Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation

Ji Hong Bai, Si Yang Zheng, Hai Meng Zhou

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

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 languageEnglish (US)
Pages (from-to)941-951
Number of pages11
JournalBiochemistry and Molecular Biology International
Volume45
Issue number5
DOIs
StatePublished - Aug 1998

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Genetics

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