The conformational changes of the active site of creatine kinase (ATP: creatine N-phosphotransferase EC 18.104.22.168.) during thermal denaturation was followed by changes in fluorescence at the active site of the enzyme labeled by o-phthalaldehyde. Conformational changes of the active site occurred at the same time as inactivation of the enzyme. The active site changes occurred before the denaturation of the enzyme molecule as a whole was detected. The above results showed that the thermal inactivation of the creatine kinase was due to the conformational changes of its active sites.
All Science Journal Classification (ASJC) codes
- Molecular Biology