neuwiedi and B. moojeni showed significantly higher LAAO activities, followed by that of B. jararaca and B. jararacussu. B. alternatus venom showed significantly lower LAAO activity. In order to compare the various Bothrops venoms, in terms of their protein profiles, the venoms were submitted to electrophoresis under non-reducing conditions. The results of the SDS-PAGE analysis are shown in Fig. 4. Despite the fact that several venoms had some bands in common, their overall profiles showed substantial differences, except in the case of B. moojeni

versus B. neuwiedi. The presence of PLA2 in the venoms was analyzed by an egg yolk zymogram. All venoms displayed a clear zone at approximately 15 kDa, which corresponds to PLA2 activity against lecithin on the gel (Fig. 5). Although equal amounts of venom were used, different patterns of clear zones were observed. This observation can be explained by differences in the activity level of each enzyme and its concentration

PD0325901 mouse in the venom. These findings are in accordance with the results obtained in the hemolytic assay. The presence of proteinases in the venoms was confirmed by the appearance of clear zones against the blue background on the casein zymogram (Fig. 6). B. jararaca venom showed intense casein degradation in the 25–28 kDa range, while B. neuwiedi venom showed intense degradation at 28 to 30 kDA. The venoms of B. jararacussu and B. moojeni showed a lower degradation profile at approximately 30 kDa, while no clear Selleckchem Epacadostat zone was observed for B. alternatus venom. Although all of the venoms showed proteinase activity, as indicated in Fig. 2, only the venoms of B. jararacussu and B. moojeni were similar in their patterns of casein degradation. The venoms also showed LAAO activity, as confirmed by the presence of yellowish bands in the OPD zymogram (Fig. 7),

nevertheless, their molecular mass was variable. B. jararaca venom showed the most intense yellowish band, around 97 kDa. While B. jararacussu and B. moojeni venoms showed similar band profiles at approximately 84 and 82 kDa, respectively. B. neuwiedi venom DOK2 was unique in that it displayed two yellow bands. One intense band of 75 kDa and another, less intense band of 119 kDa were detected. B. alternatus venom displayed the enzyme at approximately 107 kDa. Proteinases and PLA2s are considered the major toxic compounds in almost all snake venoms, although other enzymes also contribute to the toxicity (Correa-Netto et al., 2010 and Serrano et al., 2005). LAAO is also an important enzyme present in the venom of pit vipers, however, it accounts for about 0.5% of the total toxin transcripts from the venom glands, a small percentage when compared with the 53.1% and 28.5% reported for metalloproteinases and serine proteinases, respectively (Cidade et al., 2006). In the present study, we evaluated the PLA2, proteolytic, and LAAO activities of the venoms of five different Bothrops species: B. jararaca, B. jararacussu, B. moojeni, B. neuwiedi, and B.