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Type: Artigo de periódico
Title: Structural and functional characterization of myotoxin, Cr-IV 1, a phospholipase A(2) D49 from the venom of the snake Calloselasma rhodostoma
Author: Bonfim, VL
Ponce-Soto, LA
de Souza, DM
Souza, GHMF
Baldasso, PA
Eberlin, MN
Marangoni, S
Abstract: A new D49 PLA(2) was purified from the venom of Calloselasma rhodostoma after two chromatographic steps. Molecular exclusion chromatography was done through a Protein-Pack 300 SW column (0.78 cm x 30 cm), eluting with 0.25 M ammonium bicarbonate, pH 7.9, at a flow rate of 0.3 ml/min. Reverse-phase HPLC was then performed on mu-Bondapack C-18. The sample was determined to have a molecular mass of 13,870.94 Da MALDI-TOF by mass spectrometry, and the amino acid composition showed that Cr-IV 1 presented a high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical of a basic PLA2. Cr-IV 1 presented a sequence of 122 amino acid residues: DLWEFGQMIL KETGSLPFPY YTTYGCYCGV GGRGGKPKDA TDRCCFVHDC CYGKLTGCPK TNDRYSYSRL DYTIVCGEGG PCKQICECDK AAAVCFRENL RTYNKKYRYHLKPFCKEPAE TC and a calculated pI value of 8.0. Cr-IV 1 had PLA2 activity in the presence of a synthetic chromogenic substrate (4-nitro-3-(octanoyloxy)benzoic acid) and showed a rapid cytolytic effect on mouse skeletal muscle myoblasts and myotubes in culture. In mice, Cr-IV I induced myonecrosis and edema upon intramuscular and intravenous injections, respectively. The LD50 of Cr-IV 1 was determined to be 0.07 mg/k body weight by intracerebroventricular (i.c.v.) injection. The combination of structural and functional information obtained herein classifies Cr-IV I as a new member of the D49 PLA2 family, as it presents the typical behavior of a phospholipase A(2) from this family. (C) 2007 The International Association for Biologicals. Published by Elsevier Ltd. All fights reserved.
Subject: phospholipase A(2)
snake venom
Calloselasma rhodostoma
structural and functional characterization
Country: Inglaterra
Editor: Academic Press Ltd Elsevier Science Ltd
Citation: Biologicals. Academic Press Ltd Elsevier Science Ltd, v. 36, n. 3, n. 168, n. 176, 2008.
Rights: fechado
Identifier DOI: 10.1016/j.biologicals.2007.10.004
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

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