Plant Physiol. Drug Metab Dispos
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Plant Physiology 85:13-16 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Ion-Exchange Chromatography Separates Activities Synthesizing and Degrading Fructose 2,6-Bisphosphate from C3 and C4 Leaves but Not from Rat Liver 1

Fraser D. Macdonald, Qun Chou and Bob B. Buchanan

Division of Molecular Plant Biology, Hilgard Hall, University of California, Berkeley, California 94720

Fructose-6-phosphate,2-kinase and fructose-2,6-bisphosphatase were separated on the basis of charge from leaves of C3 (spinach, lettuce, and pea) and C4 (sorghum and amaranthus) plants but not from rat liver—a tissue known to contain a bifunctional enzyme with both activities. [2-32P]Fructose 2,6-bisphosphate binding experiments also suggest that the major forms of these activities reside on different proteins in leaves.


1 Supported in part by grants from the Metabolic Biology (PCM-8314892), and United States-China (INT-8311897) Programs of the National Science Foundation.




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T. Furumoto, M. Teramoto, N. Inada, M. Ito, I. Nishida, and A. Watanabe
Phosphorylation of a Bifunctional Enzyme, 6-Phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase, is Regulated Physiologically and Developmentally in Rosette Leaves of Arabidopsis thaliana
Plant Cell Physiol., October 1, 2001; 42(10): 1044 - 1048.
[Abstract] [Full Text] [PDF]




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Copyright © 1987 by the American Society of Plant Biologists