Stabilization of ribose-5-phosphate isomerase from tobacco
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概要
- 論文の詳細を見る
The highly purified ribose phosphate isomerase from tobacco leaves is heat labile. 0.2% of various kinds of proteins stabilized isomerase activity when Mg^<++> was present. 1 × 10^<-3>% Polyethyleneglycol 2,000 showed the same effect as the proteins did. Smaller polyethyleneglycols were less effective. Polyhydroxyl compounds showed little effect. Mn^<++> or Sr^<++> was also effective as a stabilizer instead of Mg^<++>.
- 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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KAWASHIMA Nobumaro
Central Research Institute, Japan Tobacco Inc.
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Kawashima Nobumaro
Central Research Institute Japan Tobacco And Salt Public Corporation
関連論文
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- Changes in the Contents of Free and Protein Amino Acids in Tobacco Seeds and Placentae during Maturation
- Purification and properties of ribose phosphate isomerase from tobacco leaves
- Comparison of Stigma Fatty Acid Composition between Male Sterile and Fertile Tobacco Plants(Biological Chemistry)
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- Total Fatty Acid and Polar Lipid Content in Developing Flower of Nicotiana tabacum
- Changes in Total and Polar Lipids and Their Fatty Acid Composition in Tobacco Leaves during Growth and Senescence
- Stabilization of ribose-5-phosphate isomerase from tobacco
- Comparison of Free and Bound Amino Acids in White and Green Tissues of Variegated Tobacco Plants
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