Kinetic properties of the isoenzymes of human creatine phosphokinase.

Kinetic properties and the functional role of particulate MM-isoenzyme of creatine phosphokinase bound to heart muscle myofibrils.

Fractional extractions of heart muscle have revealed that about 30% of cellular creatine phosphokinase activity are located in mitochondria and about 20% are bound to myofibrils [ 1,2] . The presence of significant creatine phosphokinase activity in heart and skeletal muscle myofibrils has been demonstrated also in studies of isolated myofibrillar preparations [ 1,3,4] . This particulate enzyme...

Analysis of tissue creatine phosphokinase isoenzymes by histoelectrophoresis.

Creatine kinase in serum: 4. Differences in substrate affinity among the isoenzymes.

The goal of this work was to find out whether it is possible to measure all three creatine kinase isoenzymes under the same reaction conditions in spite of their different kinetic properties. We found the tightest substrate binding for purified human BB, followed by the MB And MM isoenzyme preparations for both creatine phosphate and ADP. An increase in substrate concentration usually resulted ...

Studies on serum creatine phosphokinase isoenzyme. Seven cases of tetraplegia in the dog.

Release of enzymes from adult rat heart myocytes.

The release of lactic dehydrogenase, creatine phosphokinase, and aspartate aminotransferase from initially viable, metabolically competent adult rat heart myocytes has been examined. Freshly isolated cells contain levels of total lactic dehydrogenase, creatine phosphokinase, and aspartate aminotransferase, as well as lactic dehydrogenase and creatine phosphokinase isoenzyme profiles that are qu...