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Ion-Exchange Chromatography Separates Activities Synthesizing and Degrading Fructose 2,6-Bisphosphate from C3 and C4 Leaves but Not from Rat Liver
Author(s) -
Fraser D. Macdonald,
Qun Chou,
Bob B. Buchanan
Publication year - 1987
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.85.1.13
Subject(s) - fructose 2,6 bisphosphate , fructose , phosphofructokinase 2 , spinach , biochemistry , chemistry , enzyme , bifunctional , chenopodiaceae , botany , biology , glycolysis , catalysis , phosphofructokinase
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.

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