Please use this identifier to cite or link to this item: http://dspace.sctimst.ac.in/jspui/handle/123456789/10417
Title: Separation of bovine heart galactose lectin from endogenous glycoproteins co-purified with the lectin during affinity chromatography
Authors: Appukuttan, PS
Annamma, KI
Geetha, M
Jaison, PL
Keywords: Life Sciences & Biomedicine - Other Topics
Issue Date: 1998
Publisher: JOURNAL OF BIOSCIENCES
Citation: 23 ,2;137-141
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-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.
URI: 10.1007/BF02703006
http://dspace.sctimst.ac.in/jspui/handle/123456789/10417
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