Presence of a low-affinity nucleotide binding site on the (K+ + H+)-ATPase phosphoenzyme.

@article{Jong1986PresenceOA,
  title={Presence of a low-affinity nucleotide binding site on the (K+ + H+)-ATPase phosphoenzyme.},
  author={M L Helmich-de Jong and Sjenet E van Emst-de Vries and Herman G. P. Swarts and F M A H Schuurmans Stekhoven and Jan Joep H. H. M. De Pont},
  journal={Biochimica et biophysica acta},
  year={1986},
  volume={860 3},
  pages={641-9}
}
The effects of Mg2+ and nucleotides on the dephosphorylation process of the (K+ + H+)-ATPase phosphoenzyme have been studied. Phosphorylation with [gamma-32P]ATP is stopped either by addition of non-radioactive ATP or by complexing of Mg2+ with EDTA. The dephosphorylation process is slow and monoexponential when dephosphorylation is initiated with ATP. When phosphorylation is stopped by complexing of Mg2+ the dephosphorylation process is fast and biexponential. The discrepancy could be… CONTINUE READING