Galanthus nivalis lectin

Galanthus nivalis lectin or agglutinin (GNA) is isolated from snowdrop bulbs. It has a molecular weight of 50 kDa and consists of four identical subunits. The lectin is known to agglutinate rabbit erythrocytes but not human erythrocytes. It binds specifically to murine IgM immunoglobulin and human α2-macroglobulin. Structures containing (α-1,3) mannose residues are preferred for binding. It contains little or no carbohydrate and does not need Ca2+ or Mn2+ for binding, since unlike most mannose-specific lectins it is not a metalloprotein. Unlike the majority of mannose-binding lectins, GNA does not bind alpha-linked glucose. GNA has been useful in HIV research. It is also applicable for blood cell agglutination studies but also as a model system to help understand the molecular basis of how proteins recognize carbohydrates. The purity of GNA lectin is determined by SDS- electrophoresis, which generates one single band at 13 kDa corresponding to the four identical polypeptide chains. Applications: Blood cell agglutination studies - Model systems to help understand the molecular basis of how proteins recognize carbohydrates - HIV research.