Chaparral lectin is a metalloprotein that reversibly binds to polysaccharides and glycoconjugates containing α- d -mannose and α- d -glucose, eluted by the sugars Me-α-Man and Me-α-Glc. In contrast to Con A, it differentiates weakly between glucosyl and mannosyl residues and binds weakly to monosaccharides. It also retained the ability to bind sugars in the presence of 1% sodium deoxycholate and thus could react with detergent-solubilized membranes. Affinity-purified Lens culinaris lectin (LCA) consists of four subunits, α-chain (molecular weight: 5.7 kDa) and β-chain (molecular weight: 17.5 kDa). This lectin is used in affinity chromatography columns for the separation of glycoconjugates. The two isoforms, LCA-A and LCA-B, agglutinate human erythrocytes, although not blood group specific.The activity of LCA is determined by agglutination with human blood and 2% human erythrocyte suspension at a lectin concentration of 8 µg/ml.LCA requires calcium and manganese ions for binding. See other LCA conjugates.
For research use only, not for clinical use.