Purification and properties of ribose phosphate isomerase from tobacco leaves
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概要
- 論文の詳細を見る
The purification of ribose 5 phosphate isomerase from tobacco leaves is described. The procedure used extends over six steps to a 14.4% yield of a homogeneous protein purified 288-fold from the crude extract. The enzyme has a molecular weight of 54,000 daltons. The pH optimum (8.2), Km for ribose 5 phosphate (1.6 × 10^<-3> M), amino acid composition and isoelectric point (pI=5.13) have been determined. Comparison of these properties with those of yeast and animal isomerases is discussed.
- 日本植物生理学会の論文
著者
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Tanabe Yoko
Central Research Institute Japan Tobacco And Salt Public Corporation
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Tanabe Yoko
Central Research Institute The Japan Tobacco Public Corporation
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KAWASHIMA Nobumaro
Central Research Institute, Japan Tobacco Inc.
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Kawashima Nobumaro
Central Research Institute Japan Tobacco And Salt Public Corporation
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Kawashima Nobumaro
Central Research Institute The Japan Tobacco Public Corporation
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