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Bp-13 PLA2: Purification and Neuromuscular Activity of a New Asp49 Toxin Isolated from Bothrops pauloensis Snake Venom.
Sucasaca-Monzón, Georgina; Randazzo-Moura, Priscila; Rocha, Thalita; Torres-Huaco, Frank Denis; Vilca-Quispe, Augusto; Ponce-Soto, Luis Alberto; Marangoni, Sérgio; da Cruz-Höfling, Maria Alice; Rodrigues-Simioni, Léa.
Afiliación
  • Sucasaca-Monzón G; Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas (UNICAMP), 13083-881 Campinas, SP, Brazil.
  • Randazzo-Moura P; Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas (UNICAMP), 13083-881 Campinas, SP, Brazil.
  • Rocha T; Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), 13083-365 Campinas, SP, Brazil ; Multidisciplinary Research Laboratory, São Francisco University, 12916-350 Bragança Paulista, SP, Brazil.
  • Torres-Huaco FD; Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), 13083-365 Campinas, SP, Brazil.
  • Vilca-Quispe A; Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), 13083-365 Campinas, SP, Brazil.
  • Ponce-Soto LA; Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), 13083-365 Campinas, SP, Brazil.
  • Marangoni S; Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), 13083-365 Campinas, SP, Brazil.
  • da Cruz-Höfling MA; Department of Biochemistry and Tissue Biology, Institute of Biology, State University of Campinas (UNICAMP), 13083-365 Campinas, SP, Brazil.
  • Rodrigues-Simioni L; Department of Pharmacology, Faculty of Medical Sciences, State University of Campinas (UNICAMP), 13083-881 Campinas, SP, Brazil.
Biochem Res Int ; 2015: 826059, 2015.
Article en En | MEDLINE | ID: mdl-25789175
A new PLA2 (Bp-13) was purified from Bothrops pauloensis snake venom after a single chromatographic step of RP-HPLC on µ-Bondapak C-18. Amino acid analysis showed a high content of hydrophobic and basic amino acids and 14 half-cysteine residues. The N-terminal sequence showed a high degree of homology with basic Asp49 PLA2 myotoxins from other Bothrops venoms. Bp-13 showed allosteric enzymatic behavior and maximal activity at pH 8.1, 36°-45°C. Full Bp-13 PLA2 activity required Ca(2+); its PLA2 activity was inhibited by Mg(2+), Mn(2+), Sr(2+), and Cd(2+) in the presence and absence of 1 mM Ca(2+). In the mouse phrenic nerve-diaphragm (PND) preparation, the time for 50% paralysis was concentration-dependent (P < 0.05). Both the replacement of Ca(2+) by Sr(2+) and temperature lowering (24°C) inhibited the Bp-13 PLA2-induced twitch-tension blockade. Bp-13 PLA2 inhibited the contractile response to direct electrical stimulation in curarized mouse PND preparation corroborating its contracture effect. In biventer cervicis preparations, Bp-13 induced irreversible twitch-tension blockade and the KCl evoked contracture was partially, but significantly, inhibited (P > 0.05). The main effect of this new Asp49 PLA2 of Bothrops pauloensis venom is on muscle fiber sarcolemma, with avian preparation being less responsive than rodent preparation. The study enhances biochemical and pharmacological characterization of B. pauloensis venom.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biochem Res Int Año: 2015 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Biochem Res Int Año: 2015 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos