1. Carbohydrate structures of the glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen.
- Author
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Hino K, Yamamoto S, Sano O, Taniguchi Y, Kohno K, Usui M, Fukuda S, Hanzawa H, Haruyama H, and Kurimoto M
- Subjects
- Amino Acid Sequence, Antigens, Plant, Asparagine, Carbohydrate Conformation, Carbohydrate Sequence, Chromatography, High Pressure Liquid, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Oligosaccharides isolation & purification, Peptide Fragments chemistry, Peptide Fragments isolation & purification, Trees, Trypsin, Xylose analysis, Allergens chemistry, Oligosaccharides chemistry, Plant Proteins chemistry, Pollen chemistry
- Abstract
The glycoprotein allergen Cry j I from Japanese cedar (Cryptomeria japonica) pollen was treated with pepsin and glycopeptidase A to release asparagine-linked oligosaccharides. The reducing ends of the oligosaccharides were aminated with the fluorescent reagent 2-aminopyridine. The oligosaccharide derivatives were purified by gel permeation chromatography and reversed-phase HPLC. Their structures were determined by sequential exoglycosidase digestion and 500 MHz 1H-NMR spectroscopy. Four oligosaccharide structures, A, B, C, and D, were identified as the xylose-containing complex-type. They were present at a molar ratio of 8:1:6:1. By amino acid sequence analyses of the tryptic peptides, Asn-170 and Asn-333 of Cry j I were found to carry asparagine-linked oligosaccharides. [formula: see text]
- Published
- 1995
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