Separation of bovine heart galactose lectin from endogenous glycoproteins co-purified with the lectin during affinity chromatography |
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Authors: | P S Appukuttan K I Annamma M Geetha P L Jaison |
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Institution: | (1) Division of Biochemistry, Sree Chitra Tirunal Institute for Medical Sciences and Technology, 695 011 Thiruvananthapuram, India |
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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-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. |
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Keywords: | Galectin endogenous glycoprotein affinity chromatography bovine heart |
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