Griffonia simplicifolia lectin (GSLI) is affinitively purified from a woody climbing shrub native to Africa. GSLI consists of two subunits, A and B, which combine to form a tetramer structure, producing five isolates. The lectin binds terminal D-galactosyl residues and terminal n-acetyl - - Residual D-galactosaminyl. A-rich lectins preferentially agglutinate group A red blood cells and therefore appear to be specific to -n-acetylgalactosamine residues, while B-rich lectins preferentially agglutinate group B cells and are specific to -galactosamine residues. The specificity of the lectin for blood group B is higher than that for blood group A1. GSLI has been reported to bind to a variety of glycoproteins, including laminin. Due to some D-galactose residues are expressed in mouse tissue endothelial cells, and GSLI can exhibit highly specific glycosylation surface patterns in these cells.
For research use only, not for clinical use.