Please use this identifier to cite or link to this item: https://repositorio.inpa.gov.br/handle/1/15873
Title: A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads
Authors: 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.
Keywords: 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
Issue Date: 2015
metadata.dc.publisher.journal: Archives of Biochemistry and Biophysics
metadata.dc.relation.ispartof: Volume 588, Pags. 33-40
Abstract: 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.
metadata.dc.identifier.doi: 10.1016/j.abb.2015.10.020
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