Kinetic and thermodynamic control of ATP synthesis by sarcoplasmic reticulum adenosinetriphosphatase.

@article{Teruel1987KineticAT,
  title={Kinetic and thermodynamic control of ATP synthesis by sarcoplasmic reticulum adenosinetriphosphatase.},
  author={Jos{\'e} A Lozano Teruel and M Kurzmack and Giuseppe Inesi},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 27},
  pages={13055-60}
}
Several experimental parameters, critical to the analysis of ATP synthesis by sarcoplasmic reticulum ATPase, were determined experimentally. 1) The phosphorylated enzyme intermediate obtained with acetylphosphate in the presence of a Ca2+ gradient was shown to be entirely ADP sensitive but quite stable in the absence of added ADP. On the contrary, the phosphoenzyme obtained with ATP is unstable due to the ADP formed during the phosphoryl transfer reaction. For this reason, addition of ADP to… CONTINUE READING