venoms contain toxins that are direct or indirectanticoagulants that inhibit the clotting pathway, therefore increasing the risk of bleeding. Severalvenoms from the families Viperidae contain proteolytic enzymes that exercise some effect on theblood coagulation process. Snake venom toxins which delay blood coagulation are proteins orglycoprotein with molecular weights ranging from 6 kDa to 350 kDa. These factors inhibit bloodcoagulation by different mechanisms.Some snake venoms contain toxins that are direct orindirect anticoagulants, which inhibit the clotting process, thus increasing the risk of bleeding.Snake venom toxins that prolong blood coagulation are proteins or glycoproteins with molecularmasses ranging from 6 to 350 kDa. Methods: The crude venom of E. carinatuswas obtained fromthe Venomous Animals from department of microbiology Hazara University, Mansehra(Pakistan). Sephadex G-75 and DEAE-Sepharose columns were purchased from Pharmacia(Sweden). CaCl2 and PT kit was purchased from Fisher Diagnostics (USA). Protein markers wereobtained from BioRad (Hercules, USA). Other reagents and chemicals were of analytical gradefrom Fluka and Merck. Results: The anticoagulant fractions (F2C and F2D) isolated in thepresent work were characterized as proteases, since a photolytic effect was observed on casein,BAPNA or human plasma. Our results showed that the PT value significantly increased in the F2Cand F2D fractions as compared with PT value of the crude venom. Conclusions: Inthe presentstudy, the venom of Echiscarinatuswas fractionated by chromatography and each fractionevaluated by PT test. These fractions showed enzymatic activity. Their main components wereproteins of molecular weights of about 42, 50 and 79 kDa. . Further studies are needed to verifythis hypothesis.