CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa

Detalhes bibliográficos
Autor(a) principal: Rafael da ConceiÃÃo SimÃes
Data de Publicação: 2011
Tipo de documento: Dissertação
Idioma: por
Título da fonte: Biblioteca Digital de Teses e Dissertações da UFC
Texto Completo: http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=5881
Resumo: Mass spectrometry is a technique widely used in all prod uctive sectors. Since the late '80s with the emergence of soft ionization techniques, mass spectrometry has been widely disseminated in the analysis of biopolymers such as fatty acids, nucleic acids, oligosaccharides and especially proteins. Lectins are proteins of nonimmune origin that have at least one specific and reversible binding carbohydrate domain, without the ability to modify them. These proteins are widely distributed in nature. Lectins isolated from seeds of legumes are among the most studied and have high homology degree, being an important molecular marker of evolution in this clade. This study aimed to characterize some legume lectins by m ass spectrometry. Lectin EVA and LAA with 240 and 237 amino acid residues respectively, were analyzed for native mass and sequence of amino acids determined, showing a high degree of homology with other legume lectins. Lectin ConGF, a ConA-like, was analyzed for protein content in the crystal. Was determined that bot h mature chain and proteolytic fragments are present to form crystal, which indicates no difference between the chains structure covalently linked together by weak interactions. The partial sequence shows that ConGF has several structural features within the subtribe Diocleinae. All results demonstrate that mass spectrometry is a versatile and robust tool for characterizing proteins and can be successfully used to obtain structural information of lectins.
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spelling info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisCaracterizaÃÃo de lectinas de leguminosas por espectrometria de massaCaracterizaton of Legume lectins by Mass Spectrometry2011-02-18Benildo Sousa Cavada24242349068http://lattes.cnpq.br/5029704662813380 81219873500http://lattes.cnpq.br/9783857112928758Rafael da ConceiÃÃo SimÃesUniversidade Federal do CearÃPrograma de PÃs-GraduaÃÃo em BioquÃmicaUFCBREspectrometria de massa Lectina leguminosa LAA EVA ConGFMass spectrometry Leguminoseae Lectin EVA LAA ConGFBIOQUIMICAMass spectrometry is a technique widely used in all prod uctive sectors. Since the late '80s with the emergence of soft ionization techniques, mass spectrometry has been widely disseminated in the analysis of biopolymers such as fatty acids, nucleic acids, oligosaccharides and especially proteins. Lectins are proteins of nonimmune origin that have at least one specific and reversible binding carbohydrate domain, without the ability to modify them. These proteins are widely distributed in nature. Lectins isolated from seeds of legumes are among the most studied and have high homology degree, being an important molecular marker of evolution in this clade. This study aimed to characterize some legume lectins by m ass spectrometry. Lectin EVA and LAA with 240 and 237 amino acid residues respectively, were analyzed for native mass and sequence of amino acids determined, showing a high degree of homology with other legume lectins. Lectin ConGF, a ConA-like, was analyzed for protein content in the crystal. Was determined that bot h mature chain and proteolytic fragments are present to form crystal, which indicates no difference between the chains structure covalently linked together by weak interactions. The partial sequence shows that ConGF has several structural features within the subtribe Diocleinae. All results demonstrate that mass spectrometry is a versatile and robust tool for characterizing proteins and can be successfully used to obtain structural information of lectins. A espectrometria de massa à uma tÃcnica amplamente utilizada em todos os setores produtivos. Desde o final dos anos 80 com o surgimento de tÃcnicas de ionizaÃÃo brandas, a espectrometria de massa vem sendo amplamente difundida na anÃlise de biopolÃmeros como Ãcidos graxos, Ãcidos nuclÃicos, oligossacarÃdeos e principalmente proteÃnas. Lectinas sÃo proteÃnas de origem nÃo imune que possuem pelo menos um domÃnio de ligaÃÃo especÃfica e reversÃvel a carboidratos, sem a capacidade de modificÃ-los. Estas proteÃnas sÃo amplamente distribuÃdas na natureza. As lectinas isoladas de sementes de leguminosas estÃo entre as mais estudadas e possuem alta homologia, sendo importantes marcadores moleculares da evoluÃÃo dentro desta famÃlia vegetal. Este trabalho teve como objetivo caracterizar lectinas da famÃlia Leguminosae