Purification and Characterization of Thermostable Purine Nucleoside Phosphorylase of Bacillus stearothermophilus JTS 859(Biological Chemistry)
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概要
- 論文の詳細を見る
A thermostable purine nucleoside phosphorylase has been purified more than 800-fold from Bacillus stearothermophilm JTS 859. The enzyme had a molecular weight of 68,000 consisting of 2 identical subunits (M_w, 34,000). The isoelectric point of the enzyme was 4.7. The enzyme did not contain cysteine. The optimal pH of the enzyme reaction was from 7.5 to 11.0. The Michaelis constants for inosine, guanosine, 2'-deoxyinosine, and 2'-deoxyguanosine were 0.22, 0.14, 0.20, and 0.10mM, respectively. The optimal temperature of the reaction was 80℃. The half-life of the enzyme was 16hr in 20mM potassium phosphate and 1mM inosine (pH 7.0) at 80℃, and no decrease of the enzyme activity was observed at least for the first 30hr at 70℃.
- 社団法人日本農芸化学会の論文
- 1989-08-23
著者
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Hori N
Tobacco Science Research Laboratory
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Hori Nobuaki
Central Research Institute Japan Tobacco Inc.
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Mikami Y
Chiba Univ. Chiba Jpn
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Hori Nobuaki
Tobacco Science Research Laboratory Japan Tobacco Inc.
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WATANABE Mutsumi
Tobacco Science Research Laboratory, Japan Tobacco Inc.
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YAMAZAKI Yoshinari
Tobacco Science Research Laboratory, Japan Tobacco Inc.
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MIKAMI Yoichi
Tobacco Science Research Laboratory, Japan Tobacco Inc.
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Mikami Yoichi
Tobacco Science Research Laboratory
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Mikami Yoichi
Central Research Institute The Japan Tobacco 〓 Salt Public Corporation
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Hori Nobuaki
Tobacco Science Research Laboratory
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Yamazaki Y
Agency Of Industrial Science And Technology Ibaraki Jpn
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Mikami Y
Tokyo Laboratory Yuki Gosei Kogyo Co. Ltd.
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