Abstract
The Na+,K+-transporting adenosine triphosphatase (Na+,K+-ATPase), also often known as the sodium pump or sodium-potassium pump, is an enzyme, found in nearly all animal-cell membranes, that uses energy from the hydrolysis of intracellular ATP to transport Na+ ions outwards and K+ ions inwards. It may be thought of as having three substrates (ATP, intracellular Na+ ions, and extracellular K+ ions) and four products (ADP, orthophosphate, extracellular Na+ ions, and intracellular K+ ions.) Because more Na+ ions are pumped out than K+ ions are pumped in, the activity of the enzyme generates an outward movement of positive charge, and this outward current may also be considered a “product” of the reaction.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abercrombie, R. F., and De Weer, P., 1978, Electric current generated by squid giant axon sodium pump: External K and internal ADP effects. Am. J. Physiol. 235 (1): C63 - C68.
Akera, T., 1981, Effects of cardiac glycosides on Na+,K+-ATPase, in: Handbook of Experimental Pharmacology, Vol. 56/I ( K. Greeff, ed.), Springer-Verlag, Berlin, pp. 287–336.
Akera, T., and Brody, T. M., 1971, Membrane adenosine triphosphatase: The effect of potassium on the formation and dissociation of the ouabain-enzyme complex, J. Pharmacol. Exp. Ther. 176: 545–557.
Albers, R. W., Fahn, S., and Koval, G. J., 1963, The role of sodium ions in the activation of Electrophorus electric organ adenosine triphosphatase, Proc. Natl. Acad. Sci. USA 50: 474–481.
Albers, R. W., Koval, G. J., and Siegel, G. J., 1968, Studies on the interaction of ouabain and other cardio-active steroids with sodium-potassium-activated adenosine triphosphatase, Mol. Pharmacol. 4: 324–336.
Anner, B. M., Lane, L. K., Schwartz, A., and Pitts, B. J. R., 1977, A reconstituted Na+ + K’ pump in liposomes containing purified (Na- + K’)-ATPase from kidney medulla, Biochim. Biophys. Acta 467: 340–345.
Askari, A., and Huang, W-H., 1980, Na’,K -ATPase: Half of the subunits cross-linking reactivity suggests an oligomeric structure containing a minimum of four catalytic subunits, Biochem. Biophys. Res. Commun. 93: 448–453.
Askari, A., and Huang, W-H., 1981, Nat,K’-ATPase: (Ca’ + ouabain)-dependent phosphorylation by P„ FEBS Lett. 126: 215–218.
Askari, A., and Huang, W-H., 1983, Na,K“-ATPase: relation of quaternary conformational transitions to function, Current Topics in Membranes and Transport 19 (in press).
Askari, A., and Koyal, D., 1971, Studies on the partial reactions catalyzed by the (Na’ + K’)-activated ATPase. I1. Effects of oligomycin and other inhibitors of the ATPase on the p-nitrophenylphosphatase, Biochim. Biophys. Acta 225: 20–25.
Askari, A., Huang, W., and Henderson, G. R., 1979, Na,K-ATPase: Functional and structural modifications induced by mercurials, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. Nrby, eds.), Academic Press, London, pp. 205–215.
Askari, A., Huang, W-H., and Antieau, J. M., 1980, Na’,K’-ATPase: Ligand-induced conformational transitions and alterations in subunit interactions evidenced by cross-linking studies, Biochemistry 19: 1132–1140.
Askari, A., Huang, W-H., and McCormick, P. W., 1983, (Na+ K+)-dependent adenosine triphosphatase: Regulation of inorganic phosphate, magnesium ion and calcium ion interactions with the enzyme by ouabain, J. Biol. Chem., 258:3453–3460.
Bader, H., and Sen, A. K., 1966, (K+)-dependent acyl phosphatase as part of the (Na’ + K’)-dependent ATPase of cell membranes, Biochim. Biophys. Act 118:116–123.
Baker, E., and Simmonds, W. J., 1966, Membrane ATPase and electrolyte levels in marsupial erythrocytes, Biochim. Biophys. Acta 126: 492–499.
Baker, P. F., and Stone, A. J., 1966, A kinetic method for investigating hypothetical models of the sodium pump, Biochim. Biophys. Acta 126: 321–329.
Baker, P. F., and Willis, J. S., 1970, Potassium ions and the binding of cardiac glycosides to mammalian cells, Nature 226: 521–523.
Baker, P. F., Blaustein, M. P., Hodgkin, A. L., and Steinhardt, R. A., 1969a, The influence of calcium on sodium efflux in squid axons, J. Physiol. 200: 431–468.
Baker, P. F., Blaustein, M. P., Keynes, R. D., Manil, J., Shaw, T. I., and Steinhardt, R. A., 1969b, The ouabain-sensitive fluxes of sodium and potassium in squid giant axons, J. Physiol. 200: 459–496.
