SUMMARYThe effect of freeze‐drying on the denaturation of myosin A and myosin B prepared from rabbit skeletal muscle and of heavy meromyosin derived from trypsin‐treated myosin A was investigated by measurement of adenosine tri‐phosphatase activities and by solubilities. The results show that the myosins undergo denaturation through the process of freeze‐drying. Factors involved in the denaturation are the pH and ionic strength of the solution and the dehydration. The denaturation is inhibited by the addition of sucrose to the
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