Datura stramonium agglutinin or lectin (DSA/DSL) is purified by affinity chromatography. Seeds of Datura stramonium contain at least three different carbohydrate-binding proteins, and the most prominent lectin is a dimeric glycoprotein composed of two nonidentical subunits that contains 40% carbohydrate. It binds well to N-acetylglucosamine, oligomers, and branched pentasaccharide, including two N-acetylglucosamine disaccharides linked to mannose (β-1,6) and (β-1,2), which is known to be the most potent inhibitor of agglutination. DSL prefers binding to (GlcNAc)2-4 and elutes with the sugar chitin hydrolysate. DSL binds well in the acidic pH range and its affinity decreases above pH 8.0. This agglutinin has blood group A, B, and O specificity. Studies have shown that DSA can act as a biomarker for neoplastic urotherial cells.
Biotin is a small molecule involved in a wide range of metabolic processes. This ligand forms a complex with Avidin and Streptavidin, resulting in the strongest non-covalent protein-ligand interaction known. Biotinylated Datura stramonium Lectin (DSA/DSL) has an appropriate amount of biotin bound to provide optimum detection characteristics when using an Avidin-HRP or Streptavidin-HRP conjugate. Biotinylated lectins allow for more sensitive detection in ELISA and Western-blotting applications.