2003年3月
Identification of disulfide proteins in the salt soluble fraction of rice (Oryza sativa) seed
CEREAL CHEMISTRY
- ,
- 巻
- 80
- 号
- 2
- 開始ページ
- 172
- 終了ページ
- 174
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- 出版者・発行元
- AMER ASSOC CEREAL CHEMISTS
Evidence has been accumulating to suggest that disulfide bonding is one of the key causes of allergenicity. Recently we developed the "disulfide proteome", a technique for the comprehensive analysis of disulfide bonding of proteins. We applied this new technique to the rice seed's salt-soluble fraction, which has long been known to be allergenic. Most proteins in the fraction, including alpha-amylase/trypsin inhibitor, alpha-globulin, and glutelin fragments, have formed intramolecular disulfide bonds. Also, unknown proteins, including one sharing similarities with known allergens, had disulfide bonds, from which we can infer possible allergenicity. This is a preliminary study to screen allergens from the basis of disulfide bonding.
- リンク情報
- ID情報
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- ISSN : 0009-0352
- Web of Science ID : WOS:000181560300013