Human myocardial and skeletal muscle enzyme activities: creatine kinase and its isozyme MB as related to citrate synthase and muscle fibre types.

Activities of myocardial and skeletal muscle total creatine kinase (CK) and its isozyme MB were related to the oxidative capacity [measured as the citrate synthase (CS) activity] and to the contractile characteristics (estimated as the percentage of type I muscle fibres). Skeletal muscle biopsies were obtained both from physically trained and untrained men and myocardial biopsies from patients subjected to open-heart surgery performed because of mitral or aortic valve disease. Enzyme activities were determined on freeze-dried muscle specimens. The CK-MB activity was about twice as high in trained skeletal muscle as in untrained ones reaching the myocardial level. The total CK activity was about three times higher in skeletal muscle than in myocardium; the myocardium, however, had CS activity 3-4 times larger than that of skeletal muscle. A close correlation was demonstrated between activities of CK-MB on one hand and CS (r = 0.76) or percentage type I fibres (r = 0.83) on the other hand suggesting a connection between CK-MB activity and the oxidative capacity of the cell. This was in contrast to total CK where different regressions were obtained when comparing the myocardium and the skeletal muscle of trained or untrained men. In conclusion, CK-MB activity in trained skeletal muscle in athletes were similar to that in myocardium. CK-MB was related to the oxidative capacity and formation of cellular energy in skeletal and heart muscle.