Abstract
1. 1. The enolase activity measure of Warburg and Christian (7) has been shown not to be strictly valid. The measurement of the initial velocity of the enolase reaction has been described and the results compared with those obtained by the Warburg-Christian method. The possible kinetic significance of the deviation has been discussed. 2. 2. The kinetics of the Mg ++ activation of enolase has been studied at several pH values. The physical meaning of the kinetic constants has been discussed in terms of different mechanisms of activation. It is concluded that the binding of Mg ++ to enolase decreases markedly below pH 6.8. 3. 3. The interaction of enolase with Zn ++ at different pH values has been studied by equilibrium dialysis. The results confirm the conclusion from the kinetic experiments. It has been suggested that an imidazole group of histidine is involved in the binding of the activating ion to enolase.
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