The Ca(2+)-ATPase of the scallop sarcoplasmic reticulum is of a cold-adapted type.

At 0 to 20 degrees C, the Ca(2+)-ATPase activity of the scallop sarcoplasmic reticulum (SR) was observed to be 7-60% of the peak activity at 30 degrees C, while the ATPase activity of the rabbit SR was 0-7% of its peak at 55 degrees C. The relative rabbit ATPase activity (0.7-7.0%) at 7-20 degrees C became higher (6-15 times) and lower (1/4-1/2), respectively, by the solubilization of the rabbit ATPase with a detergent, dodecyloctaethylenglycol monoether, and by the reconstitution of the ATPase with asolectin (soybean lecithin). No activity at 0 degrees C remained irrespective of these treatments. The relative scallop ATPase activity at 0-20 degrees C was, however, scarcely affected by such solubilization and reconstitution. In contrast to the rabbit ATPase, the scallop ATPase seems to be capable of operating independently without the help of the membrane lipid at low temperature.