jararaca ( Saguchi et al., 2005) revealed 100% identity. Several serine proteinases of molecular masses of about 30 kDa share significant homology with HS114 (a cDNA that encodes an SVSP of B. jararaca) ( Saguchi et al., 2005). According to their

specificity for cleaving fibrinogen chains, the serine proteinases have been classified as α, β and γ-fibrinogenases. SVSPs preferentially cleave the Bβ-chain ( Herzig et al., 1970, Markland, 1998, Menaldo et al., 2012 and Vieira Selleckchem HDAC inhibitor et al., 2004), however, some of them such as Batroxobin from B. atrox, Bothrombin from B. jararaca, Bhalternin from B. alternatus ( Costa Jde et al., 2010, Sant’ Ana et al., 2008 and Stocker and Barlow, 1976) also cleave the Aα-chain. The SPBA enzyme isolated from B. alternatus cleaved the Bβ-chain and was also able to degrade the Aα-chain, similar to thrombin and some SVSPs, such as Jararacussin-I from B. jararacussu ( Zaganelli et al., 1996), MOO3 from B. moojeni ( Oliveira et al., 1999) and BpirSP41 from Bothrops pirajai ( Menaldo et al., 2012). Based on its enzymatic, structural and biochemical characteristics, it can be inferred that SPBA is a serine proteinase with significant proteolytic BI 2536 supplier activity on casein and fibrinogen. However, unlike most venom serine proteinases studied (Bortoleto et al., 2002, Costa

Jde et al., 2010, Perez et al., 2008 and Sant’ Ana et al., 2008), SPBA showed low coagulant activity, with an MCD of 6 ug. Many proteinases have been purified and characterized from B. moojeni, for example, the clotting enzyme Batroxobin ( Lochnit and Geyer, 1995 and Stocker and Barlow, 1976),

three serine proteinases, MSP1, MSP2 ( Serrano et al., 1993) and MOO3 ( Oliveira et al., 1999) and some metalloproteinases, such as BmMP-III ( Ullah et al., 2012) and Moojenin ( de from Morais et al., 2012). Through a combination of three chromatographic steps, two serine proteinases from the venom of B. moojeni have been isolated in this study. Serrano et al. (1993) isolated a serine proteinase from B. moojeni venom named MSP1, that displayed two bands around 32 kDa and 34 kDa. However, unlike the MSP1 which presents only traces of coagulant activity, the serine proteinases (BM-IIB32 kDa + BM-IIB34 kDa protein) from B. moojeni isolated in this study induces high blood clotting in vitro with an MCD of 1 ug. Other potent coagulant enzymes from Bothrops snake venom presented MCD higher than the enzyme from B. moojeni isolated in this study, 4.1 ug ( Perez et al., 2008) and 3.5 ug ( Menaldo et al., 2012). This capacity of both enzymes BM-IIB32 kDa and BM-IIB34 kDa to promote clotting in vitro, can be an indication of their ability to form soluble, non-cross-linked clots in vivo, thereby highlighting their clinical application as defibrinogenating agents. High partial sequence identity (63–100%) was observed between the two enzymes isolated from B. moojeni and the Bothrops serine proteinase venoms compared.