Lectins are metallic proteins that reversibly bind to polysaccharides and glycoconjugates containing α-D-mannose and α-D-glucose, eluted by the sugars Me-α-Man and Me-α-Glc. Compared with Con A, it is weaker in distinguishing between glucose and mannosyl residues, and weaker in binding to monosaccharides. In the presence of 1% sodium deoxycholate, it also retains its ability to bind to sugar and can therefore react with the detergent dissolved membrane. Affinity purified Lens culinaris lectin (LCA) consists of four subunits of α- chain (molecular weight :5.7 kDa) and β- chain (molecular weight :17.5 kDa). This lectin is used to separate glycoconjugates in affinity columns. Two isomers, LCA-A and LCA-B, agglutinate human red blood cells, although they are not blood group specific. The activity of LCA is determined by agglutination with human blood and 2% human red blood cell suspension at a lectin concentration of 8µg/ml. LCA requires calcium and manganese ions to bind. See other LCA conjugations.
For research use only, not for clinical use.