Abstract
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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.