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

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    • Keywords

       

      Galectin; endogenous glycoprotein; affinity chromatography; bovine heart

    • 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.

    • Author Affiliations

       

      P S Appukuttan1 K I Annamma1 M Geetha1 P L Jaison1

      1. Division of Biochemistry, Sree Chitra Tirunal Institute for Medical Sciences and Technology, Thiruvananthapuram - 695 011, India
    • Dates

       
  • Journal of Biosciences | News

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