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By means of circular dichroism measurements in the range from 210-240 nm and 250-300 nm it is shown that conformational changes of the phosphofructokinase from rabbit muscle correlate with the action of effectors on the enzyme. The postulated active and inactive states differ in the secondary structure. Addition of activators causes a conformational change which is interpreted as the transition of the inactive into the active state. At 210-240 nm no reversion could be observed but at 250-300 nm there are some indications for at least partial reversion.
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