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Octamers of Mitochondrial Creatine Kinase Isoenzymes Differ in Stability and Membrane Binding
Journal of Biological Chemistry
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 23-34doi:10.1074/jbc.m001919200 pmid:10748055 fatcat:q7m2mgo3yrfzlplfctnp7qgepq