Abstract
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.
Original language | English (US) |
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Pages (from-to) | 941-951 |
Number of pages | 11 |
Journal | Biochemistry and Molecular Biology International |
Volume | 45 |
Issue number | 5 |
DOIs | |
State | Published - Aug 1998 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Genetics