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

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...

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Veröffentlicht in:	Journal of biosciences 1998-06, Vol.23 (2), p.137-141
Hauptverfasser:	Appukuttan, P. S, Annamma, K. I, Geetha, M, Jaison, P. L
Format:	Artikel
Sprache:	eng
Schlagworte:	Affinity Affinity chromatography Agglutination Analytical methods binding capacity Binding sites carbohydrate binding Cattle Chromatography Electrophoresis Galactose Glycoproteins Heart Hydrophobicity Lactose lectins Molecular weight Purification Saccharides Sugar Water purification
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