Structural Characterization of the 16-kDa Allergen, RA17, in Rice Seeds. Prediction of the Secondary Structure and Identification of Intramolecular Disulfide Bridges.
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- IZUMI Hidehiko
- Department of Food and Nutrition, Nagoya College of Nutrition Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University
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- SUGIYAMA Minoru
- Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University
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- MATSUDA Tsukasa
- Department of Applied Biological Sciences, School of Agricultural Sciences, Nagoya University
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- NAKAMURA Ryo
- Department of Food Science and Technology, Nihon University
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The 16-kDa rice allergen, RA17, belonging to the α-amylase/trypsin inhibitor family was isolated from rice seed and structurally characterized by identifying cystine-containing peptides and predicting the secondary structure and hydrophobic regions. Eight peptides, which constitute three sets of cystine-containing peptides, were purified by HPLC from a thermolytic digest of RA17 and identified by their amino acid sequence and composition, indicating five intramolecular disulfide bridges: Cys34-Cys94, Cys26-(Cys50 or Cys51)-Cys110 and Cys12-(Cys62 or Cys64)-Cys122. Analyses of the CD spectrum and the Chou-Fasman prediction suggested that RA17 had some helical- and sheet-structure regions. Based on these experimental and predicted data, RA17 is proposed to be a globular molecule with a small hydrophobic core having folding restricted by five intramolecular disulfide bridges.<br>
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 63 (12), 2059-2063, 1999
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206473551360
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- NII論文ID
- 110002679420
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD3cXlsFKmtg%3D%3D
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- ISSN
- 13476947
- 09168451
- http://id.crossref.org/issn/09168451
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- NDL書誌ID
- 4949308
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- PubMed
- 10664838
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 使用不可