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pubmed:abstractText |
The Ca2+-ATPase of sarcoplasmic reticulum was utilized to demonstrate an intrinsic regulation of enzyme catalysis, whereby the ratio of forward and reverse flow is altered by the binding of Ca2+ and Pi to the enzyme. This is related to displacement of internal equilibria among intermediate enzyme ligand complexes, independent of the overall equilibrium of the ATP in equilibrium ADP + Pi transformation. A very high energy conservation with a velocity of reverse flow approaching that of forward flow, was obtained by increasing the enzyme affinity for Pi in the presence of Me2SO.
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