An activation factor of liver phosphofructokinase.

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Abstract
Pure phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) from rat liver is strongly inhibited by ATP; crude phosphofructokinase is only slightly inhibited by ATP. A factor that is removed from the enzyme during purification and can prevent the inhibition of phosphofructokinase by ATP has been isolated. The factor can be resolved into 3 components that differ in MW, as shown by gel filtration on Sephadex G-25. These factors overcome the ATP inhibition but have no effect on the catalytic activity under the optimum assay conditions. AMP acts synergistically with the activation factor in reversing ATP inhibition. The activation of phosphofructokinase by the activation factor and AMP may be sufficient to account for the glycolytic flux in the liver.