Affinity chromatography is used to purify Datura lectin. The seeds of datulas contain at least three different carbohydrate-binding proteins, the most prominent lectin being a dimeric glycoprotein composed of two distinct subunits and containing 40% carbohydrates. It binds well to N-acetylglucosamine, oligomers, and branched-chain pentasaccharides, including two N-acetylglucosamine disaccharides (-1,6) and (-1,2) linked to mannose, which are the most potent agglutination inhibitors known. DSL is more likely to bind to (GlcNAc)2-4 and eluate with glycochitin hydrolysates. DSL binds well in the acidic pH range and decreases affinity above pH 8.0. This lectin is specific for blood groups A, B and O. Studies have shown that DSA can be used as a biomarker of tumor urinary tract cells.
For research use only, not for clinical use.