Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/197814
Type: Artigo de periódico
Title: Biological And Biochemical Characterization Of New Basic Phospholipase A(2) Bmtx-i Isolated From Bothrops Moojeni Snake Venom.
Author: Calgarotto, Andrana K
Damico, Daniela C S
Ponce-Soto, L A
Baldasso, Paulo A
Da Silva, Saulo L
Souza, Gustavo H M F
Eberlin, Marcos N
Marangoni, Sergio
Abstract: BmTX-I, an Asp49 phospholipase A(2), was purified from Bothrops moojeni venom after only one chromatographic step using reverse-phase HPLC on mu-Bondapak C-18 column. A molecular mass of 14238.71Da was determined by MALDI-TOF mass spectrometry. Amino acid analysis showed a high content of hydrophobic and basic amino acids as well as 14 half-cysteine residues. The BmTX-I PLA(2) had a sequence of 121 residues of amino acids: DLWQFNKMIK KEVGKLPFPF YGAYGCYCGW GGRGEKPKDG TDRCCFVHDC CYKKLTGCPK WDDRYSYSWK DITIVCGEDL PCEEICECDR AAAVCFYENL GTYNKKYMKH LKPCKKADYP C and pI value 7.84, and showed a high degree of homology with basic Asp49 PLA(2) myotoxins from other Bothrops venoms. BmTX-I presented PLA(2) activity in the presence of a synthetic substrate and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0 and 35-45 degrees C. Maximum PLA(2) activity required Ca(2+) and in the presence of Mg(2+), Cd(2+) and Mn(2+) it was reduced in presence or absence of Ca(2+). Crotapotin from Crotalus durissus colillineatus rattlesnake venom has significantly inhibited (P<0.05) the enzymatic activity of BmTX-I. In vitro, the whole venom and BmTX-I caused a blockade of the neuromuscular transmission in young chick biventer cervicis preparations in a similar way to other bothrops species. In mice, BmTX-I and the whole venom-induced myonecrosis and a systemic interleukin-6 response upon intramuscular injection. Edema-forming activity was also analyzed through injection of the venom and the purified BmTX-I into the subplantar region of the right footpad. Since BmTX-I exert a strong proinflammatory effect; the enzymatic phospholipids hydrolysis might be relevant for these phenomena.
Subject: Amino Acid Sequence
Animals
Bothrops
Chemical Fractionation
Chickens
Chromatography, High Pressure Liquid
Crotalid Venoms
Crotalus
Crotoxin
Kinetics
Male
Mice
Molecular Sequence Data
Neuromuscular Blockade
Neurotoxins
Phospholipases A
Sequence Alignment
Sequence Analysis, Protein
Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization
Citation: Toxicon : Official Journal Of The International Society On Toxinology. v. 51, n. 8, p. 1509-19, 2008-Jun.
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2008.03.030
Address: http://www.ncbi.nlm.nih.gov/pubmed/18501940
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

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