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    Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom

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    A novel lectin was isolated from Bothrops leucurus snake venom using a combination of affinity and gel filtration chromatographies. the lectin (BIL) agglutinated glutaraldehyde-treated rabbit and human erythrocytes with preference for rabbit erythrocytes. Galactose, raffinose, lactose, fetal bovine serum and casein inhibited lectin-induced rabbit erythrocyte agglutination. BIL, with a molecular mass of 30 kDa and composed of two subunits of 15 kDa, showed dependence on calcium. BIL is an acidic protein with highest activity over the pH range of 4.0-7.0 and stable under heating to 70 degrees C. Fluorescence emission spectra showed tryptophan residues partially buried within the lectin structure. the percentages of secondary structure revealed by circular dichroism were 1% alpha-helix, 44% beta-sheet, 24% beta-turn and 31% unordered. BIL showed effective antibacterial activity against Gram-positive bacteria Staphylococcus aureus, Enterococcus faecalis and Bacillus subtilis with minimal inhibitory concentrations of 31.25, 62.25 and 125 mu g/mL, respectively. in conclusion, B. leucurus snake venom contains a galactoside-binding lectin with antibacterial activity. (C) 2011 Elsevier Inc. All rights reserved.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Univ Fed Pernambuco, Dept Bioquim, BR-50670420 Recife, PE, BrazilUniv Fed Bahia, Dept Zool, BR-40170210 Salvador, BA, BrazilUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilUniv Fed Pernambuco, Dept Zool, BR-50670420 Recife, PE, BrazilUniv Estadual Oeste Parana, Ctr Engn & Ciencias Exatas, BR-85903000 Toledo, Parana, BrazilUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilWeb of Scienc
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