Banerjee, S. P., and Wong, S. M. E., 1972, Effect of potassium on sodium-dependent adenosine diphosphate—adenosine triphosphate exchange activity in kidney microsomes, J. Biol. Chem. 247: 5409–5413.
Banerjee, S. P., Wong, S. M. E., Khanna, V. K., and Sen, A. K., 1972a, Inhibition of sodium-and potassium-dependent adenosine triphosphatase by N-ethylmaleimide. I. Effects on sodium-sensitive phosphorylation and potassium-sensitive dephosphorylation, Mol. Pharmacol. 8: 8–17.
Banerjee, S. P., Wong, S. M. E., and Sen, A. K., 1972b, Inhibition of sodium-and potassium-dependent adenosine triphosphatase by N-ethylmaleimide. II. Effects on sodium-activated transphosphorylation, Mol. Pharmacol. 8: 18–29.
Barnett, R. E., 1970, Effect of monovalent cations on the ouabain inhibition of the sodium and potassium ion activated adenosine triphosphatase, Biochemistry 9: 4644–4648.
Bastide, F., Meissner, G., Fleischer, S., and Post, R. L., 1973, Similarity of the active site of phosphorylation of the adenosine triphosphatase for transport of sodium and potassium ions in kidney to that for transport of calcium ions in the sarcoplasmic reticulum of muscle, J. Biol. Chem. 248: 8385–8391.
Bayley, H., and Knowles, J. R., 1980, Photogenerated reagents for membranes: Selective labeling of intrinsic membrane proteins in the human erythrocyte membrane, Biochemistry 19: 3883–3892.
Beaugé, L. A., 1979, Vanadate-potassium interactions in the inhibition of Na,K-ATPase, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. Nurby, eds.), Academic Press, London, pp. 373–387.
Beaugé, L. A., and Berberian, G., 1983, The effects of several ligands on the potassium—vanadate interaction in the inhibition of the Na,K-ATPase and the Na-K pump, Biochim. Biophys. Acta, 727: 336–350.
Beaugé, L. A., and DiPolo, R., 1979a, Vanadate selectively inhibits the K+0-activated Na’ efflux in squid axons, Biochim. Biophys. Acta 551: 220–223.
Beaugé, L. A., and DiPolo, R., 1979b, Sidedness of the ATP-Na’-K“ interactions with the Na pump in squid axons, Biochim. Biophys. Acta 553: 495–500.
Beaugé, L. A., and DiPolo, R., 1981, The effects of ATP on the interactions between monovalent cations and the sodium pump in dialysed squid axons, J. Physiol. 314: 457–480.
Beaugé, L. A., and DiPolo, R., 1983. Sidedness of cations and ATP interactions with the sodium pump. Curr. Top. Membr. Trans. 19: 643–647.
Beaugé, L. A., and Glynn, I. M., 1978, Commercial ATP containing traces of vanadate alters the response of (Na“ + K’)-ATPase to external potassium, Nature 272: 551–552.
Beaugé, L. A., and Glynn, I. M., 1979a, Occlusion of K ions in the unphosphorylated sodium pump, Nature 280: 510–512.
Beaugé, L. A., and Glynn, I. M., 1979b, Sodium ions, acting at high-affinity extracellular sites, inhibit sodium ATPase activity of the sodium pump by slowing dephosphorylation, J. Physiol. 289: 17–31.
Beaugé, L. A., and Glynn, I. M., 1980, The equilibrium between different conformations of the unphosphorylated sodium pump: Effects of ATP and of potassium ions, and their relevance to potassium transport, J. Physiol. 299: 367–383.
Beaugé, L. A., and Ortiz, O., 1973, Na fluxes in rat red blood cells in K-free solutions, J. Membr. Biol. 13: 165–184.
Beaugé, L. A., Cavieres, J. D., Glynn, I. M., and Grantham, J. J., 1980, The effects of vanadate on the fluxes of sodium and potassium ions through the sodium pump, J. Physiol. 301: 7–23.
Beeuwkes, R., and Rosen, S., 1975, Renal Na,K-ATPase. Optical localization and X-ray microanalysis, J. Histochem. Cytochem. 23: 828–839.
Blostein, R., 1968, Relationships between erythrocyte membrane phosphorylation and adenosine triphosphate hydrolysis, J. Biol. Chem. 243; 1957–1965.
Blostein, R., 1970, Sodium activated adenosine triphosphatase activity of the erythrocyte membrane, J. Biol. Chem. 245: 270–275.
Blostein, R., 1975, Na* ATPase of the mammalian erythrocyte membrane. Reversibility of phosphorylation at O°, J. Biol. Chem. 250: 6118–6124.
Blostein, R., 1979, Side-specific effects of sodium on (Na,K)-ATPase, J. Biol. Chem. 254: 6673–6677.
