Enzymatic properties of venoms from Brazilian scorpions of Tityus genus and the neutralisation potential of therapeutical antivenoms

• DOI: 10.1016/j.toxicon.2013.02.012
• Publication Date: 2013-03-15T22:13:09Z
• Authors: Emerson J. Venancio; Fernanda C.V. Por...; Alexandre K. Kuni...; Daniela Cajado Ca...; Giselle Pidde-Que...; Denise V. Tambourgi
• Keywords: Antivenom; Scorpion Venoms; Dynorphin

Tityus scorpion stings are an important public health problem in Brazil, where the incidence of such exceeds problems caused by other venomous animals, including snakes. In this study, we have analysed specific enzymatic activities venom from Brazilian scorpions genus, i.e., serrulatus, bahiensis and stigmurus. The data presented here revealed that spp. venoms exhibited significant hyaluronidase activity but no phospholipase activity. All samples ability to hydrolyse Abz-FLRRV-EDDnp dynorphin 1-13 substrates. These were inhibited 1,10-phenanthroline not PMSF, indicating presence metalloproteinases venoms. peptidase on was partially therapeutic anti-scorpion anti-arachnidic antivenoms. Dynorphin (YGGFLRRIRPKLK) contains two scissile bonds between residues Leu-Arg Arg-Arg susceptible cleavage metallopeptidase(s). Their releases leu-enkephalin, bioactive peptide. detection metalloproteinase(s) with specificity for both degradation leu-enkephalin releasing can be mechanistic understanding hypotension bradycardia induction cases stings, whereas hyaluronidases might contribute diffusion toxins present these Furthermore, limited inhibition toxic commercial antivenoms illustrates necessity improvements current antivenom preparation.