A Novel Fast and Efficient Approach to Purify the Thrombin-like Enzyme from Two <i>Bothrops</i>-genus Snake Venoms

Snake venoms are important sources of complex substances with a variety pharmacological activities. Among them serine proteinases (SVSPs) have effects on the hemostatic system influencing hemodynamic human or animal blood. Bothrops genus-snake rich in thrombin-like enzyme, type SVSPs, great interest to produce medicine. Therefore, aim this work was describe rapid, only two-step chromatographic-procedure developed perform faster purification SVSPs from alternatus and moojeni venoms. As result, two groups respectively BaIII-4 - 8 BmIII-2 5, were isolated their molecular masses estimated by mass spectrometry SDS-PAGE under denaturing conditions. The SVTLEs B. (BaIII-3 8) (BmIII-2 5) fractions displayed apparent around 30-40 kDa which closely relates other species, as well amino acid partial sequence triptych ions. Analysis alignment residue sequences N-terminal proteins revealed high level identity SVTLEs. These enzymes coagulated plasma showed fibrinogenolytic activity can be considered α-fibrinogenase mainly due fact that they hydrolyze Aα chain fibrinogen. SVTLE greater than those isolated. This new alternative approach more economical traditional process currently used. Faster improved extraction yield provide insights into these including use candidate molecule production drugs.