Purification and Properties of Fructose-1, 6-Bisphosphatase from Germinating Castor Bean Endosperm
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概要
- 論文の詳細を見る
Two FDPase isozymes have been purified by DEAE-Sephadex column chromatography and gel filtration, and then characterized from endosperms of germinating castor beans (Ricinus communis). One of the enzymes is localized in the cytosol and the other is confined to plastids. There are physical, kinetic and regulatory differences between the isoenzymes. The Km value of cFBPase and p-FBPase for F-1, 6-BP was 8.2μM and 23.6μM, respectively. The optimum pH of c-FBPase was in the range 7.5-7.8, whereas the p-FBPase was 6.7. The p-FBPase being more negatively charged than the c-FBPase. The c-FBPase is regulated by AMP, and F-2<6-BP, whereas the p-FBPase is slightly regulated by AMP.
- 大阪府立大学の論文
- 1996-03-31
著者
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Abe Takato
Laboratory Of Applied Molecular Biology College Of Agriculture
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Ono Kaori
Laboratory Of Applied Molecular Biology College Of Agriculture
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Fujii Michiko
Laboratory Of Biochemistry College Of Agriculture
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Fujii Michiko
Laboratory Of Applied Molecular Biology College Of Agriculture
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MIGITA Hideyuki
Laboratory of Applied Molecular Biology, College of Agriculture
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Migita Hideyuki
Laboratory Of Applied Molecular Biology College Of Agriculture
関連論文
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