Properties of Purine Nucleoside Phosphorylase from Enterobacter cloacae

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概要

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• Purine nucleoside phosphorylase from Enterobacter cloacae KY3074 was partially purified by ammonium sulfate fractionation, column chromatography on DEAE-cellulose and DEAE-Sephadex A-50, and gel nitration on Sephadex G-100 and Sepharose 4B. The molecular weight of the enzyme was calculated to be about 87, 000 by a gel nitration method on Sephadex G-200. The enzyme was found to be most active at pH 7.5 to 8.5 and 50°C, stable between pH 7.0 and 7.3, and the activity was nearly lost above 70°C. The enzyme split 2-deoxyinosine and ribonucleosides. Lineweaver-Burk plots for phosphate were non-linear, showing substrate activation. The breakdown of inosine approached an equilibrium when approximately 14% of inosine was phosphorylated.

• 社団法人 日本農芸化学会の論文

著者

• Nakanishi Toru

  Tokyo Research Laboratory Kyowa Hakko Kogyo Co. Ltd.

• MACHIDA Yozo

  Tokyo Research Laboratory, Kyowa Hakko Kogyo Co.

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