Abstract
Isoenzymes of phosphofructokinase are present in the endosperm of developing seeds of Ricinus communis L. DEAE-Sephacel chromatography will separate the isoenzymes and can be used to identify them as cytosolic and plastid activities. Plastid phosphofructokinase represents approximately 60% of the total phosphofructokinase activity in this tissue. The isoenzymes have different kinetic properties. The plastid phosphofructokinase is activated by sodium phosphate at pH 6.8 and inhibited by sodium sulfate at pH 7.2, whereas the activity of cytosolic phosphofructokinase is much less sensitive to these anions under the same assay conditions. A procedure has been developed to purify the endosperm plastid phosphofructokinase using ion-exchange chromatography and 5′-AMP affinity chromatography. The molecular weight of plastid phosphofructokinase is 175,000 as estimated by gel filtration.
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