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  • Journal
    Digital Access Sage v. 1-, 2001-
  • Article
    Williams GJ, Collins S, Muir JR, Stephens MR.
    Recent Adv Stud Cardiac Struct Metab. 1975;5:273-80.
    The ability of cardiac myosin, actomyosin, and myofibrils to hydrolyze ATP has been studied at varying hydrogen and calcium ion concentrations. The ATPase activity of dog cardiac myofibrils was measured over the pH range of 6.5-7.4, as the calcium ion concentration was varied from 0-1.5 X 10(-4) M. The ATPase of these myofibrils, and of rabbit cardiac myosin and actomyosin was also measured in the absence of ionic calcium over the pH range 6-9. The Km of MgATP of cardiac myofibrils was studied over the pH range 6.5-7.4. In the absence of calcium ions, myofibrillar, myosin, and actomyosin ATPase activities are maximal at pH 8.0. At any given calcium ion concentration, the myofibrillar ATPase is depressed by lowering pH. The results suggest that the influence of hydrogen ions on the ability of myofibrils to hydrolyze ATP is complex, and may not only be the result of a simple competition between hydrogen and calcium ions for binding sites on troponin.
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