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https://repositorio.inpa.gov.br/handle/1/17991| Título: | Purification and characterization of a lectin of the swartzieae legume taxa |
| Autor: | Fernandes, Andréia Varmes Ramos, Márcio Viana Vasconcelos, Ilka Maria Aria Monteiro, Cristina A. Moreno, Frederico Bruno Mendes Batista Pereira, José Odair Gonçalves, José Francisco de Carvalho |
| Palavras-chave: | Galactose Lactose Lactose Binding Seed Lectin N Acetylgalactosamine Plant Extract Plant Lectin Sodium Chloride Swartzia Laevicarpa Extract Unclassified Drug Chromatography, Affinity Amino Acid Sequence Amino Terminal Sequence Animals Cell Anti-fungal Activity Bacterium Isolate Cancer Cell Culture Chemical Analysis Chemical Reaction Colon Cancer Concentration Response Controlled Study Dalbergia Drug Cytotoxicity Enzyme Inhibition Erythrocyte Fusarium Solani Glioblastoma Glomerella Lindemuthiana Hemagglutination Ic 50 In Vitro Study Legume Mass Spectrometry Molecular Weight Nonhuman Ovary Cancer Seed Plant Protein Analysis Protein Degradation Protein Function Protein Purification Protein Structure Rabbit Sequence Homology Sophora Structure Analysis Swartzia Laevicarpa Temperature Sensitivity Thanatephorus Cucumeris Toxicity Testing Acetylgalactosamine Amino Acid Sequence Animal Cell Death Chromatography, Affinity Electrophoresis Fabaceae Fungi Galactose Hemagglutination Hemagglutination Tests Humans Lactose Molecular Sequence Data Molecular Weight Neoplasms Peptide Fragments Plant Lectins Rabbits Rats Seeds Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization Tumor Cells, Cultured |
| Data do documento: | 2012 |
| Revista: | Protein and Peptide Letters |
| É parte de: | Volume 19, Número 10, Pags. 1082-1088 |
| Abstract: | This work aimed at describing the first biochemical and structural data of a lectin belonging to Swartzieae, a primitive Legume Taxa. A lactose-binding seed lectin (SLL) was purified by affinity chromatography of crude saline extracts of Swartzia laevicarpa on immobilized lactose. The SLL agglutinated rabbit erythrocytes but not rat or human (A, B, O) erythrocytes. Lectin activity was retained after heating at 100 °C for 15 min and was best inhibited by Nacetylgalactosamine, lactose and galactose. The lectin exhibited a single electrophoretic pattern that corresponded to a molecular mass of 29,000 Da, which was confirmed by MS analysis. In addition, the lectin reacted positively with Schiff's reagent. The unique N-terminal amino acid sequence (39 residues) and the internal peptide sequence were determined by Edman degradation and MS/MS, respectively. The sequencing revealed complete homology of the SLL with legume lectins belonging to primitive groups (Dalbergieae and Sophoreae). The SLL (at 1 mg/ml) did not exhibit antifungal activity against various phytopathogens or cytotoxicity (at 100 μg/ml) towards different cancer cell lines. © 2012 Bentham Science Publishers. |
| DOI: | 10.2174/092986612802762679 |
| Aparece nas coleções: | Artigos |
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