A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads

Detalhes bibliográficos
Autor(a) principal: Alves, Ana Cecília
Data de Publicação: 2015
Outros Autores: Vasconcelos, Mayron Alves de, Santiago, Mayara Quiroz, Pinto-Junior, Vanir Reis, Osterne, Vinicius José Silva, Lóssio, Cláudia Figueiredo, Souza Ferreira Bringel, Pedro Henrique, Castro, Rondinelle Ribeiro, Nagano, C. S., Delatorre, Plínio, Souza, Luis Augusto Gomes, Nascimento, K. S., Assreuy, Ana Maria Sampaio, Cavada, B. S.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional do INPA
Texto Completo: https://repositorio.inpa.gov.br/handle/1/15873
Resumo: A novel lectin from seeds of Clathrotropis nitida (CNA) was purified and characterized. CNA is a glycoprotein containing approximately 3.3% carbohydrates in its structure. CNA promoted intense agglutination of rabbit erythrocytes, which was inhibited by galactosides and porcine stomach mucin (PSM). The lectin maintained its hemagglutinating activity after incubation in a wide range of temperatures (30-60 °C) and pH (6.0-7.0), and its binding activity was dependent on divalent cations (Ca+2 and Mg+2). SDS-PAGE showed an electrophoretic profile consisting of a single band of 28 kDa, as confirmed by electrospray ionization mass spectrometry, which indicated an average molecular mass of 27,406 ± 2 Da and the possible presence of isoforms and glycoforms. In addition, CNA exhibited no toxicity to Artemia sp. nauplii and elicited reversible and dose-dependent vasorelaxation in precontracted aortic rings. CNA was successfully immobilized on chitosan beads and was able to capture PSM in solution. This study demonstrated that CNA is a lectin that has potential as a biotechnological tool in glycomics and glycoproteomics applications. © 2015 Elsevier Inc.
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spelling Alves, Ana CecíliaVasconcelos, Mayron Alves deSantiago, Mayara QuirozPinto-Junior, Vanir ReisOsterne, Vinicius José SilvaLóssio, Cláudia FigueiredoSouza Ferreira Bringel, Pedro HenriqueCastro, Rondinelle RibeiroNagano, C. S.Delatorre, PlínioSouza, Luis Augusto GomesNascimento, K. S.Assreuy, Ana Maria SampaioCavada, B. S.2020-05-19T20:34:03Z2020-05-19T20:34:03Z2015https://repositorio.inpa.gov.br/handle/1/1587310.1016/j.abb.2015.10.020A novel lectin from seeds of Clathrotropis nitida (CNA) was purified and characterized. CNA is a glycoprotein containing approximately 3.3% carbohydrates in its structure. CNA promoted intense agglutination of rabbit erythrocytes, which was inhibited by galactosides and porcine stomach mucin (PSM). The lectin maintained its hemagglutinating activity after incubation in a wide range of temperatures (30-60 °C) and pH (6.0-7.0), and its binding activity was dependent on divalent cations (Ca+2 and Mg+2). SDS-PAGE showed an electrophoretic profile consisting of a single band of 28 kDa, as confirmed by electrospray ionization mass spectrometry, which indicated an average molecular mass of 27,406 ± 2 Da and the possible presence of isoforms and glycoforms. In addition, CNA exhibited no toxicity to Artemia sp. nauplii and elicited reversible and dose-dependent vasorelaxation in precontracted aortic rings. CNA was successfully immobilized on chitosan beads and was able to capture PSM in solution. This study demonstrated that CNA is a lectin that has potential as a biotechnological tool in glycomics and glycoproteomics applications. © 2015 Elsevier Inc.Volume 588, Pags. 33-40Attribution-NonCommercial-NoDerivs 3.0 Brazilhttp://creativecommons.org/licenses/by-nc-nd/3.0/br/info:eu-repo/semantics/openAccessCalciumCarbohydrateChitosanGalactosideLectinMagnesiumStomach MucinImmobilized ProteinPlant LectinVasodilator AgentAnimals CellAnimals ExperimentAnimals ModelBinding AffinityCarbohydrate AnalysisClathrotropis NitidaControlled StudyDose ResponseElectrospray Mass SpectrometryGlycobiologyMaleMedicinal PlantMolecular WeightNonhumanPhysical ChemistrySeed PlantElectrophoresis, Polyacrylamide