The purpose of this study was to investigate the kinetic properties of human
creatine kinase (CK) isoenzymes partially purified from heart and skeletal muscle. Utilizing
the backward CK-catalyzed reaction of creatine phosphate + ADP ^ creatine + ATP, K
values for heart and skeletal muscle CK MM (3.7 mmol/1) were significantly (p < 0.05)
greater than CK MB (2.1 mmol/1) which were significantly (p < 0.05) greater than mitochondrial
CK (1.8 mmol/1) at variable creatine phosphate and fixed ADP concentrations. However,
K(m) values for similar isoenzymes from the two different tissues, i.e., CK MB from heart
vs. skeletal muscle, were not different. These results show that kinetic analysis of CK isoenzymes
cannot differentiate the tissue source of elevated blood CK isoenzymes after the acute
stress of long distance running or after acute myocardial infarction.