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Phosphatase activity and potassium transport in liposomes with sodium potassium atpase incorporated


Biochimica et Biophysica Acta 1103(1): 85-93
Phosphatase activity and potassium transport in liposomes with sodium potassium atpase incorporated
We have used liposomes with incorporated pig kidney Na+,K+-ATPase to study vanadate sensitive K+-K+ exchange and net K+ uptake under conditions of acetyl- and p-nitrophenyl phosphatase activities. The experiments were performed at 20.degree. C. Cytoplasmic phosphate contamination was minmized with a phosphate trapping system based on glycogen, phosphorylase a and glucose-6-phosphate dehydrogenase. In the absence of Mg2+ (no phosphatase activity) 5-10 mM p-nitrophenyl phosphate slightly stimulated K+-K+ exchange whereas 5-10 mM acetyl phosphate did not. In the presence of 3 mM MgCl2 (high rate of phosphatase activity) acetyl phosphate did not affect K+-K+ exchange whereas p-nitropheynl phosphate induced a greater stimulation than in the absence of Mg2+; a further addition of 1 mM ADP resulted in a 35-65% inhibition of phosphatase activity with an increase in K+-K+ exchange, which sometimes reached the levels seen with 5 mM phosphate and 1 mM ADP. The net K+ uptake in the presence of 3 mM MgCl2 was not affected by acetyl phosphatase or p-nitrophenyl phosphate, whereas it was inhibited by 5 mM phosphate (with and without 1 mM ADP). The results of this work suggest that the phosphatase reaction is not by itself associated to K+ translocation. The ADP-dependent stimulation of K+-K+ exchange in the presence of phosphatase activity could be explained by the overlapping of one more step/s of the reversible phosphorylation from phosphate with the phosphatase cycle.


Accession: 007650837



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