Ca2+ activated myosin-ATPase in cardiac myofibrils of rainbow trout, freshwater turtle, and rat.

The Ca(2+)-activated myosin-ATPase and its dependence on hypoxia were assessed in freshwater turtle, rainbow trout, and in some cases rat. At 20 degrees C and pH 7.3, the maximal ATPase activity was (mean +/- SEM): turtle 0.040 +/- 0.003, trout 0.090 +/- 0.005, and rat 0.12 +/- 0.004 mmol*min-1*g-1 myofibrillar dry weight. The turnover number was about three times lower for turtle than for trout. Trout is typically active at lower temperatures than turtle, and its myosin-ATPase activity was about three times lower at 10 degrees than at 20 degrees C. Addition of 12 mM phosphocreatine showed that the myosin-ATPase activity covered by myofibrillar creatine kinase was 22 +/- 2% for turtle, 14 +/- 2% for trout, and 69 +/- 5% for rat. At pH 6.8 relative to 7.3, the maximal M-ATPase activity was the same, whereas the Ca(2+)-sensitivity decreased, and more so for trout than for turtle. This difference disappeared, when trout myocardium was examined at 10 degrees C. P(i) (15 mM) affected neither maximal activity nor Ca(2+)-sensitivity. ADP, however, reduced maximal myosin-ATPase activity, and more so in trout than in turtle. In conclusion, the "slow"-type myosin, the low sensitivity of acidification and ADP, and the high creatine kinase/myosin-ATPase ratio in turtle relative to trout accord with the well-known ability of turtle myocardium to work during hypoxia. However, the difference in living temperature between turtle and trout obscures the situation (e.g. inclusion of rat data suggests that the creatine kinase/myosin-ATPase ratio is related to temperature.