INFLUENCE OF pH AND TEMPERATURE ON MYOSIN INACTIVATION

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Abstract
The inactivation of myosin adenosine triphosphatase activity was studied in 0.6 M potassium chloride solution at pH ranging from 7.0 to 10.8 and for 5 °C to 40 °C. The inactivation is a first-order process with respect to time and 0.6th order with respect to the concentration of protein. The rate of inactivation is independent of the pH for pH 7.0 to pH 8.5 at 35 °C and increases rapidly with pH at higher pH. At 12 °C, close to pH 10.4, the rate is inversely proportional to the 4.5th power of the hydrogen ion concentration. The energies of activation are 56 kcal mole−1at pH 8.0 and 58 kcal mole−1at pH 10.5. A discussion of the data stresses the importance of structural changes and indicates a possible role for the electrostatic charge in the inactivation process.

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