Inhibition of (Na+ + K+)-ATPase by ouabain: involvement of calcium and membrane proteins.
Biochim Biophys Acta, 1979/11/02;557(2):399-408.
Lelievre L, Zachowski A, Charlemagne D, Laget P, Paraf A
PMID: 227455
Abstract
Treatment of plasma membrane isolated from murine plasmocytoma MOPC 173 with an EDTA-containing buffer resulted in a 300-fold increase in sensitivity of (Na+ + K+)-stimulated Mg2+-ATPase to ouabain. This phenomenon was associated with the solubilization by EDTA of phospholipid free proteins (approx. 30 000-34 000 daltons) from the cytoplasmic face of the plasma membrane and with removal of about 90% of the membrane bound Ca2+. The recovery of the original resistance to ouabain required specifically Ca2+ and was associated with a binding of the solubilized proteins to the membrane.
MeSH terms
Animals; Calcium; Cell Line; Cell Membrane; Edetic Acid; Magnesium; Membrane Proteins; Mice; Molecular Weight; Ouabain; Plasmacytoma; Sodium-Potassium-Exchanging ATPase
More resources
EndNote: Download