Salt Effects on the Kinetics of the Electrogenic Na+ Transport in the Na,K-ATPase

In the experiments with caged H + , the dissociation constants of sodium ions were determined by measuring the capacitance incre ments initiated by fast pH shift and assuming

This observation alone is not sufficient to derive a quantitative pH dependency for the activation of MCS factors, as the effect is small and—as we shall see later—not only depends

(A) Post-Albers cycle of the Na,K-ATPase under physiological conditions. E 1 and E 2 are conformations of the ion pump with ion binding sites facing the cytoplasm and

(B) Kinetic simulations of the experimental fluorescence transients based on a reversible conformational change model (solid line; see Figure 5) and the rate constants,

Therefore, F max depends on pa- rameters specific for each vesicle preparation (enzyme activity, membrane conductance and lipid composition) and, as a consequence, no information

FIGURE 3 Fluorescence changes after subsequent CLT additions to the Na,K-ATPase corresponding to different steady-state fluorescence levels of the standard experiment in the absence (

Using simulations of the expected equilibrium behavior for different binding models based on thermodynamic data obtained from isothermal titration calorimetry we show that this

subunit is assumed to raise the Na + binding affinity as suggested by the current findings, as well as the stabilizing effects of FXYD 1 described recently.29 On