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Effects of cations on high-affinity and low-affinity ATP-binding sites of (Na+, K+)-ATPase as studied by disulfides of thioinosine triphosphate and its analogue.

1 
Binding of the disulfides of thioinosine triphosphate and thioinosine 5′-[β,γ-methylene]triphosphate, (SnoPPP), and (SnoPP[CH2]P)2, to the (Na+,K+)-ATPase in the presence of 10mM EDTA results in an inactivation of the enzyme. 
 
2 
K+, Rb+ and Cs+ protect the high-affinity and low-affinity binding sites of (Na+,K+)-ATPase against inactivation by (SnoPPP), and (SnoPP[CH2]P)2. The protection constants increase with the atomic radii of the monovalent cations. 
 
3 
The protective effects of low concentrations of K +, Rb+ and Cs+ on the inactivation of the (Na+,K+)-ATPase by (SnoPP[CH2]P)2 are smaller than the effects on the inactivation by (SnoPPP)2. The electronegativity of the bridge atom between β and θ phosphate groups obviously has a function on the mode of action of monovalent cations. 
 
4 
High concentrations of K+, Rb+ and Cs+ accelerate the inactivation of the high-affinity and low-affinity binding sites of the (Na+,K+)-ATPase by (SnoPP[CH2]P)2. 
 
5 
Na+ concentrations below 10 mM advance the inactivation of the high-affinity and low-affinity binding sites of the (Na+, Kplus;)-ATPase by (SnoPPP)2 and (SnoPP[CH2]P)2. Na+ concentrations above 10 mM protect against inactivation. 
 
6 
K+ raises the activatingeffect in the presence of low concentrations of Na+ by inactivation through (SnoPPP)2 and (SnoPP[CH2]P)2. The protective effect of higher concentrations of Na+ is amplified by K+, when using (SnoPPP)2, whereas it is reduced in the case of (SnoPP[CH2]P)2. 
 
7 
Mg2+ concentrations up to 5 mM advance the inactivation of the high-affinity and low-affinity binding sites of the (Na+, K+)-ATPase by (SnoPPP)2 and (SnoPP[CH2]P)2. Higher concentrations of Mg2+ have a protective effect. 
 
8 
The monovalent cations (Na+, K+, Rb+, Cs+) and Mg2+ act in a noncompetitive manner with respect to nucleotide binding. It is therefore concluded, that they are effective by inducing conformational changes of the enzyme.