Myosin ATPase activity in an estuarine decapod crustacean,Scylla serrata,as a function of salinity adaptation

The myosin ATPase activity of the flexor muscle of an estuarine crab, Scylla serrata, was studied in relation to salinity adaptation. The enzyme is activated more by calcium than by magnesium; it exhibits maximum activity at pH 9.0, and substrate inhibition above 0.5 mM ATP. The enzyme activity increases in crabs adapted to higher salinities. The enzyme from normal (70% sea water) crabs shows two pH optima; one at pH 7.0, the other at pH 9.0. The neutral optimum shifts to pH 6.0 upon adaptation to full strength sea water, but disappears upon adaptation to 25% sea water. The enzyme from normal crabs shows an optimum at 30 °C; adaptation to full strength sea water raises this optimum to 38 °C, whereas adaptation to 25% sea water decreases it to 24 °C. These changes are discussed in relation to estuarine conditions.