GelPriority JournalProtein AnalysisProtein ImmobilizationRatTemperatureVascular RingVasodilatationAmino Acid SequenceAnimalsArtemiaChemistryDrug EffectsFabaceaeGeneticsHemagglutinationHumanIn Vitro StudyIsolation And PurificationMolecular GeneticsPhysiologyRabbitSequence HomologyAorta, ThoracicWistar RatAmino Acid SequenceAnimalAorta, ThoracicArtemiaChitosanFabaceaeHemagglutinationHumansImmobilized ProteinsIn Vitro TechniquesMaleMolecular Sequence DataMolecular WeightPlant LectinsPlants, MedicinalRabbitsRatsRats, WistarSeedsSequence Homology, Amino AcidVasodilator AgentsA novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beadsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleArchives of Biochemistry and Biophysicsengreponame:Repositório Institucional do INPAinstname:Instituto Nacional de Pesquisas da Amazônia (INPA)instacron:INPAORIGINALartigo-inpa.pdfartigo-inpa.pdfapplication/pdf966884https://repositorio.inpa.gov.br/bitstream/1/15873/1/artigo-inpa.pdf224f9812842f1898063ad1efecc30db3MD511/158732020-05-19 16:52:01.336oai:repositorio:1/15873Repositório de PublicaçõesPUBhttps://repositorio.inpa.gov.br/oai/requestopendoar:2020-05-19T20:52:01Repositório Institucional do INPA - Instituto Nacional de Pesquisas da Amazônia (INPA)false
dc.title.en.fl_str_mv A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
title A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
spellingShingle A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
Alves, Ana Cecília
Calcium
Carbohydrate
Chitosan
Galactoside
Lectin
Magnesium
Stomach Mucin
Immobilized Protein
Plant Lectin
Vasodilator Agent
Animals Cell
Animals Experiment
Animals Model
Binding Affinity
Carbohydrate Analysis
Clathrotropis Nitida
Controlled Study
Dose Response
Electrospray Mass Spectrometry
Glycobiology
Male
Medicinal Plant
Molecular Weight
Nonhuman
Physical Chemistry
Seed Plant
Electrophoresis, Polyacrylamide Gel
Priority Journal
Protein Analysis
Protein Immobilization
Rat
Temperature
Vascular Ring
Vasodilatation
Amino Acid Sequence
Animals
Artemia
Chemistry
Drug Effects
Fabaceae
Genetics
Hemagglutination
Human
In Vitro Study
Isolation And Purification
Molecular Genetics
Physiology
Rabbit
Sequence Homology
Aorta, Thoracic
Wistar Rat
Amino Acid Sequence
Animal
Aorta, Thoracic
Artemia
Chitosan
Fabaceae
Hemagglutination
Humans
Immobilized Proteins
In Vitro Techniques
Male
Molecular Sequence Data
Molecular Weight
Plant Lectins
Plants, Medicinal
Rabbits
Rats
Rats, Wistar
Seeds
Sequence Homology, Amino Acid
Vasodilator Agents
title_short A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
title_full A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
title_fullStr A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
title_full_unstemmed A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
title_sort A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
author Alves, Ana Cecília
author_facet Alves, Ana Cecília
Vasconcelos, Mayron Alves de
Santiago, Mayara Quiroz
Pinto-Junior, Vanir Reis
Osterne, Vinicius José Silva
Lóssio, Cláudia Figueiredo
Souza Ferreira Bringel, Pedro Henrique
Castro, Rondinelle Ribeiro
Nagano, C. S.
Delatorre, Plínio
Souza, Luis Augusto Gomes
Nascimento, K. S.
Assreuy, Ana Maria Sampaio
Cavada, B. S.
author_role author
author2 Vasconcelos, Mayron Alves de
Santiago, Mayara Quiroz
Pinto-Junior, Vanir Reis
Osterne, Vinicius José Silva
Lóssio, Cláudia Figueiredo
Souza Ferreira Bringel, Pedro Henrique
Castro, Rondinelle Ribeiro
Nagano, C. S.
Delatorre, Plínio
Souza, Luis Augusto Gomes
Nascimento, K. S.
Assreuy, Ana Maria Sampaio
Cavada, B. S.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Alves, Ana Cecília
Vasconcelos, Mayron Alves de
Santiago, Mayara Quiroz
Pinto-Junior, Vanir Reis
Osterne, Vinicius José Silva
Lóssio, Cláudia Figueiredo
Souza Ferreira Bringel, Pedro Henrique
Castro, Rondinelle Ribeiro
Nagano, C. S.
Delatorre, Plínio
Souza, Luis Augusto Gomes
Nascimento, K. S.
Assreuy, Ana Maria Sampaio
Cavada, B. S.
