Abstract
1. 1. The paper reports that rabbit muscle pyruvate kinase displays kinetic properties typical of a regulatory enzyme when examined at pH 7.4. 2. 2. Time-dependent conformational changes in the enzyme are shown. 3. 3. Reasons are suggested to explain why these properties have escaped attention. 4. 4. It is suggested that the results can be explained by assuming that the substrates of the enzyme and the activator, fructose-1, 6-diphosphate, induce conformational changes in the enzyme, some of which are antagonistic in their effects.
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