@article{oai:omu.repo.nii.ac.jp:00009204,
 author = {FUJII, Michiko and MIGITA, Hideyuki and ONO, Kaori and ABE, Takato},
 journal = {Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and life sciences},
 month = {Mar},
 note = {application/pdf, 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., Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and life sciences. 1996, 48, p.109-118},
 pages = {109--118},
 title = {Purification and Properties of Fructose-1, 6-Bisphosphatase from Germinating Castor Bean Endosperm},
 volume = {48},
 year = {1996}
}