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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, Priscila
Ponce-Soto, L A
Rodrigues-Simioni, Léa
Marangoni, Sérgio
Abstract: Bp-12 was isolated from Bothrops pauloensis snake venom in only one chromatographic step in reverse phase HPLC on micro-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 CLKELCECDK AVAICLRENL NTYNKKYRYF LKPLCKKADA 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 microM) and 16 +/- 6 min (3.6 microM). Bp-12 can induce indirect and directly blocked evoked twitches, even in the preparations in which Ca(2+) is replaced by Sr(2+), 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: Amino Acid Sequence
Chromatography, High Pressure Liquid
Crotalid Venoms
Group Ii Phospholipases A2
Isoelectric Point
Molecular Sequence Data
Molecular Weight
Neuromuscular Junction
Reptilian Proteins
Sequence Alignment
Sequence Homology, Amino Acid
Citation: The Protein Journal. v. 27, n. 6, p. 355-62, 2008-Sep.
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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