Characterization of the sugar-binding specificity of the toxic lectins isolated from Abrus pulchellus seeds.
Glycoconj J
; 18(5): 391-400, 2001 May.
Article
in En
| MEDLINE
| ID: mdl-11925506
ABSTRACT
The sugar-binding specificity of the toxic lectins from Abrus pulchellus seeds was investigated by combination of affinity chromatography of glycopeptides and oligosaccharides of well-defined structures on a lectin-Sepharose column and measurement of the kinetic interactions in real time towards immobilized glycoproteins. The lectins showed strong affinity for a series of bi- and triantennary N-acetyllactosamine type glycans. The related asialo-oligosaccharides interact more strongly with the lectins. The best recognized structures were asialo-glycopeptides from fetuin. Accordingly, the kinetic interaction with immobilized asialofetuin was by far the most pronounced. Human and bovine lactotransferrins and human serotransferrin interacted to a lesser extent. The interaction with asialofetuin was inhibited by galactose in a dose dependent manner. Lactose, N-acetyllactosamine and lacto-N-biose exhibited similar degree of inhibition while N-acetylgalactosamine was a poor inhibitor. These results suggested that the carbohydrate-binding site of the Abrus pulchellus lectins was specific for galactose and possess a remarkable affinity for the sequences lactose [beta-D-Gal-(1-->4)-D-Glc], N-acetyllactosamine [beta-D-Gal-(1-->4)-D-GlcNAc] and lacto-N-biose [beta-D-Gal-(1-->3)-D-GlcNAc].
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Seeds
/
Abrus
/
Carbohydrate Metabolism
/
Lectins
Limits:
Animals
/
Humans
Language:
En
Journal:
Glycoconj J
Journal subject:
BIOQUIMICA
/
METABOLISMO
Year:
2001
Document type:
Article