The Glycoprotein Allergen Ag-54 (C1a h II) from Cladosporium herbarum
| Autor: | Berit Smestad Paulsen, Marit Swärd-Nordmo, Jens K. Wold |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
chemistry.chemical_classification
medicine.diagnostic_test Immunology Size-exclusion chromatography Mannose Immunoelectrophoresis General Medicine Biology Carbohydrate Polysaccharide Amino acid chemistry.chemical_compound medicine.drug_formulation_ingredient chemistry Pyranose Biochemistry Cladosporium herbarum Side chain medicine Monosaccharide Immunology and Allergy Denaturation (biochemistry) Threonine Glycoprotein |
| Zdroj: | International Archives of Allergy and Immunology. 85:288-294 |
| ISSN: | 1423-0097 1018-2438 |
| DOI: | 10.1159/000234519 |
| Popis: | The carbohydrate moiety of an important allergen, Ag-54 in Cladosporium herbarum was studied by alkaline-borohydride treatment, gel filtration, high-performance liquid chromatography, methylation analysis, gas liquid chromatography and mass spectrometry. The Ag-54 protein core possessed a very limited number of sugar chains. The carbohydrate moiety consisted mainly of one large highly branched polysaccharide chain which accounted for nearly 75% of the total molecular weight of the glycoprotein. The carbohydrate moiety is made up of D-mannose and D-glucose units in pyranose form having D-galactofuranose side chains attached. Mannose is both 1,2- and 1,6-linked, while glucose is 1,4- and 1,6-linked. Some of the 1,6-linked galactofuranose side chains are bound through C-2 of the 1,6-linked mannose units, and the rest to C-3 of 1,6-linked mannose and 1,2-linked mannose units. A few oligoglucosidic chains of approximately 4 glucose units are also attached to the protein. |
| Databáze: | OpenAIRE |
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