The catalytic activity and activation energy of creatine kinase isoenzymes.
The catalytic activity and activation energy of an enzyme are obtained by measuring the rate of the enzymic reaction at two different temperatures. With the aid of the Arrhenius equation, these two parameters can be used to calculate a value proportional to the quantity of enzyme. Using this approach to investigate the isoenzymes of creatine kinase, it was shown that the activation energy increased in the order creatine kinase MM, MB, BB. Mixtures of the isoenzymes showed an apparent mean activation energy, which likewise could be determined using the Arrhenius equation. Ageing of the isoenzymes results in an exponential decrease of catalytic activity, accompanied by a continuous increase in activation energy, the calculated quantity of enzyme remaining constant. Inactivation is therefore not an all-or-nothing process; rather a stepwise inactivation of individual molecules must be assumed. The results of these ageing experiments and observations by other authors suggest that a similar inactivation occurs in vivo.
D003402:Creatine Kinase / Q000378:metabolism*; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D007527:Isoenzymes; D007700:Kinetics; D008433:Mathematics; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D013816:Thermodynamics; D014599:Uterus / Q000201:enzymology
D007527:Isoenzymes; D003402:Creatine Kinase