Differentiation of human alkaline phosphatases by lectin binding affinity.
Purified human alkaline phosphatases were separated by lectin binding affinity to Wheat germ lectin-Sepharose, Concanavalin A-Sepharose and Lentil lectin-Sepharose into three isoenzymes: the placental, the intestinal and the liver-bone-kidney-type isoenzyme. Therefore, the carbohydrate chains of purified human alkaline phosphatases demonstrate the same isoenzyme classes than studies on structural, catalytical or immunological properties. The liver-bone-kidney-type isoenzyme shows a not yet described microheterogeneity on Concanavalin A and Lentil lectin. Thus, lectin binding affinity is a useful tool for the purification and separation of human alkaline phosphatase.
D000469:Alkaline Phosphatase / Q000302:isolation & purification*; D001842:Bone and Bones / Q000201:enzymology; D002846:Chromatography, Affinity / Q000379:methods*; D003208:Concanavalin A; D006801:Humans; D007422:Intestines / Q000201:enzymology; D007527:Isoenzymes / Q000302:isolation & purification*; D007668:Kidney / Q000201:enzymology; D037102:Lectins; D008099:Liver / Q000201:enzymology; D010920:Placenta / Q000201:enzymology; D013045:Species Specificity
D007527:Isoenzymes; D037102:Lectins; D003208:Concanavalin A; D000469:Alkaline Phosphatase