Please use this identifier to cite or link to this item: https://repositorio.inpa.gov.br/handle/1/17991
Title: Purification and characterization of a lectin of the swartzieae legume taxa
Authors: 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
Keywords: 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
Issue Date: 2012
metadata.dc.publisher.journal: Protein and Peptide Letters
metadata.dc.relation.ispartof: 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.
metadata.dc.identifier.doi: 10.2174/092986612802762679
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