Octamers of mitochondrial creatine kinase isoenzymes differ in stability and membrane binding.

@article{Schlattner2000OctamersOM,
  title={Octamers of mitochondrial creatine kinase isoenzymes differ in stability and membrane binding.},
  author={Uwe Schlattner and Theo Wallimann},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 23},
  pages={17314-20}
}
Octamer stability and membrane binding of mitochondrial creatine kinase (MtCK) are important for proper functioning of the enzyme and were suggested as targets for regulatory mechanisms. A quantitative analysis of these properties, using fluorescence spectroscopy, gel filtration, and surface plasmon resonance, revealed substantial differences between the two types of MtCK isoenzymes, sarcomeric (sMtCK) and ubiquitous (uMtCK). As compared with human and chicken sMtCK, human uMtCK showed a 23-34… CONTINUE READING