Affinity purified Lens culinaris lectin (LCA) is composed of four subunits that consists of an α-chain (MW: 5.7 kDa) and β-chain (MW: 17.5 kDa). It has a carbohydrate specificity toward α-D-mannose and α-D-glucose, eluting with the sugar MeαMan+MeαGlc. This lectin is useful in affinity chromatography columns for the separation of glycoconjugates. The two isomers LCA-A and LCA-B agglutinates human red blood cells, although not blood group specific. Activity of LCA is determined by haemagglutination with human blood and agglutinates a 2% suspension of human erythrocytes at a lectin concentration of 8µg/ml. LCA requires calcium and manganese ions for binding. See other LCA conjugates.
Lens culinaris (Lentil) Lectin (LCA/LCH) is conjugated to ferritin, that has a molecular weight of 474,000 g/mol (all 24 subunits combined). Ferritin-conjugated lectins can be used to visualize localization of specific saccharide moieties and examine the distribution of plasma membrane glycoproteins. These conjugates can be viewed via electron microscopy.