Purification and preliminary structure of a potent platelet aggregating glycoprotein isolated from the venom of Crotalus durissus cascavella.

A very potent platelet-aggregating glycoprotein, convulxin, was purified from the venom of Crotalus durissus cascavella by gel filtration on Sephadex G75 and by adsorption to Sepharose 4B gel. The apparent molecular weights of the native protein were 78400 and 60000 daltons determined by SDS electrophoresis and by gel filtration under denaturating conditions, respectively. Under the same conditions, the apparent molecular weights of the reduced protein were 13000 and 12000 respectively. These discrepancies are due to the presence of a carbohydrate moiety in the molecule. Analysis for carbohydrates showed the presence of around 4,8% sugars. Convulxin is built up of closely similar subunits linked by disulfide brides and is devoid of free sulfhydryl groups.