Separation of bovine heart galactose lectin from endogenous glycoproteins co-purified with the lectin during affinity chromatography.
J Biosci
;
1998 Jun; 23(2): 137-141
Artigo
em Inglês
| IMSEAR
| ID: sea-161203
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-dependensti nce 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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Índice:
IMSEAR (Sudeste Asiático)
Idioma:
Inglês
Revista:
J Biosci
Ano de publicação:
1998
Tipo de documento:
Artigo
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