Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/243641
Type: Artigo
Title: Bp-13 PLA(2): purification and neuromuscular activity of a new Asp49 toxin isolated from Bothrops pauloensis snake venom
Author: Sucasaca-Monzón, Georgina
Randazzo-Moura, Priscila
Rocha, Talita
Torres-Huaco, Frank Denis
Vilca-Quispe, Augusto
Ponce-Soto, Luis Alberto
Marangoni, Sérgio
Cruz-Höfling, Maria Alice da
Rodrigues-Simioni, Léa
Abstract: A new PLA(2) (Bp-13) was purified from Bothrops pauloensis snake venom after a single chromatographic step of RP-HPLC on mu-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 PLA(2) myotoxins from other Bothrops venoms. Bp-13 showed allosteric enzymatic behavior and maximal activity at pH 8.1, 36 degrees-45 degrees C. Full Bp-13 PLA(2) activity required Ca2+; its PLA(2) activity was inhibited by Mg2+, Mn2+, Sr2+, and Cd2+ in the presence and absence of 1 mM Ca2+. In the mouse phrenic nerve-diaphragm (PND) preparation, the time for 50% paralysis was concentration-dependent (P < 0.05). Both the replacement of Ca2+ by Sr2+ and temperature lowering (24 degrees C) inhibited the Bp-13 PLA(2) -induced twitch-tension blockade. Bp-13 PLA(2) 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 PLA(2) 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.
A new PLA(2) (Bp-13) was purified from Bothrops pauloensis snake venom after a single chromatographic step of RP-HPLC on mu-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 PLA(2) myotoxins from other Bothrops venoms. Bp-13 showed allosteric enzymatic behavior and maximal activity at pH 8.1, 36 degrees-45 degrees C. Full Bp-13 PLA(2) activity required Ca2+; its PLA(2) activity was inhibited by Mg2+, Mn2+, Sr2+, and Cd2+ in the presence and absence of 1 mM Ca2+. In the mouse phrenic nerve-diaphragm (PND) preparation, the time for 50% paralysis was concentration-dependent (P < 0.05). Both the replacement of Ca2+ by Sr2+ and temperature lowering (24 degrees C) inhibited the Bp-13 PLA(2) -induced twitch-tension blockade. Bp-13 PLA(2) 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 PLA(2) 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
Subject: Miotoxina
Espectrometria de massas por ionização e dessorção a laser assistida por matriz
Venenos de serpentes
Sequência de aminoácidos
Cromatografia liquida de alta pressão
Country: Reino Unido
Editor: Hindawi
Citation: Bp-13 Pla(2): Purification And Neuromuscular Activity Of A New Asp49 Toxin Isolated From Bothrops Pauloensis Snake Venom. Hindawi Publishing Corporation, p. 2015.
Rights: aberto
Identifier DOI: 10.1155/2015/826059
Address: https://www.hindawi.com/journals/bri/2015/826059/
Date Issue: 2015
Appears in Collections:IB - Artigos e Outros Documentos
FCM - Artigos e Outros Documentos

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