Effects of pH on the interaction of ligands with the (H+ + K+)-ATPase purified from pig gastric mucosa.

@article{Ljungstrm1984EffectsOP,
  title={Effects of pH on the interaction of ligands with the (H+ + K+)-ATPase purified from pig gastric mucosa.},
  author={Marianne Ljungstr{\"o}m and Felix V. Vega and Sven M{\aa}rdh},
  journal={Biochimica et biophysica acta},
  year={1984},
  volume={769 1},
  pages={220-30}
}
The effects of K+, Na+ and ATP on the gastric (H+ + K+)-ATPase were investigated at various pH. The enzyme was phosphorylated by ATP with a pseudo-first-order rate constant of 3650 min-1 at pH 7.4. This rate constant increased to a maximal value of about 7900 min-1 when pH was decreased to 6.0. Alkalinization decreased the rate constant. At pH 8.0 it was 1290 min-1. Additions of 5 mM K+ or Na+, did not change the rate constant at acidic pH, while at neutral or alkaline pH a decrease was… CONTINUE READING