Characterization of the sugar-binding specificity of the toxic lectins isolated from Abrus pulchellus seeds
| Autor: | M V, Ramos, A H, Sampaio, B S, Cavada, J J, Calvete, T B, Grangeiro, H, Debray |
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| Rok vydání: | 2002 |
| Předmět: |
Binding Sites
Molecular Sequence Data Carbohydrates Glycopeptides Oligosaccharides Surface Plasmon Resonance Chromatography Affinity Substrate Specificity Kinetics Carbohydrate Sequence Lectins Abrus Seeds Carbohydrate Conformation Animals Carbohydrate Metabolism Humans Cattle Plant Lectins Protein Binding |
| Zdroj: | Glycoconjugate journal. 18(5) |
| ISSN: | 0282-0080 |
| Popis: | 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]. |
| Databáze: | OpenAIRE |
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