It has shown that injection of tityustoxin (TsTX) induced pulmonary edema in rats ( Freire-Maia et al., 1978). TsTX ( Gomez and Diniz, 1966) is a heterogeneous

fraction from T. serrulatus venom ( Arantes et al., 1992), including the α-type toxin among its components. The α-toxin Aah II isolated from the venom of an Old World scorpion, Androctonus australis Hector, was also able to induce interstitial lung MAPK Inhibitor Library cost edema in rats ( Sami-Merah et al., 2008). In the interval of 36–40% acetonitrile, Ts-MG venom presented a greater number of peptides than Ts-DF venom, suggesting a greater diversity of NaScTxs in the former, which may explain the higher toxicity of Ts-MG venom. Indeed, Ts-MG venom possesses 9 assumed selleck chemical NaScTxs while Ts-DF has 4 ( Table 5). Interestingly, Ts-DF has the all previously described T. serrulatus NaScTxs, including the α-toxins, whose edematogenic activity has been attributed to. The inability to induce acute pulmonary edema of Ts-DF venom

can be explained by either smaller concentration of these toxins, or by the smaller number of supposed NaScTxs that could act synergistically in the induction of the envenoming signs. Ts-DF venom presents higher D values than Ts-MG venom in the last 10 min of elution time (50–60% of acetonitrile). Most high molecular mass components (>9000 Da) elute in acetonitrile percentages greater than 40% and correspond to proteins, such as those from Tityus species that have been assigned to lysozyme, proteases or hyaluronidase enzymes ( Batista

et al., 2007 and Cologna et al., 2009). The fingerprinting analysis conducted with Ts-MG venom shows there are many peptides greater than 9000 Da eluting in the last 20 min of fractioning, and their number are smaller in Ts-DF venom ( Fig. 5). In fact, in T. serrulatus venom from Minas Gerais was previously described a hyaluronidase Afatinib supplier (P85841) whose full amino acid sequence is yet to be determined. It is known that these proteins lack importance and direct action in the poisoning, but have fundamental action in the distribution of neurotoxins in whole organism, because promote random hydrolysis of (1–>4)-linkages between N-acetyl-beta-D-glucosamine and d-glucuronate residues in hyaluronate. Hyaluronidase belongs to the glycosyl hydrolase 56 family ( Richardson et al., 2008). Recently, a metalloprotease named antarease (P86392) was identified in T. serrulatus venom from Minas Gerais, a protein with approximately 25,500 ± 100 Da, which elutes at 60% acetonitrile, and has proteolytic activity ( Fletcher et al., 2010). Probably due to fractionation methodology used in the present study, it was not possible to identify this enzyme in the venoms studied.