Purification, Partial Characterization, and CNBr-Sepharose Immobilization of a Vasorelaxant Glucose/Mannose Lectin from Canavalia virosa Seeds
作者： Vinicius JS Osterne , Mayara Q Santiago , Vanir R Pinto-Junior , João B Cajazeiras , Jorge LA Correia
DOI: 10.1007/S12010-014-0751-3
关键词:
摘要: A novel mannose/glucose-binding lectin from Canavalia virosa (designated as ConV) has been purified seeds of C. by affinity chromatography on a mannose-Sepharose 4B column. ConV strongly agglutinates rabbit erythrocytes and was inhibited monosaccharides (D-mannose, D-glucose, α-methyl-D-mannoside) glycoproteins (ovalbumin fetuin). SDS-PAGE revealed three bands corresponding to subunits (α, β, γ) confirmed ESI mass spectrometry with exact 25,480 ± 2 Da, 12,864 ± 1 Da, 12,633 ± 1 Da, respectively. The more stable in pH ranging 7.0 9.0, supported up 80 oC without any loss activity unaffected EDTA. showed no toxicity against Artemia sp. nauplii relaxed endothelized rat aorta, the participation domain. In our tests, immobilized CNBr-Sepharose capable binding 0.8 mg ovalbumin per chromatography, allowing use tool for capture purification glycoproteins.
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