Artigo

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

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)....

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Autor principal: Alves, Ana Cecília
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.
Grau: Artigo
Idioma: English
Publicado em: Archives of Biochemistry and Biophysics 2020
Assuntos:
Rat
Acesso em linha: https://repositorio.inpa.gov.br/handle/1/15873
id oai:repositorio:1-15873
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spelling oai:repositorio:1-15873 A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads 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. 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 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. 2020-05-19T20:34:03Z 2020-05-19T20:34:03Z 2015 Artigo https://repositorio.inpa.gov.br/handle/1/15873 10.1016/j.abb.2015.10.020 en Volume 588, Pags. 33-40 Attribution-NonCommercial-NoDerivs 3.0 Brazil http://creativecommons.org/licenses/by-nc-nd/3.0/br/ application/pdf Archives of Biochemistry and Biophysics
institution Instituto Nacional de Pesquisas da Amazônia - Repositório Institucional
collection INPA-RI
language English
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
spellingShingle 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
Alves, Ana Cecília
A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
topic_facet 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.
format Artigo
author Alves, Ana Cecília
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.
author2Str 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.
title A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
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 novel vasorelaxant lectin purified from seeds of clathrotropis nitida: partial characterization and immobilization in chitosan beads
publisher Archives of Biochemistry and Biophysics
publishDate 2020
url https://repositorio.inpa.gov.br/handle/1/15873
_version_ 1787143548053749760
score 11.755432