Amy Hamaker provided the

English editing of the manuscript. “
“Snake venoms are especially interesting since they contain high concentrations of proteins and peptides that are chemically and structurally similar to their mammalian counterparts and which, upon envenomation, trigger a wide spectrum of secondary effects that interfere with the maintenance and functioning of essential biological functions such as hemostasis, platelet aggregation and lipid digestion (Lewis and Gutmann, 2004) and thus, some of these proteins have been commercialized as diagnostic and clinical tools (Lewis and Garcia, 2003). Crotalidae and Viperidae proteinases (Kang et al., 2011, Serrano, 2013 and Takeda et al., 2012) are synthesized by the exocrine venom glands and are either metalloproteinases or serine proteinases and catalyze the cleavage of covalent peptide bonds in proteins. Snake venom serine proteinases (SVSPs) likely originated Selleckchem Ipilimumab as digestive enzymes and subsequently evolved by gene duplication

and sequence modifications to serve other functions. SVSPs encountered in Bothrops venoms Ion Channel Ligand Library manufacturer are in many aspects functionally similar to endogenous blood clotting enzymes and they interfere with the maintenance and regulation of the blood coagulation cascade by proteolytically cleaving specific bonds and activating proteins involved in blood coagulation, fibrinolysis, and platelet aggregation and also in the proteolytic degradation of cells resulting in an imbalance of the hemostatic system (Kini, 2005 and Serrano and Maroun, 2005). SVSPs are encountered in the venoms of a number of Bothrops species, for example two SVSPs, Bhalternin and Balterobin have been isolated from Bothrops alternatus venom ( Costa Jde et al., 2010 and Smolka et al., 1998), MSP 1, MSP 2, MMO3 and Interleukin-3 receptor Batroxobin have been isolated from Bothrops moojeni venom ( Oliveira et al., 1999, Serrano et al., 1993 and Stocker and Barlow, 1976) and serine proteinases have been identified in the venoms of Bothrops jararacussu ( Bortoleto et al., 2002 and Hill-Eubanks et al., 1989), Bothrops

atrox ( Itoh et al., 1987, Kirby et al., 1979 and Petretski et al., 2000), Bothrops jararaca ( Mandelbaum and Henriques, 1964, Nishida et al., 1994 and Serrano et al., 1995). The amino acid sequence homology shared between the SVSPs mentioned above is approximately 65%, however, the homology exhibited by these enzymes with mammalian serine proteinases such as thrombin and trypsin, ranges from 30% to 40%. SVSPs are structurally similar to the chymotrypsin family of proteinases, consist of approximately 232 amino acids and are made up of two homologous domains each containing a six-stranded β-barrel, the overall structures and the relative orientations of the three amino acids forming the catalytic triad, His57-Asp102-Ser195 are strictly conserved ( Barrett and Rawlings, 1995 and de Giuseppe et al., 2013).