, 2010).

Although venomics studies have revealed that metalloproteinases and serine proteinases are considered the most toxic components ( Cardoso et al., 2010), we found that B. alternatus venom showed only RG 7204 moderate proteolytic activity. Souza et al. (2000) found that B. alternatus venom contains a 55 kDa metalloproteinase, designated alternagin ( Souza et al., 2000), which has been shown to be the major component responsible for the hemorrhagic effect of this venom, despite the fact that it displayed low proteolytic activity on casein ( Gay et al., 2005). This could explain the moderate activity shown in the liquid assay and the absence of activity on the zymogram. B. alternatus showed the lowest LAAO activity. Venomics studies have demonstrated that B. alternatus venom contains five LAAO isoforms, with molecular masses ranging from 50 to 57 kDa (monomeric form), collectively accounting for 6.9% of the crude venom, and that there is a high homology between these LAAOs and those found in B. moojeni venom ( Ohler et al., 2010). Nevertheless, in the present study, the activity levels differed between those two species, a fact that might be attributable to the use of crude venom

rather than purified enzymes. Despite the relatively low overall enzymatic activity observed in our study, B. alternatus bites have often been reported to cause local tissue damage, hemorrhage, coagulation disorders, respiratory failure, renal failure, and shock ( Gay et al., 2009). On the basis of our results, we classified the enzymatic activity in the http://www.selleckchem.com/products/MDV3100.html venom of the five species evaluated as low, moderate or high (Fig. 8). Other authors have reported that venom components

are not homogeneously distributed among the various Bothrops species ( Ferreira et al., BCKDHA 1992, Francischetti et al., 1998, Hodgson and Wickramaratna, 2002, Leite et al., 1992, Moura-da-Silva et al., 1990, Moura-da-Silva et al., 1991 and Zamuner et al., 2004). However, to our knowledge, this is the first study to compare these three enzyme classes. In particular, we found few studies examining LAAO activity in Bothrops species. We have demonstrated significant variation among Bothrops species in terms of the enzymes present in the venom. According to our classification, B. moojeni venom showed the highest enzyme activity, followed by the venoms of B. neuwiedi, B jararacussu, B. jararaca, and B. alternatus. Knowledge of such differences is of great relevance to the understanding of the effects of snake bite envenomation, antiserum production, taxonomy, and venom toxicity, as well as being essential to the study of venom components as potential therapeutic targets. The authors report no declarations of interest. The authors alone are responsible for the content of this manuscript. This work do not has an Ethical Statement because all the assays were done in vitro without animal use.