Effects of sodium and potassium on the partial reactions of a highly purified (Na+ plus K+)-ATPase: modulation of the rate of ouabain interaction

Ann N Y Acad Sci. 1974;242(0):235-45. doi: 10.1111/j.1749-6632.1974.tb19093.x.
No abstract available

Publication types

  • Comparative Study

MeSH terms

  • Adenosine Triphosphatases / isolation & purification
  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Binding Sites
  • Carbon Radioisotopes
  • Cholic Acids
  • Deoxycholic Acid
  • Dogs
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Activation / drug effects
  • Glycerol
  • Kidney / enzymology*
  • Kidney Medulla / enzymology*
  • Kinetics
  • Mathematics
  • Microsomes / enzymology
  • Ouabain / pharmacology*
  • Potassium / pharmacology*
  • Protein Binding
  • Protein Conformation
  • Sodium / pharmacology*
  • Tritium

Substances

  • Carbon Radioisotopes
  • Cholic Acids
  • Deoxycholic Acid
  • Tritium
  • Ouabain
  • Sodium
  • Adenosine Triphosphatases
  • Glycerol
  • Potassium