Steady state kinetic studies of purified yeast plasma membrane proton-translocating ATPase.

@article{Koland1986SteadySK,
  title={Steady state kinetic studies of purified yeast plasma membrane proton-translocating ATPase.},
  author={John G. Koland and Gordon G. Hammes},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 13},
  pages={5936-42}
}
The plasma membrane H+-ATPase from bakers' yeast was purified and reconstituted with phosphatidylserine. The steady state kinetics of ATP hydrolysis catalyzed by the H+-ATPase were studied over a wide range of Mg2+ and ATP concentrations. Whereas MgATP was the substrate hydrolyzed, excess concentrations of either Mg2+ or ATP were inhibitory. The dependence of the steady state initial velocity of ATP hydrolysis on the concentration of MgATP at a fixed concentration of Mg2+ was sigmoidal rather… CONTINUE READING