atravÃs de espectrometria de massa. As lectinas de Erythrina velutina (EVA) e Luetzelburgia auriculata (LAA) com 240 e 237 resÃduos de aminoÃcidos respectivamente foram analisadas quanto a massa molecular nativa e foi determinada a sequencia de aminoÃcidos. As estruturas primÃrias mostraram alto grau de homologia com outras lectinas de leguminosas. A lectina ConGF, uma ConA-Like, foi analisada quanto ao conteÃdo protÃico do cristal. O cristal està composto da cadeia madura alfa e seus os fragmentos proteolÃticos, o que indica nÃo haver diferenÃa entre a estrutura ligada covalentemente e as cadeias unidas por interaÃÃes fracas. A sequÃncia parcial demonstra que ConGF possui caracterÃsticas estruturais da subtribo Diocleinae. Todos os resultados demonstram que a tÃcnica de espectrometria de massa à uma ferramenta versÃtil e robusta para caracterizaÃÃo de proteÃnas e pode ser usada com sucesso para obtenÃÃo de informaÃÃes estruturais de lectinas.FundaÃÃo de Amparo à Pesquisa do Estado do CearÃConselho Nacional de Desenvolvimento CientÃfico e TecnolÃgicoCoordenaÃÃo de AperfeiÃoamento de Pessoal de NÃvel Superiorhttp://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=5881application/pdfinfo:eu-repo/semantics/openAccessporreponame:Biblioteca Digital de Teses e Dissertações da UFCinstname:Universidade Federal do Cearáinstacron:UFC2019-01-21T11:19:00Zmail@mail.com -
dc.title.pt.fl_str_mv CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
dc.title.alternative.en.fl_str_mv Caracterizaton of Legume lectins by Mass Spectrometry
title CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
spellingShingle CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
Rafael da ConceiÃÃo SimÃes
Espectrometria de massa
Lectina
leguminosa
LAA
EVA
ConGF
Mass spectrometry
Leguminoseae
Lectin
EVA
LAA
ConGF
BIOQUIMICA
title_short CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
title_full CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
title_fullStr CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
title_full_unstemmed CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
title_sort CaracterizaÃÃo de lectinas de leguminosas por espectrometria de massa
author Rafael da ConceiÃÃo SimÃes
author_facet Rafael da ConceiÃÃo SimÃes
author_role author
dc.contributor.advisor1.fl_str_mv Benildo Sousa Cavada
dc.contributor.advisor1ID.fl_str_mv 24242349068
dc.contributor.advisor1Lattes.fl_str_mv http://lattes.cnpq.br/5029704662813380
dc.contributor.authorID.fl_str_mv 81219873500
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/9783857112928758
dc.contributor.author.fl_str_mv Rafael da ConceiÃÃo SimÃes
contributor_str_mv Benildo Sousa Cavada
dc.subject.por.fl_str_mv Espectrometria de massa
Lectina
leguminosa
LAA
EVA
ConGF
topic Espectrometria de massa
Lectina
leguminosa
LAA
EVA
ConGF
Mass spectrometry
Leguminoseae
Lectin
EVA
LAA
ConGF
BIOQUIMICA
dc.subject.eng.fl_str_mv Mass spectrometry
Leguminoseae
Lectin
EVA
LAA
ConGF
dc.subject.cnpq.fl_str_mv BIOQUIMICA
dc.description.sponsorship.fl_txt_mv FundaÃÃo de Amparo à Pesquisa do Estado do CearÃ
Conselho Nacional de Desenvolvimento CientÃfico e TecnolÃgico
CoordenaÃÃo de AperfeiÃoamento de Pessoal de NÃvel Superior
dc.description.abstract.por.fl_txt_mv Mass spectrometry is a technique widely used in all prod uctive sectors. Since the late '80s with the emergence of soft ionization techniques, mass spectrometry has been widely disseminated in the analysis of biopolymers such as fatty acids, nucleic acids, oligosaccharides and especially proteins. Lectins are proteins of nonimmune origin that have at least one specific and reversible binding carbohydrate domain, without the ability to modify them. These proteins are widely distributed in nature. Lectins isolated from seeds of legumes are among the most studied and have high homology degree, being an important molecular marker of evolution in this clade. This study aimed to characterize some legume lectins by m ass spectrometry. Lectin EVA and LAA with 240 and 237 amino acid residues respectively, were analyzed for native mass and sequence of amino acids determined, showing a high degree of homology with other legume lectins. Lectin ConGF, a ConA-like, was analyzed for protein content in the crystal. Was determined that bot h mature chain and proteolytic fragments are present to form crystal, which indicates no difference between the chains structure covalently linked together by weak interactions. The partial sequence shows that ConGF has several structural features within the subtribe Diocleinae. All results demonstrate that mass spectrometry is a versatile and robust tool for characterizing proteins and can be successfully used to obtain structural information of lectins.
