The K(+) affinity of gastric H(+),K(+)-ATPase is affected by both lipid composition and the beta-subunit.

@article{Hermsen2000TheKA,
  title={The K(+) affinity of gastric H(+),K(+)-ATPase is affected by both lipid composition and the beta-subunit.},
  author={Harm P H Hermsen and Herman G. P. Swarts and Lianne Wassink and Francina J Dijk and Maarten T M Raijmakers and Corn{\'e} H. W. Klaassen and Jan B. Koenderink and Michiyuki Maeda and Jan Joep H. H. M. De Pont},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1480 1-2},
  pages={182-90}
}
It is generally assumed that negatively charged residues present in the alpha-subunit of gastric H(+),K(+)-ATPase are involved in K(+) binding and transport. Despite the fact that there is no difference between various species regarding these negatively charged residues, it was observed that the apparent K(+) affinity of the pig enzyme was much lower than that of the rat H(+),K(+)-ATPase. By determining the K(+)-stimulated dephosphorylation reaction of the phosphorylated intermediate K(0.5… CONTINUE READING