Abstract
IT is well known that the Mg++-activated ATPase of actomyosin extracted as the complex from muscle, “natural” actomyosin, is inhibited by low concentrations of ethylene dioxybis (ethyleneamino) tetra-acetic acid (EGTA), a property not possessed by actomyosin prepared from separately purified actin and myosin1. During a study of the factors responsible for the differences in enzyme behaviour of these two preparations a simple procedure has been developed which enables “natural” actomyosin to be readily converted to so-called “desensitized” actomyosin, the behaviour of which resembles actomyosin prepared from the independently purified actin and myosin in that its Mg++-activated ATPase is no longer sensitive to EGTA2,3. It was noted that in addition to the difference in sensitivity to EGTA of the two preparations the specific ATPase activity of “natural” actomyosin in the presence of Ca++ was 30–50 per cent of that of the desensitized actomyosin.
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