ArticleMolecules (Basel, Switzerland)2013
Purification, partial characterization and immobilization of a mannose-specific lectin from seeds of Dioclea lasiophylla mart.
Article in Molecules (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 22 citations in OpenAlex.
- Glucose-Binding Dioclea bicolor Lectin (DBL): Purification, Characterization, Structural Analysis, and Antibacterial Properties.The protein journal · 2024Article
- Partial Characterization of Lectins Purified from the Surco and Vara (Furrow and Rod) Varieties of BlackMolecules (Basel, Switzerland) · 2022Article
- ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships.International journal of molecular sciences · 2018Review
- Differential recognition of natural and remodeled glycotopes by three Diocleae lectins.Glycoconjugate journal · 2018Article
- Eutirucallin: A Lectin with Antitumor and Antimicrobial Properties.Frontiers in cellular and infection microbiology · 2017Article
- Cytotoxic and antiproliferative effect of tepary bean lectins on C33-A, MCF-7, SKNSH, and SW480 cell lines.Molecules (Basel, Switzerland) · 2014Article
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Authors and funding
15 authors at 1 institution in 1 country.
Funding
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Abstract
Lectin from the seeds of Dioclea lasiophylla (DlyL) was purified in a single step by affinity chromatography on a Sephadex® G-50 column. DlyL strongly agglutinated rabbit erythrocytes and was inhibited by monosaccharides (D-mannose and α-methyl-D-mannoside) and glycoproteins (ovalbumin and fetuin). Similar to other Diocleinae lectins, DlyL has three chains, α, β and γ, 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 °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® 4B bound 0.917 mg of ovalbumin per cycle, showing the ability to become a tool for glycoproteomics studies.
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