Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation.
The conformational changes of the active site of creatine kinase (ATP: creatine N-phosphotransferase EC 2.7.3.2.) 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.
Bai
J H
JH
Department of Biological Science and Biotechnology, Tsinghua University, Beijing, P.R.China.
Zheng
S Y
SY
Zhou
H M
HM
D001665:Binding Sites; D003402:Creatine Kinase / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D019281:Dimerization; D006358:Hot Temperature; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D009764:o-Phthalaldehyde
D009764:o-Phthalaldehyde; D003402:Creatine Kinase