The study demonstrates intrinsic regulation of Ca2+-ATPase catalysis through displacement of internal equilibria, achieving high energy conservation when enzyme affinity for Pi is increased with Me2SO.
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.
No takes yet. Share an insight, caveat, or question.
Meis et al. (1985) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: