Abstract
The process of the denaturation of “myosin B” solution was studied by the measurement of ATPase activity, SH groups, sedimentation behaviour and flow birefringence. When “myosin B” solution was stored at lower temperature, lower pH or higher ionic strength, the interaction between myosin A and actin became less strong, and further storage brought about an irreversible dissociation. The condition for measuring Mg-modified ATPase activity of “myosin B” at low ionic strength was explained in the relation with superprecipitation.
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