Temperature-pressure studies on magnesium-activated adenosinetriphosphatase from skeletal muscle

Abstract

The effects of pressure, temperature, and pH on the activity of purified rabbit skeletal muscle magnesium-activated ATPase were measured. The enzyme is rapidly and irreversibly inactivated by both temperature and pressure and shows no evidence of reversible denaturation. The extent of irreversible inactivation depends on the amount of pressure applied and is largest at the optimum pH of the enzyme.