Purification and Some Properties of Alkaline Proteinase Produced by Pseudomonas maltophilia
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概要
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An organism capable of producing an alkaline proteinase was isolated and identified as Pseudomonas maltophilia. By simple Sephadex-gel chromatographies, the alkaline proteinase was purified to homogeneity with a specific activity 74-fold higher than that of the culture broth. The purified enzyme had a molecular weight of 46, 000 consisting of 19, 000 and 27, 000 molecular subunits. The optimum pH and temperature were pH 10.5 and 55°C, respectively. Calcium ion activated and stabilized the enzyme activity. The enzyme was inhibited by ethylenediaminetetraacetate, phenylmethylsulfonyl fluoride and chymostatin, indicating that the enzyme was a serine metalloenzyme.
- 社団法人 日本農芸化学会の論文
著者
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Kobayashi Tohru
Tochigi Research Laboratories Kao Corporation
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Ito Susumu
Tochigi Research Laboratories Kao Corporation
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OGASAWARA Akira
Tochigi Research Laboratories, Kao Corporation
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SAITOH Masahiro
Tochigi Research Laboratories, Kao Corporation
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