Purification of the proton pumping ATPase from plant plasma membranes

Biochem Biophys Res Commun. 1984 Jun 15;121(2):735-40. doi: 10.1016/0006-291x(84)90243-2.


The plasma membrane ATPase from oat roots has been purified near homogeneity by a simple procedure. Plasma membranes isolated from sucrose gradients are first extracted with Triton X-100 and KC1 and the residue solubilized with lysolecithin. Rate-zonal centrifugation in a vertical rotor with a glycerol gradient results in a preparation of very high specific activity (6 mumoles min-1 mg protein-1 at 30 degrees C) and where over 70% of the protein corresponds to a polypeptide of about 100 kilodaltons previously identified as the ATPase. The purified enzyme could be reconstituted in proteoliposomes catalyzing ATP-driven proton transport sensitive to vanadate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Cell Membrane / enzymology
  • Centrifugation, Density Gradient
  • Edible Grain / enzymology*
  • Proton-Translocating ATPases / isolation & purification*
  • Proton-Translocating ATPases / metabolism


  • Proton-Translocating ATPases