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Title: Purification and primary structure determination of a galactose-specific lectin from Vatairea guianensis Aublet seeds that exhibits vasorelaxant effect
Authors: Silva, Helton Colares
Nagano, C. S.
Souza, Luis A.G.
Nascimento, K. S.
Isídro, Renato
Delatorre, Plínio
Rocha, Bruno Anderson Matias da
Sampaio, Alexandre Holanda
Assreuy, Ana Maria Sampaio
Pires, Alana de Freitas
Damasceno, Luis Eduardo A.
Marques-Domingos, Gabriela F O
Cavada, B. S.
Keywords: Amino Acid Residues
Amino Acid Sequence
Ammonium Sulfate
Brazilian Amazon
Spectrometry, Mass, Electrospray Ionization
Ethylenediaminetetraacetic Acid
Galactose-specific Lectins
Guar Gums
Minor Components
Ph Value
Primary Structures
Sodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis
Tandem Mass Spectrometry
Vasorelaxant Effect
Vatairea Guianensis
Chromatography, Affinity
Amino Acids
Mass Spectrometry
Nitric Oxide
Sodium Sulfate
Cyamopsis Tetragonoloba
Oryctolagus Cuniculus
Vatairea Macrocarpa
Issue Date: 2012
metadata.dc.publisher.journal: Process Biochemistry
metadata.dc.relation.ispartof: Volume 47, Número 12, Pags. 2347-2355
Abstract: Vatairea guianensis seeds, a typical plant from the Brazilian Amazon region that belongs to the Dalbergieae tribe, possess a lectin that was isolated by precipitation with solid ammonium sulfate followed by guar gum affinity chromatography. This lectin was named VGL. The V. guianensis lectin strongly agglutinated rabbit erythrocytes and was inhibited by d-galactose and d-galactose-derived sugars, especially N-acetyl-d-galactosamine. VGL has been shown to be a stable protein, maintaining its hemagglutinating activity after incubation at a wide range of temperature and pH values and after incubation with ethylenediamine tetraacetic acid (EDTA). In a sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis, the purified VGL exhibited an electrophoretic profile consisting of a major 30-32 kDa double band, which is termed the alpha-chain, and two minor components of 18 and 15 kDa, which are referred to as the beta- and gamma-chains, respectively. An analysis using electrospray ionization mass spectrometry also indicated that purified VGL contains a mixture of chains with molecular weights of 28,437 ± 2, 14,952 ± 2 and 12,332 ± 2. The complete amino acid sequence of VGL, as determined using tandem mass spectrometry, consists of 239 amino acid residues. VGL is a glycoprotein exhibiting high similarity in primary structure to other lectins from evolutionarily related plants, such as Vatairea macrocarpa lectin and lectins belonging to the Sophoreae tribe. VGL exhibits vasorelaxant activity in contracted rat aortas, an effect that is strictly dependent on the endothelium and involves nitric oxide and the lectin domain. © 2012 Elsevier Ltd.
metadata.dc.identifier.doi: 10.1016/j.procbio.2012.09.014
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