Na+, K+-Dependent adenosine triphosphate phosphohydrolase Two types of kinetics

This publication has 17 references indexed in Scilit:

• The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain III. A minimal model
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1981
• The (Na+ + K+)-activated ATPase Enzymatic and transport properties
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1979
• (Na+ + K+)-ATPase: effects of detergents on the cross-linking of subunits in the presence of Cu2+ and o-phenanthroline
  Biochimica et Biophysica Acta (BBA) - Protein Structure, 1979
• A simple method for calculating Km and V from a single enzyme reaction progress curve
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1977
• EFFECT OF ATP ON Na: K AFFINITY AND CATALYTIC ACTIVITY OF (Na⁺+ K⁺)-ACTIVATED ENZYME SYSTEM
  Annals of the New York Academy of Sciences, 1974
• A Second Ouabain-sensitive Sodium-dependent Adenosine Triphosphatase in Brain Microsomes
  Journal of Biological Chemistry, 1969
• Estimation of enzymically produced orthophosphate in the presence of cysteine and adenosine triphosphate
  Analytical Biochemistry, 1969
• Sodium Fluxes in Internally Dialyzed Squid Axons
  The Journal of general physiology, 1968
• Co-operative Effects in Enzyme Catalysis: A Possible Kinetic Model Based on Substrate-Induced Conformation Isomerization
  Biochemical Journal, 1967