Peanut lectin (PNA) is purified by affinity chromatography and consists of four subunits, each of about 27,000 subunits. This lectin has an isoelectric point between pH 5.5 and pH 6.5. It is carbohydrate-specific for Galβ3GalNAc with galactose-eluting sugar. Galactose and lactose are poor inhibitors, while disaccharide galactose beta (1->3)GalNAc and defatalized human red blood cell substance N (t antigen, present in many M and N blood groups) are potent inhibitors of PNA. Alkaline phosphatase (AP) is coupled to peanut agglutinin (PNA), and PNA binding has been shown in a variety of applications such as Western blotting and ELISA. Alkaline phosphatase is a large protein (140 kDa) that catalyzes the hydrolysis of phosphate groups in the substrate to produce color or fluorescent products. The optimal enzyme activity of this protein is between pH 8 and 10, and its reaction rate remains linear with increased sensitivity over time.
For research use only, not for clinical use.