dc.subject.eng.fl_str_mv Calcium
Carbohydrate
Chitosan
Galactoside
Lectin
Magnesium
Stomach Mucin
Immobilized Protein
Plant Lectin
Vasodilator Agent
Animals Cell
Animals Experiment
Animals Model
Binding Affinity
Carbohydrate Analysis
Clathrotropis Nitida
Controlled Study
Dose Response
Electrospray Mass Spectrometry
Glycobiology
Male
Medicinal Plant
Molecular Weight
Nonhuman
Physical Chemistry
Seed Plant
Electrophoresis, Polyacrylamide Gel
Priority Journal
Protein Analysis
Protein Immobilization
Rat
Temperature
Vascular Ring
Vasodilatation
Amino Acid Sequence
Animals
Artemia
Chemistry
Drug Effects
Fabaceae
Genetics
Hemagglutination
Human
In Vitro Study
Isolation And Purification
Molecular Genetics
Physiology
Rabbit
Sequence Homology
Aorta, Thoracic
Wistar Rat
Amino Acid Sequence
Animal
Aorta, Thoracic
Artemia
Chitosan
Fabaceae
Hemagglutination
Humans
Immobilized Proteins
In Vitro Techniques
Male
Molecular Sequence Data
Molecular Weight
Plant Lectins
Plants, Medicinal
Rabbits
Rats
Rats, Wistar
Seeds
Sequence Homology, Amino Acid
Vasodilator Agents
topic Calcium
Carbohydrate
Chitosan
Galactoside
Lectin
Magnesium
Stomach Mucin
Immobilized Protein
Plant Lectin
Vasodilator Agent
Animals Cell
Animals Experiment
Animals Model
Binding Affinity
Carbohydrate Analysis
Clathrotropis Nitida
Controlled Study
Dose Response
Electrospray Mass Spectrometry
Glycobiology
Male
Medicinal Plant
Molecular Weight
Nonhuman
Physical Chemistry
Seed Plant
Electrophoresis, Polyacrylamide Gel
Priority Journal
Protein Analysis
Protein Immobilization
Rat
Temperature
Vascular Ring
Vasodilatation
Amino Acid Sequence
Animals
Artemia
Chemistry
Drug Effects
Fabaceae
Genetics
Hemagglutination
Human
In Vitro Study
Isolation And Purification
Molecular Genetics
Physiology
Rabbit
Sequence Homology
Aorta, Thoracic
Wistar Rat
Amino Acid Sequence
Animal
Aorta, Thoracic
Artemia
Chitosan
Fabaceae
Hemagglutination
Humans
Immobilized Proteins
In Vitro Techniques
Male
Molecular Sequence Data
Molecular Weight
Plant Lectins
Plants, Medicinal
Rabbits
Rats
Rats, Wistar
Seeds
Sequence Homology, Amino Acid
Vasodilator Agents
description A novel lectin from seeds of Clathrotropis nitida (CNA) was purified and characterized. CNA is a glycoprotein containing approximately 3.3% carbohydrates in its structure. CNA promoted intense agglutination of rabbit erythrocytes, which was inhibited by galactosides and porcine stomach mucin (PSM). The lectin maintained its hemagglutinating activity after incubation in a wide range of temperatures (30-60 °C) and pH (6.0-7.0), and its binding activity was dependent on divalent cations (Ca+2 and Mg+2). SDS-PAGE showed an electrophoretic profile consisting of a single band of 28 kDa, as confirmed by electrospray ionization mass spectrometry, which indicated an average molecular mass of 27,406 ± 2 Da and the possible presence of isoforms and glycoforms. In addition, CNA exhibited no toxicity to Artemia sp. nauplii and elicited reversible and dose-dependent vasorelaxation in precontracted aortic rings. CNA was successfully immobilized on chitosan beads and was able to capture PSM in solution. This study demonstrated that CNA is a lectin that has potential as a biotechnological tool in glycomics and glycoproteomics applications. © 2015 Elsevier Inc.
publishDate 2015
dc.date.issued.fl_str_mv 2015
dc.date.accessioned.fl_str_mv 2020-05-19T20:34:03Z
dc.date.available.fl_str_mv 2020-05-19T20:34:03Z
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 https://repositorio.inpa.gov.br/handle/1/15873
dc.identifier.doi.none.fl_str_mv 10.1016/j.abb.2015.10.020
url https://repositorio.inpa.gov.br/handle/1/15873
identifier_str_mv 10.1016/j.abb.2015.10.020
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartof.pt_BR.fl_str_mv Volume 588, Pags. 33-40
dc.rights.driver.fl_str_mv Attribution-NonCommercial-NoDerivs 3.0 Brazil
http://creativecommons.org/licenses/by-nc-nd/3.0/br/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Attribution-NonCommercial-NoDerivs 3.0 Brazil
http://creativecommons.org/licenses/by-nc-nd/3.0/br/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Archives of Biochemistry and Biophysics
publisher.none.fl_str_mv Archives of Biochemistry and Biophysics
dc.source.none.fl_str_mv reponame:Repositório Institucional do INPA
instname:Instituto Nacional de Pesquisas da Amazônia (INPA)
instacron:INPA
instname_str Instituto Nacional de Pesquisas da Amazônia (INPA)
instacron_str INPA
institution INPA
reponame_str Repositório Institucional do INPA
collection Repositório Institucional do INPA
bitstream.url.fl_str_mv https://repositorio.inpa.gov.br/bitstream/1/15873/1/artigo-inpa.pdf
bitstream.checksum.fl_str_mv 224f9812842f1898063ad1efecc30db3
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repository.name.fl_str_mv Repositório Institucional do INPA - Instituto Nacional de Pesquisas da Amazônia (INPA)
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