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. 1980 Sep 15;58(18):947-51.
doi: 10.1007/BF01477053.

Differentiation of human alkaline phosphatases by lectin binding affinity

F G Lehmann

Differentiation of human alkaline phosphatases by lectin binding affinity

F G Lehmann. Klin Wochenschr. .

Abstract

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.

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