Glutamine-specific Deamidation of α_<s1>-Casein by Transglutaminase(Food & Nutrition)
スポンサーリンク
概要
- 論文の詳細を見る
α_<s1>-Casein was deamidated specifically in the moiety of the glutaminyl side chains by transglutaminase. The deamidation was achieved by reversibly blocking the amino groups in substrate protein. The deamidated product was found out to have 80% (11 residues) of the total deamidated glutaminyl residues. No significant conformational changes were observed even after the modifications. Consequently, the solubility in acidic pH regions, especially at pH 5, was increased. On the other hand, the Ca^<2+>-sensitivity largely decreased to the extent that nearly all the deamidated product was soluble at 20 mM CaCl_2. Deamidation by transglutaminase may be useful as a new method to solubilize insoluble proteins without destroying protein structures.
- 社団法人日本農芸化学会の論文
- 1986-12-23
著者
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Nio Noriki
Central Research Laboratories, Ajinomoto Co., Inc.
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MOTOKI Masao
Central Research Laboratories, Ajinomoto Co., Inc.
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Motoki M
Ajinomoto Co. Inc. Kawasaki Jpn
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Motoki Masao
Central Research Laboratories Ajinomoto Co. Inc.
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SEGURO Katsuya
Central Research Laboratories, Ajinomoto Co., Inc.
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Nio N
Ajinomoto Co. Inc. Kanagawa Jpn
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Takinami K
Kansai Univ. Osaka Jpn
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Seguro K
Ajinomoto Co. Inc. Kanagawa Jpn
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Seguro Katsuya
Central Research Laboratories Ajinomoto Co. Inc.
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TAKINAMI Koichi
Research Institute of Molecular Genetics, Shimane University
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Takinami Koichi
Central Research Laboratories Ajinomoto Co. Inc.
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Takinami Koichi
Research Institute Of Molecular Genetics Shimane University
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