Investigation of Multiple Forms of Tri a Bd 27K, a Major Wheat Allergen, by Immunoblotting Analysis

• Published in: Bioscience, biotechnology, and biochemistry Vol. 74; no. 1; pp. 199 - 202
• Main Authors: HIEMORI, Miki, YOSIDA, Yukari, KIMOTO, Masumi, YAMASHITA, Hiromi, TAKAHASHI, Kyoko, TAKAHASHI, Kiyoshi, KOMIYAMA, Nobuko, TSUJI, Hideaki
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.01.2010; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Amino Acid Sequence; Animals; Antibodies, Monoclonal - immunology; Antigens, Plant - analysis; Antigens, Plant - blood; Antigens, Plant - chemistry; Antigens, Plant - immunology; Biological and medical sciences; fucose residue; Fundamental and applied biological sciences. Psychology; Humans; Immunoblotting; Mites - immunology; multiple form; N-linked glycan moiety; Polysaccharides - metabolism; Tri a Bd 27K; Triticum - immunology; Triticum aestivum; wheat allergen; Wheat Hypersensitivity - blood; Wheat Hypersensitivity - immunology; Allergy; Tri a Bd 27K; multiple form; Glycan; wheat allergen; Residue; Immunoblotting assay; Cereal; Wheat; fucose residue; N-linked glycan moiety; Allergen; Fucose
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.90634

Tri a Bd 27K, a major wheat allergen, is a glycoprotein. Tri a Bd 27K was found to occur in multiple forms by two-dimensional polyacrylamide gel electrophoresis and immunoblotting with a monoclonal antibody against the allergen. Furthermore, it was found that only Tri a Bd 27K components, which have N-linked glycan moieties with fucose residues, bound to IgE antibodies in the sera of wheat-sensitive patients.