Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/79177
Type: Artigo de periódico
Title: Structural Characterization and Neuromuscular Activity of a New Lys49 Phospholipase A(2) Homologous (Bp-12) Isolated from Bothrops pauloensis Snake Venom
Author: Randazzo-Moura, P
Ponce-Soto, LA
Rodrigues-Simioni, L
Marangoni, S
Abstract: Bp-12 was isolated from Bothrops pauloensis snake venom in only one chromatographic step in reverse phase HPLC on mu-Bondapack C-18. The molecular mass of 13,789.56 Da was determined by mass spectrometry. The amino acids composition showed that Bp-12 presented high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical of a basic PLA(2). The sequence of Bp-12 contains 122 amino acid residues: SLFELGKMIL QETGKNPAKS LGAFYCYCGW GSQGQPKDAV DRCCYVHKCC YKKITGCNPK KDRYSYSWKD KTLVCGEDNS CLKEL CECDKAVAICLRENL NTYNKKYRYFLKPLCKKADA AC, with a pI value of 8.55 and with a high homology with Lys49 PLA(2) from other snake venoms. In mouse phrenic nerve-diaphragm, the time needed for 50% paralysis was: 45 +/- 6 min (1.4 mu M) and 16 +/- 6 min (3.6 mu M). Bp-12 can induce indirect and directly blocked evoked twitches, even in the preparations in which Ca2+ is replaced by Sr2+, being the addition of d-tubocurarine required for direct blocking. These results identify Bp-12 as a new member of the Lys49 PLA(2) family and shows that this toxin might contribute to the effects of the crude venom on the neuromuscular junction.
Subject: Phospholipase A(2)
Lys49
Neuromuscular blockade
Snake venom
Bothrops pauloensis
Country: EUA
Editor: Springer
Rights: fechado
Identifier DOI: 10.1007/s10930-008-9144-1
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

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