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Abstract
The ATPase activity of myosin from chicken gizzard measured in the presence of either Mg 2+ or Ca 2+ is increased in the absence of dithiothreitol or upon reaction with Cu 2+, o-iodosobenzoate, or N-ethylmaleimide. Iodosobenzoate or Cu 2+ produce no change in K +(EDTA)-ATPase while N-ethylmaleimide produces a decrease. These treatments also make the actin-activated ATPase insensitive to Ca 2+ when assayed in the presence of tropomyosin and a partially purified myosin light chain kinase. Phosphorylation of N-ethylmaleimide modified myosin remains dependent on Ca 2+ and therefore appears not to be required for activation by actin of the ATPase activity of modified myosin.
Published Version
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