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Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and life sciences >
Vol.48 >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10466/2806

Title: Purification and Properties of Fructose-1, 6-Bisphosphatase from Germinating Castor Bean Endosperm
Authors: FUJII, Michiko
MIGITA, Hideyuki
ONO, Kaori
ABE, Takato
Issue Date: 31-Mar-1996
Publisher: University of Osaka Prefecture
Citation: Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and life sciences. 1996, 48, p.109-118
Abstract: 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.
URI: http://hdl.handle.net/10466/2806
Appears in Collections:Vol.48

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