Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells. |
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Authors: | R C Woledge and P J Reilly |
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Institution: | Department of Physiology, University College London, United, Kingdom. |
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Abstract: | The enthalpy change for the hydrolysis of phosphorylcreatine (PCr) by hydrochloric acid or by alkaline phosphatase was observed at 0, 25, and 37 degrees C. The value for delta H is -44 kJ mol-1 under alkaline, Mg2+-free conditions and is almost independent of temperature, ionic strength, and concentration of reactants. In muscle the reaction is accompanied by a transfer of protons from the buffers (largely histidine) to orthophosphate, release of Mg2+ from PCr, and binding of Mg2+ to orthophosphate. Measurements are reported of the heats of these processes. The calculated value of the overall heat of hydrolysis of PCr (including these processes) at pH 7, pMg 3 is -35 kJ mol-1. |
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