Abstract
1. 1. A 120-kDa (Ca2+ + Mg2+)-dependent ATPase was purified from the freshwater/land crab Potamon potamios muscle sarcoplasmic reticulum. 2. 2. The enzyme showed two Km values for ATP of 40 and 330 mM at 10–75 and > 75 μM ATP concentrations, respectively. Km values for calcium and magnesium were 2 and 294 μM, respectively. 3. 3. Optimal enzyme activity was observed at pH 7.5 and the Arrhenius plot showed a break at 25°C. 4. 4. An alternative method for the simultaneous purification of P. potamios(Ca2+ + Mg2+)- and (Na+ + K+)-dependent ATPase enzymes is also described.
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