Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/347887
Type: Artigo
Title: Pharmacological and partial biochemical characterization of Bmaj-9 isolated from Bothrops marajoensis snake venom
Author: Galbiatti, C.
Rocha, T.
Randazzo-Moura, P.
Ponce-Soto, L. A.
Marangoni, S.
Cruz-Höfling, M. A.
Rodrigues-Simioni, L.
Abstract: Bmaj-9, a basic PLA2 (13679.33 Da), was isolated from Bothrops marajoensis snake venom through only one chromatographic step in reversed phase HPLC on ¼-Bondapak C-18 column. The amino acid composition showed that Bmaj-9 had a high content of Lys, His, and Arg, typical of a basic PLA2. The sequence of Bmaj-9 contains 124 amino acid residues with a pI value of 8.55, such as DLWQWGQMIL KETGKLPFSY YTAYGCYCGW GGRGGKPKAD TDRCCFVHDC, revealing a high homology with Asp49 PLA2 from other snake venoms. It also exhibited a pronounced phospholipase A2 activity when compared with crude venom. In chick biventer cervicis preparations, the time for 50% and 100% neuromuscular paralysis was respectively (in minutes): 110 ± 10 (1 µg/mL); 40 ± 6 and 90 ± 2 (5 µg/mL); 30 ± 3 and 70 ± 5 (10 µg/mL); 42 ± 1 and 60 ± 2 (20 µg/mL), with no effect on the contractures elicited by either exogenous ACh (110 µM) or KCl (20 mM). Bmaj-9 (10 µg/mL) neither interfered with the muscular response to direct electrical stimulation in curarized preparations nor significantly altered the release of CK at 0, 15, 30 and 60 minutes incubations (27.4 ± 5, 74.2 ± 8, 161.0 ± 21 and 353.0 ± 47, respectively). The histological analysis showed that, even causing blockade at the maximum dosage (5 µg/mL), the toxin does not induce significant morphological alterations such as necrosis or infiltration of inflammatory cells. These results identified Bmaj-9 as a new member of the basic Asp49 PLA2 family able to interact with the motor nerve terminal membrane, thereby inducing a presynaptic neuromuscular blockade
Subject: Venenos de serpentes
Bloqueio neuromuscular
Country: Reino Unido
Editor: Springer Nature
Rights: Aberto
Identifier DOI: 10.1590/S1678-91992012000100008
Address: https://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000100008
Date Issue: 2012
Appears in Collections:IB - Artigos e Outros Documentos
FCM - Artigos e Outros Documentos

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