Isoenzyme-specific thermostability of human cytosolic creatine kinase

Yan Song Gao, Tong Jin Zhao, Zhe Chen, Chang Li, Yin Wang, Yong Bin Yan, Hai Meng Zhou

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Creatine kinase (CK) is a key enzyme involved in intracellular energy homeostasis. The distinct tissue distribution of muscle CK (MMCK) and brain CK (BBCK) implies that they function under conditions facing dissimilar environmental stresses. We found that MMCK and BBCK were significantly different in their stability and reversibility against heat stress. MMCK was more stable than BBCK, and BBCK was only marginally stable and began to inactivate at temperatures just above normal body temperature. The thermal inactivation of MMCK was fully irreversible, whereas that of BBCK was highly reversible at temperatures below 55°C. These differences in stability were proposed to be closely correlated to the isoenzymes' adaptation to the distinct tissue environments.

Original languageEnglish (US)
Pages (from-to)27-32
Number of pages6
JournalInternational Journal of Biological Macromolecules
Issue number1
StatePublished - Jul 2010


  • Creatine kinase
  • Isoenzyme
  • Reversiblility
  • Thermostability
  • Tissue-specific stability

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology
  • Biochemistry


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