Phosphofructokinase was purified extensively from beef heart and studied kinetically at pH 6.25 and low hexose-monophosphate concentrations to observe its behavior under conditions similar to those prevailing in cell-free extracts with oscillatory control. Adenosine 5′-triphosphate was a very powerful inhibitor at this pH, and the inhibition was prevented by AMP, ADP, and FDP. Adenosine 5′-monophosphate induced an activation even when the ATP concentration was kept below its inhibitory value. The results indicate that the DPNH oscillations observed in cell-free extracts are probably due to the variable activity of phosphofructokinase under the influence of the adenine nucleotides and fructose 1,6-diphosphate. © 1968.