Separation of bovine heart galactose lectin from endogenous glycoproteins co-purified with the lectin during affinity chromatography.
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Date
1998-06
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Abstract
During affinity chromatographic purification of bovine heart 14 kDa galactose-binding lectin (galectin 1) on
lactose-Sepharose, several high molecular weight non-lectin glycoproteins were co-purified with the lectin.
Glycoprotein binding to the affinity matrix was neither hydrophobic nor ionic, but galactose-dependensti nce
lactose abolished binding. Purification of galectin from the co-purified glycoproteins by affinity electrophoresis
in presence of the specific sugar lactose increased agglutination activity about 65-fold, indicating that a
complex containing galectin molecules bound sugar specifically to endogenous glycoproteins with sugar
binding sites still available had been retained on lactose-Sepharose.
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Appukuttan P S, Annamma K I, Geetha M, Jaison P L. Separation of bovine heart galactose lectin from endogenous glycoproteins co-purified with the lectin during affinity chromatography. Journal of Biosciences. 1998 Jun; 23(2): 137-141.