Isozymes of creatine phosphokinase and myokinase in human heart and skeletal muscle.

The isozyme patterns of creatine phosphokinase (CPK) and myokinase (MK) were investigated in biopsy material from human heart and skeletal muscle. The protein separation was performed on crude muscle homogenates by means of flat-bed isoelectric focusing. Two isozymes were demonstrated for each enzyme, irrespective of the sampling site. The pI values were, on the average, 9.8 (MK-1) and 8.9 (MK-2), 7.2 (CPK-1) and 6.9 (CPK-2), respectively. MK-1 and CPK-1 constituted an average of 81% and 70% of total staining density for each enzyme, respectively. The relative contribution of MK-1 differed, however. Heart muscle showed the highest values (mean 91%) and vastus lateralis the lowest (mean 74%). The mean value for soleus was 86% MK-1. Furthermore, the percentage of MK-1 present was negatively correlated with the percentage of fast twitch fibres in m. vastus lateralis (r = -0.67). No corresponding differences could be demonstrated for CPK isozyme distribution. In conclusion, it was demonstrated that MK and CPK each occurred as two isozymes in human heart and skeletal muscle, and that the relative distribution of MK isozymes, in contrast to CPK, was related to muscle fibre type composition, and thus to the metabolic profile of the muscle.