Appukuttan, PSAnnamma, KIGeetha, MJaison, PL2017-03-102017-03-10199823 ,2;137-14110.1007/BF02703006https://dspace.sctimst.ac.in/handle/123456789/10417During 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-dependent since 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.Life Sciences & Biomedicine - Other Topics