Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFBA |
Texto Completo: | http://www.repositorio.ufba.br/ri/handle/ri/5430 |
Resumo: | Acesso restrito: Texto completo. p. 57-63. |
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Nunes, Erika dos SantosSouza, Mary Angela Aranda deVaz, Antônio Fernando de MeloSantana, Giselly Maria de SáGomes, Francis SoaresCoelho, Luana Cassandra Breitenbach BarrosoPaiva, Patrícia Maria GuedesSilva, Rejane Maria Lira daSilva-Lucca, Rosemeire AparecidaOliva, Maria Luiza VilelaGuarnieri, Miriam CamargoCorreia, Maria Tereza dos SantosNunes, Erika dos SantosSouza, Mary Angela Aranda deVaz, Antônio Fernando de MeloSantana, Giselly Maria de SáGomes, Francis SoaresCoelho, Luana Cassandra Breitenbach BarrosoPaiva, Patrícia Maria GuedesSilva, Rejane Maria Lira daSilva-Lucca, Rosemeire AparecidaOliva, Maria Luiza VilelaGuarnieri, Miriam CamargoCorreia, Maria Tereza dos Santos2012-02-24T12:27:40Z2011http://www.repositorio.ufba.br/ri/handle/ri/5430v. 159, n. 1.Acesso restrito: Texto completo. p. 57-63.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.Submitted by JURANDI DE SOUZA SILVA (jssufba@hotmail.com) on 2012-02-24T12:27:40Z No. of bitstreams: 1 __pdn.sciencedirect.com_....0-S109649591100039X-main.pdf: 285488 bytes, checksum: eb5db11aed712ad4983cbc91c31fc451 (MD5)Made available in DSpace on 2012-02-24T12:27:40Z (GMT). No. of bitstreams: 1 __pdn.sciencedirect.com_....0-S109649591100039X-main.pdf: 285488 bytes, checksum: eb5db11aed712ad4983cbc91c31fc451 (MD5) Previous issue date: 2011DOI: 10.1016/j.cbpb.2011.02.001reponame:Repositório Institucional da UFBAinstname:Universidade Federal da Bahia (UFBA)instacron:UFBAAntibacterial activityFluorescenceCircular dichroismBothrops leucurusLectinSnake venomPurification of a lectin with antibacterial activity from Bothrops leucurus snake venomComparative biochemistry and physiology b-biochemistry & molecular biologyinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10000-01-01enginfo:eu-repo/semantics/openAccessORIGINAL__pdn.sciencedirect.com_....0-S109649591100039X-main.pdf__pdn.sciencedirect.com_....0-S109649591100039X-main.pdfapplication/pdf285488https://repositorio.ufba.br/bitstream/ri/5430/1/__pdn.sciencedirect.com_....0-S109649591100039X-main.pdfeb5db11aed712ad4983cbc91c31fc451MD51LICENSElicense.txtlicense.txttext/plain1762https://repositorio.ufba.br/bitstream/ri/5430/2/license.txt1b89a9a0548218172d7c829f87a0eab9MD52TEXT__pdn.sciencedirect.com_....0-S109649591100039X-main.pdf.txt__pdn.sciencedirect.com_....0-S109649591100039X-main.pdf.txtExtracted texttext/plain44095https://repositorio.ufba.br/bitstream/ri/5430/3/__pdn.sciencedirect.com_....0-S109649591100039X-main.pdf.txt16d76980526327fb9aff9de8de374d17MD53ri/54302022-07-05 14:03:22.463oai:repositorio.ufba.br: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Repositório InstitucionalPUBhttp://192.188.11.11:8080/oai/requestopendoar:19322022-07-05T17:03:22Repositório Institucional da UFBA - Universidade Federal da Bahia (UFBA)false |
dc.title.pt_BR.fl_str_mv |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
dc.title.alternative.pt_BR.fl_str_mv |
Comparative biochemistry and physiology b-biochemistry & molecular biology |
title |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
spellingShingle |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom Nunes, Erika dos Santos Antibacterial activity Fluorescence Circular dichroism Bothrops leucurus Lectin Snake venom |
title_short |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
title_full |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
title_fullStr |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
title_full_unstemmed |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
title_sort |
Purification of a lectin with antibacterial activity from Bothrops leucurus snake venom |
author |
Nunes, Erika dos Santos |
author_facet |
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 |
author_role |
author |
author2 |
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 |
author2_role |
author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
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 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 |
dc.subject.por.fl_str_mv |
Antibacterial activity Fluorescence Circular dichroism Bothrops leucurus Lectin Snake venom |
topic |
Antibacterial activity Fluorescence Circular dichroism Bothrops leucurus Lectin Snake venom |
description |
Acesso restrito: Texto completo. p. 57-63. |
publishDate |
2011 |
dc.date.issued.fl_str_mv |
2011 |
dc.date.accessioned.fl_str_mv |
2012-02-24T12:27:40Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.repositorio.ufba.br/ri/handle/ri/5430 |
dc.identifier.number.pt_BR.fl_str_mv |
v. 159, n. 1. |
url |
http://www.repositorio.ufba.br/ri/handle/ri/5430 |
identifier_str_mv |
v. 159, n. 1. |
dc.language.iso.fl_str_mv |
eng |
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eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
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openAccess |
dc.source.pt_BR.fl_str_mv |
DOI: 10.1016/j.cbpb.2011.02.001 |
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reponame:Repositório Institucional da UFBA instname:Universidade Federal da Bahia (UFBA) instacron:UFBA |
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