Creatine kinase, energy-rich phosphates and energy metabolism in heart muscle of different vertebrates.

Maximal activities of creatine kinase, pyruvate kinase and cytochrome oxidase and total concentrations of creatine and phosphorylated adenylates were measured in cardiac muscle of hagfish, eight teleost species, frog, turtle, pigeon and rat. The ratio of creatine kinase to cytochrome oxidase with cytochrome oxidase as a rough estimate of aerobic capacity and cellular "energy turnover", was increased in myocardia of hagfish, turtle and crucian carp. These myocardia are likely to be frequently exposed to oxygen deficiency. In agreement with this, they possess a high relative glycolytic capacity as indicated by a high pyruvate kinase/cytochrome oxidase ratio. The creatine kinase/cytochrome oxidase ratio for the other myocardia varied within a factor of 2, except the value for cod myocardium which was below the others. Total creatine varied among species and was high in active species such as herring, pigeon and rat but also high in crucian carp. The variation in total concentration of phosphorylated adenylates was considerably less than the variation in total creatine. The high creatine kinase/cytochrome oxidase ratio in myocardia likely to be challenged by hypoxia may represent an enhanced efficiency for both "spatial" and "temporal" buffering of phosphorylated adenylates to attenuate the impact of a depressed energy liberation. As to the differences in total creatine, this factor influences not only the cellular energy distribution but possibly also contractility via an effect on the free phosphate level.