The glycoprotein allergen Ag-54 (Cla h II) from Cladosporium herbarum. Further biochemical characterization
Swärd-Nordmo, M; Paulsen, BS; Wold, JK
| HERO ID | 5417842 |
|---|---|
| In Press | No |
| Year | 1988 |
| Title | The glycoprotein allergen Ag-54 (Cla h II) from Cladosporium herbarum. Further biochemical characterization |
| Authors | Swärd-Nordmo, M; Paulsen, BS; Wold, JK |
| Journal | International Archives of Allergy and Applied Immunology |
| Volume | 85 |
| Issue | 3 |
| Page Numbers | 295-301 |
| Abstract | The carbohydrate-protein linkage of the allergen Ag-54 in the mould Cladosporium herbarum was studied after alkaline-borohydride treatment of the glycoprotein. By incorporating tritium into the peptide-linked monosaccharide through the alkaline scission of the linkage, it was demonstrated that the highly branched galactomannan moiety of Ag-54 was linked to the protein through mannose. Threonine was identified as the carbohydrate-linked amino acid. In addition, a few glucose units were peptide-linked, but the corresponding amino acids were not identified. When deglycosylated with trifluoromethanesulfonic acid, Ag-54 retained only 5% of its allergenic activity as compared to the native Ag-54 when tested by rocket immunoelectrophoresis and autoradiography. Immunological identity between native and deglycosylated Ag-54 was observed. Deglycosylation also resulted in reduced stability towards denaturation by heat or urea. |
| Doi | 10.1159/000234520 |
| Pmid | 3127346 |
| Is Certified Translation | No |
| Dupe Override | No |
| Is Public | Yes |
| Language Text | English |