Modulation of plasma membrane H+-ATPase from oat roots by lysophosphatidylcholine, free fatty acids and phospholipase A2

@article{Palmgren1988ModulationOP,
  title={Modulation of plasma membrane H+-ATPase from oat roots by lysophosphatidylcholine, free fatty acids and phospholipase A2},
  author={M. Palmgren and M. Sommarin and Peter Ulvlskov and P. L. J{\o}rgensen},
  journal={Physiologia Plantarum},
  year={1988},
  volume={74},
  pages={11-19}
}
Plasma membrane vesicles were purified from 8-day-old oat (Avena sativa L. cv. Brighton) roots in an aqueous polymer two-phase system. The plasma membranes possessed high specific ATPase activity [ca 4 μmol P1 (mg protein)−1 min−1 at 37°C]. Addition of lysophosphatidylcholine (lyso-PC) produced a 2–3 fold activation of the plasma membrane ATPase, an effect due both to exposure of latent ATP binding sites and to a true activation of the enzyme. Lipid activation increased the affinity for ATP and… Expand
Substrate stabilization of lysophosphatidylcholine‐solubilized plasma membrane H+‐ATPase from oat roots
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