Separation of bovine heart galactose lectin from endogenous glycoproteins co-purified with the lectin during affinity chromatography

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dc.contributor.authorAppukuttan, PS
dc.contributor.authorAnnamma, KI
dc.contributor.authorGeetha, M
dc.contributor.authorJaison, PL
dc.date.accessioned2017-03-10T03:28:32Z
dc.date.available2017-03-10T03:28:32Z
dc.date.issued1998
dc.description.abstractDuring 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.
dc.identifier.citation23 ,2;137-141en_US
dc.identifier.uri10.1007/BF02703006
dc.identifier.urihttps://dspace.sctimst.ac.in/handle/123456789/10417
dc.publisherJOURNAL OF BIOSCIENCES
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.titleSeparation of bovine heart galactose lectin from endogenous glycoproteins co-purified with the lectin during affinity chromatography
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