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Campo DC | Valor | Idioma |
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dc.contributor.author | Rocha, Bruno Anderson Matias da | - |
dc.contributor.author | Moreno, Frederico Bruno Mendes Batista | - |
dc.contributor.author | Delatorre, Plínio | - |
dc.contributor.author | Souza, Emmanuel Prata | - |
dc.contributor.author | Marinho, Emmanuel S. | - |
dc.contributor.author | Benevides, R. G. | - |
dc.contributor.author | Rustiguel, Joane Kathelen Rodrigues | - |
dc.contributor.author | Souza, Luis A.G. | - |
dc.contributor.author | Nagano, C. S. | - |
dc.contributor.author | Debray, Henri | - |
dc.contributor.author | Sampaio, Alexandre Holanda | - |
dc.contributor.author | Azevedo, Walter Filgueira de | - |
dc.contributor.author | Cavada, B. S. | - |
dc.date.accessioned | 2020-06-15T22:01:58Z | - |
dc.date.available | 2020-06-15T22:01:58Z | - |
dc.date.issued | 2009 | - |
dc.identifier.uri | https://repositorio.inpa.gov.br/handle/1/18496 | - |
dc.description.abstract | The unique carbohydrate-binding property of lectins makes them invaluable tools in biomedical research. Here, we report the purification, partial primary structure, carbohydrate affinity characterization, crystallization, and preliminary X-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds (CRLII). Isolation and purification of CRLII was performed by a single step using a Sepharose-4B-lactose affinity chromatography column. The carbohydrate affinity characterization was carried using assays for hemagglutination activity and inhibition. CRLII showed hemagglutinating activity toward rabbit erythrocytes. O-glycoproteins from mucine mucopolysaccharides showed the most potent inhibition capacity at a minimum concentration of 1.2 μg mL-1. Protein sequencing by mass spectrometry was obtained by the digestion of CRLII with trypsin, Glu-C, and AspN. CRLII partial protein sequence exhibits 46% similarity with the ConA-like α chain precursor. Suitable protein crystals were obtained with the hanging-drop vapor-diffusion method with 8% ethylene glycol, 0.1 M Tris-HCl pH 8.5, and 11% PEG 8,000. The monoclinic crystals belong to space group P21 with unit cell parameters a∈=∈49.4, b∈=∈89.6, and c∈=∈100.8 Å. © 2008 Humana Press. | en |
dc.language.iso | en | pt_BR |
dc.relation.ispartof | Volume 152, Número 3, Pags. 383-393 | pt_BR |
dc.rights | Restrito | * |
dc.subject | Chromatography, Affinity | en |
dc.subject | Antigen-antibody Reactions | en |
dc.subject | Binding Energy | en |
dc.subject | Column Chromatography | en |
dc.subject | Crystallization | en |
dc.subject | Ethylene | en |
dc.subject | Ethylene Glycol | en |
dc.subject | Mass Spectrometry | en |
dc.subject | Purification | en |
dc.subject | Sugars | en |
dc.subject | X Ray Diffraction Analysis | en |
dc.subject | Carbohydrate Binding | en |
dc.subject | Cymbosema Roseum | en |
dc.subject | Isolation And Purification | en |
dc.subject | Lactose-specific Lectin | en |
dc.subject | Lectins | en |
dc.subject | Monoclinic Crystals | en |
dc.subject | Tandem Mass Spectrometry | en |
dc.subject | Unit Cell Parameters | en |
dc.subject | Proteins | en |
dc.subject | Asparagine | en |
dc.subject | Ethylene Glycol | en |
dc.subject | Glutamic Acid | en |
dc.subject | Glycoprotein | en |
dc.subject | Glycosaminoglycan | en |
dc.subject | Hydrochloric Acid | en |
dc.subject | Lectin | en |
dc.subject | Sepharose | en |
dc.subject | Trypsin | en |
dc.subject | Alpha Chain | en |
dc.subject | Amino Acid Sequence | en |
dc.subject | Animals Cell | en |
dc.subject | Binding Affinity | en |
dc.subject | Column Chromatography | en |
dc.subject | Concentration (parameters) | en |
dc.subject | Controlled Study | en |
dc.subject | Crystallization | en |
dc.subject | Cymbosema Roseum | en |
dc.subject | Erythrocyte | en |
dc.subject | Hemagglutination | en |
dc.subject | Hemagglutination Inhibition | en |
dc.subject | Mass Spectrometer | en |
dc.subject | Nonhuman | en |
dc.subject | Ph | en |
dc.subject | Plant | en |
dc.subject | Seed Plant | en |
dc.subject | Protein Carbohydrate Interaction | en |
dc.subject | Protein Determination | en |
dc.subject | Protein Isolation | en |
dc.subject | Protein Purification | en |
dc.subject | Protein Structure | en |
dc.subject | Rabbit | en |
dc.subject | Structure Analysis | en |
dc.subject | X-ray Diffraction | en |
dc.subject | Cymbosema Roseum | en |
dc.subject | Oryctolagus Cuniculus | en |
dc.title | Purification, characterization, and preliminary x-ray diffraction analysis of a lactose-specific lectin from Cymbosema roseum seeds | en |
dc.type | Artigo | pt_BR |
dc.identifier.doi | 10.1007/s12010-008-8334-9 | - |
dc.publisher.journal | Applied Biochemistry and Biotechnology | pt_BR |
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