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Título: | A novel vasorelaxant lectin purified from seeds of Clathrotropis nitida: Partial characterization and immobilization in chitosan beads |
Autor: | 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. |
Palavras-chave: | 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 |
Data do documento: | 2015 |
Revista: | Archives of Biochemistry and Biophysics |
É parte de: | 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. |
DOI: | 10.1016/j.abb.2015.10.020 |
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