Affinity purified phaseolus lectin (PHA-E) is a tetramer glycoprotein responsible for the erythrocyte agglutination properties of the PHA portion. It is carbohydrate-specific for oligosaccharides and bovine thyroglobulin or acetic acid elutes. PHA-E can bind to human red blood cells and lymphocytes and is specific for blood type a (-SA). The PHA-E receptor on normal lymphocytes is 5 times that on red blood cells. The crystal structure of the ligand-free PHA-E has the typical legume lectin fold, which is characterized by two antiparallel - sheets and two short - helices, and contains a GlcNAc residue of an n-chain glycan. Asparagine-linked erythrocyte glycopeptides are inhibitors of PHA-E-induced agglutination and mitosis and become inactive if treated with galactosidase. PHA-E binds to diggalactosylated and segmented N-glycan. This lectin is widely used as a biochemical tool for the detection of GlcNAc and gal glycoproteins.
For research use only, not for clinical use.