Effect of pH and Urea on the Optical Rotation, Viscosity, and Adenosinetriphosphatase Activity of Myosin A*
نویسنده
چکیده
Earlier studies in this laboratory (1) and by other workers (Z-4) have suggested that the effect of alkaline pH and urea on myosin resulted in major structural alterations in the molecule. Many of these studies were concerned with the attempt at the isolation of subunits or small polypeptide fragments by the treatment of myosin with high urea concentrations for long periods of time or by exposure of the molecule to alkaline pH. No systematic studies on the effect of alkaline pH and urea on the physical properties of myosin have been reported simulatneously with their effect on the adenosinetriphosphatase activity of myosin. For this reason an investigation of myosin and actomyosin by means of optical rotation, viscosity, and adenosinetriphosphatase activity at various alkaline pH values and urea concentrations has been undertaken in an attempt to correlate structural changes in the molecule with changes in myosin adenosinetriphosphatase activity.
منابع مشابه
The dissociation and reassociation of the subunit polypeptide chains of myosin.
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