M. Christensen et al., CREATINE-KINASE, ENERGY-RICH PHOSPHATES AND ENERGY-METABOLISM IN HEART-MUSCLE OF DIFFERENT VERTEBRATES, Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 164(2), 1994, pp. 118-123
Maximal activities of creatine kinase, pyruvate kinase and cytochrome
oxidase and total concentrations of creatine and phosphorylated adenyl
ates were measured in cardiac muscle of hagfish, eight teleost species
, frog, turtle, pigeon and rat. The ratio of creatine kinase to cytoch
rome oxidase with cytochrome oxidase as a rough estimate of aerobic ca
pacity and cellular ''energy turnover'', was increased in myocardia of
hagfish, turtle and crucian carp. These myocardia are likely to be fr
equently exposed to oxygen deficiency. In agreement with this, they po
ssess a high relative glycolytic capacity as indicated by a high pyruv
ate kinase/cytochrome oxidase ratio. The creatine kinase/cytochrome ox
idase ratio for the other myocardia varied within a factor of 2, excep
t the value for cod myocardium which was below the others. Total creat
ine varied among species and was high in active species such as herrin
g, pigeon and rat but also high in crucian carp. The variation in tota
l concentration of phosphorylated adenylates was considerably less tha
n the variation in total creatine. The high creatine kinase/cytochrome
oxidase ratio in myocardia likely to be challenged by hypoxia may rep
resent an enhanced efficiency for both ''spatial'' and ''temporal'' bu
ffering of phosphorylated adenylates to attenuate the impact of a depr
essed energy liberation. As to the differences in total creatine, this
factor influences not only the cellular energy distribution but possi
bly also contractility via an effect on the free phosphate level.