Staining of glycoproteins in polyacrylamide and agarose gels with fluorescent lectins
| Autor: | Beck Ea, B.A. Perret, M. Furlan |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Carbohydrates
Biophysics Mannose Biochemistry chemistry.chemical_compound Lectins Ultraviolet light Humans Molecular Biology Polyacrylamide gel electrophoresis Glycoproteins Electrophoresis Agar Gel chemistry.chemical_classification Chromatography Staining and Labeling biology Cell Biology Fluoresceins Staining chemistry Concanavalin A Galactose biology.protein Agarose Electrophoresis Polyacrylamide Gel Glycoprotein Protein Binding |
| Zdroj: | Analytical Biochemistry. 96:208-214 |
| ISSN: | 0003-2697 |
| Popis: | We describe a simple and sensitive method for staining of the carbohydrate moiety of glycoproteins in polyacrylamide or agarose electrophoretic gels. Gels are incubated in a solution of fluorescein-labeled concanavalin A. Following destaining with a neutral buffer, glycoproteins exhibit fluorescence under long-range ultraviolet light. Thus, the glucose/mannose containing β- and γ-chains of human fibrinogen give fluorescent bands, whereas the carbohydrate-free α-chain does not react. Less than 100 ng of hexose bound to fibrinogen β- or γ-chains could be detected. The procedure is suitable for staining of other carbohydrate residues in glycoproteins, which can be recognised by specific agglutinins, as shown by binding of fluorescein-labeled lectins from Ricinus communis to galactose residues of fibrinogen. |
| Databáze: | OpenAIRE |
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