Reconstitution of (Na+ + K+)-ATPase proteoliposomes having the same turnover rate as the membranous enzyme

This publication has 26 references indexed in Scilit:

• Soluble and enzymatically stable (Na++K+)-ATPase from mammalian kidney consisting predominantly of protomer αβ-units
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1983
• Exclusive labeling of the extracytoplasmic surface of sodium and potassium ion activated adenosine triphosphatase and a determination of the distribution of surface area across the bilayer
  Biochemistry, 1982
• Mechanism of the Na+, K+ pump protein structure and conformations of the pure
  Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1982
• Sidedness of the effects of sodium and potassium ions on the conformational state of the sodium—potassium pump
  The Journal of Physiology, 1981
• A new simple preparation method for NaK-ATPase-rich membrane fragments
  Analytical Biochemistry, 1981
• Ultrastructure of Na,K-transport vesicles reconstituted with purified renal Na,K-ATPase.
  The Journal of cell biology, 1980
• A Simple, Versatile, Sensitive and Volume-Independent Method for Quantitative Protein Determination which is Independent of Other External Influences
  Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
• A reconstituted Na++K+ pump in liposomes containing purified (Na++K+-ATPase from kidney medulla
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1977
• Reconstituction of an ATP-dependent sodium pump with an ATPase from electric eel and pure phospholipids
  Biochemical and Biophysical Research Communications, 1975
• The connexion between active cation transport and metabolism in erythrocytes
  Biochemical Journal, 1965