Snake venom is a complex mixture of toxins and enzymes showing several activities on the biological system. They are rich in proteolitic enzymes with specific biological activities, such as hemorrhagic, coagulation disorders, necroses and inflammation. The just mentioned proteolitic enzymes, wich are named serine proteases and metalloproteases, affect the hemostatic system by degrading coagulation factors, activating specific factors in coagulation cascade acting on the fibrinogenolysis and/or fibrinolysis or degrading proteins in the endothelial surface. The presence of components in animal plasma, which confer resistance to several snake venoms have been reported. The goal of this work is to isolate and characterize biochemical and functionally a protease inhibitor present in the plasma of Bothrops alternatus, and to understand the action neutralizing mechanism of the proteases present in Bothrops venom (serine proteases and metalloproteases of B. atrox and B. jararacussu). Therefore, new information related to these inhibitors will be known, in the tentative of a better understanding of their use as a new therapeutic model with antivenom action in the neutralization of different kind of proteases, in the supplementation of the conventional serum therapy and in the molecular interaction with these toxins in order to comprehend the action mechanisms involving these multifunctional enzymes.
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