Abstract
Previous work indicated that certain conditions favoring moderate interaction of myosin with the fluorescent dye, ANS, corresponded to conditions favorable for ATP-ase activity of myosin, but conditions leading to extensive dye-binding corresponded to loss of enzymic activity. The present study indicates that two additional conditions resulting in a progressive decline in ATPase activity are also accompanied by a progressive increase in dye-binding: slow aging at 4 ° and brief exposure to temperatures from 25 to 50 °. The results are interpreted as reflecting a conformational change in the protein which reduces the effectiveness of myosin as an enzyme and exposes nonpolar groups conductive to ANS binding.
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