Purification and Characterization of Trehalose Phosphorylase from Catellatospora ferruginea
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概要
- 論文の詳細を見る
Trehalose phosphorylase was purified from the cell extracts of Catellatospora ferruginea. The enzyme had an apparent molecular weight of 400,000 by gel filtration and 98,000 by SDS-PAGE, suggesting that the enzyme was a tetramer. The enzyme was specific for trehalose in phosphorolysis and specific for β-D-glucose 1-phosphate in synthesis. In addition to D-glucose, D-xylose and D-fucose were also possible sugar acceptors during synthesis. Phosphate ions were a key to the activity and stability of the enzyme, controlling the equilibrium of the reversible reaction and the heat stability of the enzyme. The enzyme was strongly inhibited by p-chloromercuribenzoate and pyridoxal phos-phate. The enzyme was inactivated by heat or by storage frozen with ammonium chloride and lithium chloride.
- 社団法人日本農芸化学会の論文
- 1998-04-23
著者
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Masuda Tomomi
Tokyo Research Laboratories Kyowa Hakko Kogyo Co.ltd.
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AISAKA KAZUO
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co.Ltd.
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CHIKAMUNE TADASHI
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co.Ltd.
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KAMITORI KAZUYO
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co.Ltd.
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Aisaka K
Biofrontier Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Aisaka K
Japan Tobacco Inc. Osaka Jpn
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Aisaka Kazuo
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Kamitori Kazuyo
Tokyo Research Laboratories Kyowa Hakko Kogyo Co.ltd.
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Chikamune Tadashi
Tokyo Research Laboratories Kyowa Hakko Kogyo Co.ltd.
関連論文
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- Purification and Characterization of Trehalose Phosphorylase from Catellatospora ferruginea
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