Preparation and properties of concanavalin A-binding glycopeptides derived from rat brain glycoproteins
| Autor: | Hildegard Hof, Javaid I. Javaid, Eric G. Brunngraber |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Size-exclusion chromatography
Biophysics Mannose Biochemistry Fucose chemistry.chemical_compound Affinity chromatography Concanavalin A Animals Amino Acids Molecular Biology Glycoproteins Hexoses Brain Chemistry Chromatography Binding Sites biology Glycopeptides Lectin Hexosamines Glycopeptide Rats chemistry Galactose biology.protein Sialic Acids Protein Binding |
| Zdroj: | Biochimica et biophysica acta. 404(1) |
| ISSN: | 0006-3002 |
| Popis: | Mannose-rich glycopeptides derived from brain glycoproteins were recovered by affinity chromatography on Concanavalin A-Sepharose. These glycopeptides, which adsorb to the lectin and are eluted with alpha-methylmannoside, constitute about 25--30% of the total glycopeptide material recovered from rat brain glycoproteins. They contain predominately mannose and N-acetylglucosamine (mannose/N-acetylglucosamine = 3), as well as small amounts of galactose and fucose. Approx. 65% of the Concanavalin A-binding glycopeptide carbohydrate was recovered after treatment with leucine aminopeptidase, gel filtration on Biogel P-4, and ion-exchange chromatography on coupled Dowex 50-hydrogen and Dowex 1-chloride columns. The purified glycopeptide fraction contained six mannose and two N-acetylglucosamine residues per aspartic acid and possessed an apparent molecular weight of about 2000 as assessed by gel filtration and amino acid analysis. Galactose and fucose were absent. Treatment of the purified glycopeptides with alpha-mannosidase drastically reduced their affinity for Concanavalin A, suggesting the presence of one or more terminal mannose residues. |
| Databáze: | OpenAIRE |
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