https://repositorio.ufba.br/handle/ri/5430
Tipo: | Artigo de Periódico |
Título: | Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
Título(s) alternativo(s): | Comparative biochemistry and physiology b-biochemistry & molecular biology |
Autor(es): | Nunes, Erika dos Santos Souza, Mary Angela Aranda de Vaz, Antônio Fernando de Melo Santana, Giselly Maria de Sá Gomes, Francis Soares Coelho, Luana Cassandra Breitenbach Barroso Paiva, Patrícia Maria Guedes Silva, Rejane Maria Lira da Silva-Lucca, Rosemeire Aparecida Oliva, Maria Luiza Vilela Guarnieri, Miriam Camargo Correia, Maria Tereza dos Santos |
Autor(es): | Nunes, Erika dos Santos Souza, Mary Angela Aranda de Vaz, Antônio Fernando de Melo Santana, Giselly Maria de Sá Gomes, Francis Soares Coelho, Luana Cassandra Breitenbach Barroso Paiva, Patrícia Maria Guedes Silva, Rejane Maria Lira da Silva-Lucca, Rosemeire Aparecida Oliva, Maria Luiza Vilela Guarnieri, Miriam Camargo Correia, Maria Tereza dos Santos |
Abstract: | A novel lectin was isolated from Bothrops leucurus snake venom using a combination of affinity and gel filtration chromatographies. The lectin (BlL) 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. BlL, with a molecular mass of 30 kDa and composed of two subunits of 15 kDa, showed dependence on calcium. BlL is an acidic protein with highest activity over the pH range of 4.0–7.0 and stable under heating to 70 °C. Fluorescence emission spectra showed tryptophan residues partially buried within the lectin structure. The percentages of secondary structure revealed by circular dichroism were 1% α-helix, 44% β-sheet, 24% β-turn and 31% unordered. BlL 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 μg/mL, respectively. In conclusion, B. leucurus snake venom contains a galactoside-binding lectin with antibacterial activity. |
Palavras-chave: | Antibacterial activity Fluorescence Circular dichroism Bothrops leucurus Lectin Snake venom |
URI: | http://www.repositorio.ufba.br/ri/handle/ri/5430 |
Data do documento: | 2011 |
Aparece nas coleções: | Artigo Publicado em Periódico (Química) |
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