Journal
MOLECULES
Volume 18, Issue 9, Pages 10857-10869Publisher
MDPI
DOI: 10.3390/molecules180910857
Keywords
lectin; Dioclea lasiophylla; Diocleinae; toxicity; immobilization
Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Fundacao Cearense de Apoio ao Desenvolvimento Cientifico e Tecnologico (FUNCAP)
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Lectin from the seeds of Dioclea lasiophylla (DlyL) was purified in a single step by affinity chromatography on a Sephadex (R) G-50 column. DlyL strongly agglutinated rabbit erythrocytes and was inhibited by monosaccharides (D-mannose and alpha-methyl-D-mannoside) and glycoproteins (ovalbumin and fetuin). Similar to other Diocleinae lectins, DlyL has three chains, alpha, beta and gamma, with mass of 25,569 +/- 2, 12,998 +/- 1 and 12,588 +/- 1 Da, respectively, and has no disulfide bonds. The hemagglutinating activity of DlyL was optimal in pH 8.0, stable at a temperature of 70 degrees C and decreased in EDTA solution, indicating that lectin activity is dependent on divalent metals. DlyL exhibited low toxicity on Artemia sp. nauplii, but this effect was dependent on the concentration of lectin in solution. DlyL immobilized on cyanogen bromide-activated Sepharose (R) 4B bound 0.917 mg of ovalbumin per cycle, showing the ability to become a tool for glycoproteomics studies.
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