Purification and Characterization of Adenosine Deaminase from Klebsiella sp. LF 1202
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概要
- 論文の詳細を見る
Adenosine deaminase was induced when the cells of Klebsiella sp. LF 1202 were cultured in the medium containing adenosine as a sole source of carbon and nitrogen. The induction was partially repressed by the addition of ammonium sulfate in the medium. The amount of adenosine deaminase reached approzimately 4.6% of the total intracellular soluble proteins. The enzyme was purified approximately 22-fold with a 25% activity yield. The enzyme was a monomer with a molecular weight of 26,000. The optimal activity was obtained at pH 8.0,37℃, and the K_m value for adenosine was 37μM. Metal ions such as Zn^<2+>, Co^<2+>, Fe^2 and Ni^+ inhibited the activity of the enzyme. Sulfhydryl blocking agents such as p-chloromercuribenzoate and HgCl_2 were also found to be potent inhibitors for adenosine deaminase.
- 社団法人日本生物工学会の論文
- 1991-02-25
著者
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Inoue Y
Research Institute For Food Science Kyoto University
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Inoue Yoshiharu
Research Institute For Food S-cience Kyoto University
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Inoue Yoshiharu
Research Institute For Food Science Kyoto University
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KIMURA AKIRA
Research Institute for Food Science, Kyoto University
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Kimura Akira
Research Institute For Food Science Kyoto University
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Ling Feng
Research Institute for Food Science, Kyoto University
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Inoue Y
Kyoto Univ. Kyoto
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Kimura A
Research Institute For Food Science Kyoto University
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Ling Feng
Research Institute For Food Science Kyoto University
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Kimura Akira
Research Center for Solar Energy Chemistry, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan
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