, 2010). Most of the enzymes are likely to be glycoproteins with the number and position of N- or O-glycosylation sites differing from one enzyme to another (Serrano and Maroun, 2005). Metalloproteinases are enzymes that depend on metal ions to be active. Snake venom metalloproteinases are associated with hemorrhage, myonecrosis, skin damage, and reactions manifesting as inflammation or edema (Gomes et al., 2011, Gutierrez et al., 2009 and Teixeira et al., 2005). Members of the PLA2 family are calcium-dependent enzymes

that catalyze BMS-754807 in vivo the hydrolysis of the sn-2 ester bond of phosphoglycerides, leading to the formation of free fatty acids and lysophospholipids (da Silva Cunha et al., 2011 and Fuly et al., 2000). In many types of snake venom, the Venetoclax supplier majority of the toxic components are composed of PLA2 isoforms. In addition to their role in prey digestion, they impair certain major physiological functions and can cause presynaptic neurotoxicity and myotoxicity, as well as inhibit coagulation and platelet aggregation. They are also involved in the development of convulsions, inflammation, hypotension, hemolysis,

and hemorrhage, potentially contributing to the development of edema (Campos et al., 2009, Fortes-Dias et al., 1999, Fuly et al., 2007, Huang et al., 1997, Leiguez et al., and Moreira et al.,). In the venom of various snakes, members of the LAAO family also contribute to toxicity. The LAAOs catalyze the oxidative deamination of specific l-amino acids to produce the corresponding alpha-keto acid, hydrogen peroxide, and ammonia. An LAAO typically presents as a homodimeric acidic glycoprotein with a flavin cofactor. Studies have shown that snake venom LAAOs are involved in the apoptosis of various cell lines, such as vascular endothelial cells, which could contribute to prolonged bleeding after a snake bite (Alves et al., 2008 and Suhr and Kim, 1996). In addition, LAAOs can inhibit platelet aggregation, thereby having an anticoagulant effect (Sakurai et al., 2003).

Bothrops envenomation is characterized by cardiovascular effects, proteolytic activity with a pronounced local effect, Bay 11-7085 myonecrosis, hemorrhage, and edema, all of which are attributable to the synergism of these enzymes, together with the effects of other components ( Gutierrez et al., 2009, Machado et al., 2010 and Mebs and Ownby, 1990). In Brazil, Bothrops antivenom is currently produced at the Butantan Institute in Sao Paulo. The antivenom is prepared by hyper-immunizing healthy horses using the venom of five species: B. jararaca; B. jararacussu; B. alternatus; B. moojeni; and B. neuwiedi ( Furtado et al., 2010). Multiple species are used because there are differences among the species regarding the components of the venom ( Furtado et al., 2010, Neiva et al., 2009 and Nunez et al., 2009).