A espectrometria de massa à uma tÃcnica amplamente utilizada em todos os setores produtivos. Desde o final dos anos 80 com o surgimento de tÃcnicas de ionizaÃÃo brandas, a espectrometria de massa vem sendo amplamente difundida na anÃlise de biopolÃmeros como Ãcidos graxos, Ãcidos nuclÃicos, oligossacarÃdeos e principalmente proteÃnas. Lectinas sÃo proteÃnas de origem nÃo imune que possuem pelo menos um domÃnio de ligaÃÃo especÃfica e reversÃvel a carboidratos, sem a capacidade de modificÃ-los. Estas proteÃnas sÃo amplamente distribuÃdas na natureza. As lectinas isoladas de sementes de leguminosas estÃo entre as mais estudadas e possuem alta homologia, sendo importantes marcadores moleculares da evoluÃÃo dentro desta famÃlia vegetal. Este trabalho teve como objetivo caracterizar lectinas da famÃlia Leguminosae atravÃs de espectrometria de massa. As lectinas de Erythrina velutina (EVA) e Luetzelburgia auriculata (LAA) com 240 e 237 resÃduos de aminoÃcidos respectivamente foram analisadas quanto a massa molecular nativa e foi determinada a sequencia de aminoÃcidos. As estruturas primÃrias mostraram alto grau de homologia com outras lectinas de leguminosas. A lectina ConGF, uma ConA-Like, foi analisada quanto ao conteÃdo protÃico do cristal. O cristal està composto da cadeia madura alfa e seus os fragmentos proteolÃticos, o que indica nÃo haver diferenÃa entre a estrutura ligada covalentemente e as cadeias unidas por interaÃÃes fracas. A sequÃncia parcial demonstra que ConGF possui caracterÃsticas estruturais da subtribo Diocleinae. Todos os resultados demonstram que a tÃcnica de espectrometria de massa à uma ferramenta versÃtil e robusta para caracterizaÃÃo de proteÃnas e pode ser usada com sucesso para obtenÃÃo de informaÃÃes estruturais de lectinas.
description Mass spectrometry is a technique widely used in all prod uctive sectors. Since the late '80s with the emergence of soft ionization techniques, mass spectrometry has been widely disseminated in the analysis of biopolymers such as fatty acids, nucleic acids, oligosaccharides and especially proteins. Lectins are proteins of nonimmune origin that have at least one specific and reversible binding carbohydrate domain, without the ability to modify them. These proteins are widely distributed in nature. Lectins isolated from seeds of legumes are among the most studied and have high homology degree, being an important molecular marker of evolution in this clade. This study aimed to characterize some legume lectins by m ass spectrometry. Lectin EVA and LAA with 240 and 237 amino acid residues respectively, were analyzed for native mass and sequence of amino acids determined, showing a high degree of homology with other legume lectins. Lectin ConGF, a ConA-like, was analyzed for protein content in the crystal. Was determined that bot h mature chain and proteolytic fragments are present to form crystal, which indicates no difference between the chains structure covalently linked together by weak interactions. The partial sequence shows that ConGF has several structural features within the subtribe Diocleinae. All results demonstrate that mass spectrometry is a versatile and robust tool for characterizing proteins and can be successfully used to obtain structural information of lectins.
publishDate 2011
dc.date.issued.fl_str_mv 2011-02-18
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
status_str publishedVersion
format masterThesis
dc.identifier.uri.fl_str_mv http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=5881
url http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=5881
dc.language.iso.fl_str_mv por
language por
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade Federal do CearÃ
dc.publisher.program.fl_str_mv Programa de PÃs-GraduaÃÃo em BioquÃmica
dc.publisher.initials.fl_str_mv UFC
dc.publisher.country.fl_str_mv BR
publisher.none.fl_str_mv Universidade Federal do CearÃ
dc.source.none.fl_str_mv reponame:Biblioteca Digital de Teses e Dissertações da UFC
instname:Universidade Federal do Ceará
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reponame_str Biblioteca Digital de Teses e Dissertações da UFC
collection Biblioteca Digital de Teses e Dissertações da UFC
instname_str Universidade Federal do Ceará
instacron_str UFC
institution UFC
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repository.mail.fl_str_mv mail@mail.com
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