Kinetics of Na+-ATPase: influence of Na+ and K+ on substrate binding and hydrolysis.
暂无分享,去创建一个
[1] I. Plesner,et al. Kinetics of (Na+ + K+)-ATPase: analysis of the influence of Na+ and K+ by steady-state kinetics. , 1985, Biochimica et biophysica acta.
[2] N. O. Christiansen,et al. Kinetics of Na-ATPase activity by the Na,K pump. Interactions of the phosphorylated intermediates with Na+, Tris+, and K+ , 1983, The Journal of general physiology.
[3] M. Esmann,et al. The effect of K+ on the equilibrium between the E2 and the K+-occluded E2 conformation of the (Na+ + K+)-ATPase. , 1983, Biochimica et biophysica acta.
[4] M. Esmann,et al. The effects of Na+ and K+ on the conformational transitions of (Na+ + K+)-ATPase. , 1983, Biochimica et biophysica acta.
[5] M. Esmann,et al. Effect of magnesium ions on the high-affinity binding of eosin to the (Na+ + K+)-ATPase. , 1983, Biochimica et biophysica acta.
[6] A. F. Rega,et al. THE INTERACTION OF K+ Na+, Mg2+, AND ATP WITH THE (Na, K)‐ATPase * , 1982, Annals of the New York Academy of Sciences.
[7] A. B. Maunsbach,et al. STRUCTURE OF THE Na, K PUMP: CRYSTALLIZATION OF PURE MEMBRANE‐BOUND Na, K‐ATPase AND IDENTIFICATION OF FUNCTIONAL DOMAINS OF THE α‐SUBUNIT , 1982, Annals of the New York Academy of Sciences.
[8] P. L. Jørgensen,et al. High-affinity 86Rb-binding and structural changes in the alpha-subunit of Na+,K+-ATPase as detected by tryptic digestion and fluorescence analysis. , 1982, Biochimica et biophysica acta.
[9] W. Schoner,et al. Evidence for a Mg2+-induced conformational change at the ATP-binding site of (Na+ + K+)-ATPase demonstrated with a photoreactive ATP-analogue. , 1981, European journal of biochemistry.
[10] I. Plesner,et al. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain IV. Rate constant determination , 1981 .
[11] M. Nakao,et al. Transient state in the phosphorylation of sodium- and potassium- transport adenosine triphosphatase by adenosine triphosphate. , 1981, Journal of Biological Chemistry.
[12] I. Plesner,et al. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. III. A minimal model. , 1981, Biochimica et biophysica acta.
[13] I. Plesner,et al. The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. I. Substrate identity. , 1981, Biochimica et biophysica acta.
[14] U. Pick,et al. Sidedness of the effects of sodium and potassium ions on the conformational state of the sodium—potassium pump , 1981, The Journal of physiology.
[15] I. Glynn,et al. Sodium ions, acting at high‐affinity extracellular sites, inhibit sodium‐ATPase activity of the sodium pump by slowing dephosphorylation. , 1979, The Journal of physiology.
[16] P. Ottolenghi,et al. Large-scale preparation of Na, K-ATPase from ox brain. , 1975, Analytical biochemistry.
[17] P. J. Garrahan,et al. The interaction of sodium and potassium with the sodium pump in red cells , 1973, The Journal of physiology.
[18] S. Kume,et al. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. , 1972, The Journal of biological chemistry.
[19] A. Kleinzeller,et al. Current Topics in Membranes and Transport , 1970 .
[20] P. R. Bevington,et al. Data Reduction and Error Analysis for the Physical Sciences , 1969 .
[21] S. Cha. A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state. , 1968, The Journal of biological chemistry.
[22] K. Nagano,et al. Ouabain-sensitive Mg++-ATPase, K+-ATPase and Na+-ATPase activities accompanying a highly specific Na+-K+-ATPase preparation. , 1967, Journal of biochemistry.
[23] K. Burton. Formation constants for the complexes of adenosine di- or tri-phosphate with magnesium or calcium ions. , 1959, The Biochemical journal.
[24] D. Glick. Methods of Biochemical Analysis , 1968 .
[25] P. Ottolenghi,et al. Binding of sodium and potassium to the sodium pump of pig kidney evaluated from nucleotide‐binding behaviour. , 1984, The Journal of physiology.
[26] A. Schwartz,et al. A kinetic description for sodium and potassium effects on (Na++K+)‐adenosine triphosphatase: a model for a two‐nonequivalent site potassium activation and an analysis of multiequivalent site models for sodium activation , 1974, The Journal of physiology.
[27] A. Shimizu,et al. Stability Constants of Mg-Complexes with ATP, Phosphoenolpyruvate, and Sulphate. , 1970 .
[28] K. Nagano,et al. Comparison of some minor activities accompanying a preparation of sodium-plus-potassium ion-stimulated adenosine triphosphatase from pig brain. , 1968, The Biochemical journal.
[29] R. Albers. Biochemical aspects of active transport. , 1967, Annual review of biochemistry.
[30] S. Colowick,et al. Methods in Enzymology , Vol , 1966 .
[31] D. D. Perrin,et al. THE STABILITY CONSTANTS OF METAL-ADENINE NUCLEOTIDE COMPLEXES. , 1964, Biochemistry.