Specific Binding of Allergenic Soybean Protein Gly m Bd 30K with α'- and α-Subunits of Conglycinin in Soy Milk
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概要
- 論文の詳細を見る
When defatted soy milk was ultracentrifuged, 34 kDa allergenic soybean protein Gly m Bd 30 K was more abundant in the precipitate than in the supernatant by an SDS-PAGE analysis. The addition of more than 10 mM of 2-mercaptoethanol (2-ME) to the soy milk resulted not only in further removal of the 34 kDa allergenic protein to the precipitate, but also in better recovery of conglycinin in the supernatant. After a two-dimensional SDS-PAGE analysis (the first dimension, minus 2-ME; the second, plus 2-ME) of the precipitates, superimposition between the CBB-stained gel and the electroblotted membrane stained with a monoclonal antibody specific to Gly m Bd 30 K indicated that part of Gly m Bd 30 K was preferentially bound to the α'- and α-subunits of conglycinin, and that part of them had formed the dimer through a disulfide bond.
- 社団法人日本農芸化学会の論文
- 1996-06-23
著者
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Mori H
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Mori Hironori
Department Of Biotechnology Faculty Of Agriculture The University Of Tokyo
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Kawamura Yukio
Protein Science Laboratory National Food Research Institute
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SAMOTO Masahiko
Central Research Institute, Fuji Oil Co.
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Miyazaki Chiaki
Fuji Co. Ltd
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Miyazaki Chiaki
Central Research Institute Fuji Oil Co. Ltd.
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Akasaka Takeshi
Central Research Institute Fuji Oil Co., Ltd.
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Mori Hiroyuki
Central Research Institute Fuji Oil Co., Ltd.
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Samoto Masahiko
Protein Development R&d Division Fuji Oil Co. Ltd.
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Akasaka Takeshi
Central Research Institute Fuji Oil Co. Ltd.
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Mori Hiroyuki
Central Research Institute Fuji Oil Co. Ltd.
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