Steady-state levels of phosphorylated intermediates of (Na,K)-ATPase monitored with oligomycin and anthroylouabain.

@article{Fortes1984SteadystateLO,
  title={Steady-state levels of phosphorylated intermediates of (Na,K)-ATPase monitored with oligomycin and anthroylouabain.},
  author={P. A. Fortes and J. Lee},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 18},
  pages={
          11176-9
        }
}
We present experiments designed to test whether or not the ADP-sensitive (E1P) and the K-sensitive (E2P) phosphoenzyme forms of (Na,K)-ATPase are intermediates of ATP hydrolysis in the presence of Na and K. We have used the apparent rate constant of anthroylouabain binding, k' on, and its inhibition by oligomycin to monitor the steady-state levels of E2P and E1P, respectively. We have measured k' on in purified dog kidney (Na,K)-ATPase at 37 degrees C as a function of Na, K, and MgATP or Mg… Expand
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Oligomycin inhibition of Na,K,ATPase
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