ArticleMolecules (Basel, Switzerland)2011
Crystallization and characterization of an inflammatory lectin purified from the seeds of Dioclea wilsonii.
Article in Molecules (Basel, Switzerland), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Glucose-Binding Dioclea bicolor Lectin (DBL): Purification, Characterization, Structural Analysis, and Antibacterial Properties.The protein journal · 2024Article
- 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
- Myocardial stress perfusion magnetic resonance: initial experience in a pediatric and young adult population using regadenoson.Pediatric radiology · 2017Article
- Correlation between proinflammatory role of a lectin from Typhonium giganteum Engl. and macrophage.International journal of clinical and experimental pathology · 2015Article
- Purification, partial characterization and immobilization of a mannose-specific lectin from seeds of Dioclea lasiophylla mart.Molecules (Basel, Switzerland) · 2013Article
- Effects of Canavalia lectins on acute inflammation in sensitized and non-sensitized rats.Inflammation · 2013Article
- Structure predictions of two Bauhinia variegata lectins reveal patterns of C-terminal properties in single chain legume lectins.PloS one · 2013Article
- Purification and biological activities of Abelmoschus esculentus seed lectin.The protein journal · 2012Article
- Antinociceptive and anti-inflammatory effects of a lectin-like substance from Clitoria fairchildiana R. Howard seeds.Molecules (Basel, Switzerland) · 2012Article
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16 authors at 4 institutions in 1 country.
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Abstract
DwL, a lectin extracted from the seeds of Dioclea wilsonii, is a metalloprotein with strong agglutinating activity against rabbit and ABO erythrocytes, inhibited by glucose and mannose. DwL was purified by affinity chromatography on a Sephadex G-50 column and ion exchange chromatography on a HiTrap SP XL column. SDS-PAGE revealed three electrophoretic bands corresponding to the α (25,634 ± 2 Da), β (12,873 ± 2 Da) and γ (12,779 ± 2 Da) chains. Protein sequencing was done by Tandem Mass Spectrometry. The primary sequence featured 237 amino acids and was highly homologous to other reported Diocleinae lectins. A complete X-ray dataset was collected at 2.0 Å for X-Man-complexed DWL crystals produced by the vapor diffusion method. The crystals were orthorhombic and belonged to the space group I222, with the unit-cell parameters a = 59.6, b = 67.9 and c = 109.0 Å. DWL differed in potency from other ConA-like lectins and was found to induce neutrophil migration in rats, making it particularly useful in structural/functional studies of this class of proteins.
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