Blostein, R., 1983, Sidedness of sodium interactions with the sodium pump in the absence of K’, Curr. Top. Membr. Trans. 19: 649–652.
Blostein, R., and Chu, L., 1977, Sidedness of (sodium, potassium)-adenosine triphosphatase of inside-out red cell membrane vesicles. Interactions with potassium, J. Biol. Chem. 252: 3035–3043.
Blostein, R., and Whittington, E. S., 1973, Studies of high potassium and low potassium sheep erythrocyte membrane sodium-adenosine triphosphatase: Interactions with oligomycin, adenosine triphosphate, sodium, and potassium, J. Biol. Chem. 248: 1772–1777.
Blostein, R., Pershadsingh, H. A., Drapeau, P., and Chu, L., 1979, Side-specificity of alkali cation interactions with Na,K-ATPase: Studies with inside-out red cell membrane vesicles, in: Na,K-ATPase: Structure and Kinetics ( J. C. Skou and J. G. Nsrby, eds.), London, Academic Press, pp. 233–245.
Bodemann, H. H., and Hoffman, J. F., 1976a, Side-dependent effects of internal versus external Na and K on ouabain binding to reconstituted human red blood cell ghosts, J . Gen. Physiol. 67: 497–525.
Bodemann, H. H., and Hoffman, J. F., 1976b, Comparison of the side-dependent effects of Na and K on orthophosphate-, UTP- and ATP-promoted ouabain binding to reconstituted human red blood cell ghosts, J. Gen. Physiol. 67: 527–545.
Bond, G. H., and Hudgins, P. M., 1981, Dog kidney (Na+,K+)-ATPase is more sensitive to inhibition by vanadate than human red cell (Na+,K +)-ATPase, Biochim. Biophys. Acta 646: 479–482.
Bond, G. H., Bader, H., and Post, R. L., 1971, Acetyl phosphate as a substitute for ATP in (Na’ + K+)-dependent ATPase, Biochim. Biophys. Acta 241: 57–67.
Bonting, S. L., and Caravaggio, L. L., 1963, Studies on Na: K activated ATPase. V. Correlation of enzyme activity with cation flux in six tissues, Arch. Biochem. Biophys. 101: 37–46.
Bonting, S. L., Simon, K. A., and Hawkins, N. M., 1961, Studies on sodium-potassium-activated adenosine triphosphatase. I. Quantitative distribution in several tissues of the cat, Arch. Biochem. Biophys. 95: 416–423.
Bonting, S. L., Schuurmans Stekhoven, F. M. A. H., Swarts, H. G. P., and de Pont, J. J. H. H. M., 1979, The low-energy phosphorylated intermediate of Na,K-ATPase, in: Na +,K + -ATPase: Structure and Kinetics ( J. C. Skou and J. G. Nsrby, eds.), Academic Press, London, pp. 317–330.
Brinley, F. J., and Mullins, L. J., 1968, Sodium fluxes in internally dialyzed squid axons, J. Gen. Physiol. 52: 181–211.
Brotherus, J. R., Griffith, O. H., Brotherus, M. O., Jost, P. C., and Silvius, J. R., 1981a, Lipid—protein multiple binding equilibria in membranes, Biochemistry 20: 5261–5267.
Brotherus, J. R., Moller, J. V., and Jorgensen, P. L., 1981b, Soluble and active renal Na,K-ATPase with maximum protein molecular mass 170,000 ± 9000 Daltons; formation of larger units by secondary aggregation, Biochem. Biophys. Res. Commun. 100: 146–154.
Brunner, J., Senn, H., and Richards, F. M., 1980, 3-Trifluoromethyl-3-phenyldiazirine. A new carbene generating group for photolabeling reagents, J. Biol. Chem. 255:3313–3318.
Caldwell, P. C., and Keynes, R. D., 1957, The utilization of phosphate bond energy for sodium extrusion from giant axons, J. Physiol. 137: 12 P.
Caldwell, P. C., and Keynes, R. D., 1959, The effect of ouabain on the efflux of sodium from a squid axon, J. Physiol. 148: 8–9 P.
Caldwell, P. C., Hodgkin, A. L., Keynes, R. D., and Shaw, T. I., 1960, The effects of injecting “energy-rich” phosphate compounds on the active transport of ions in the giant axons of Loligo, J. Physiol. 152: 561–590.
Cantley, L. C., 1981, Structure and mechanism of the (Nat,K+)-ATPase, Curr. Top. Bioenerg. 11: 201–237.
Cantley, L. C., and Aisen, P., 1979, The fate of cytoplasmic vanadium. Implications on (Na,K)-ATPase inhibition, J. Biol. Chem. 254: 1781–1784.
Cantley, L. C., Josephson, L., Warner, R., Yanagisawa, M., Lechene, C., and Guidotti, G., 1977, Vanadate is a potent (Na,K)-ATPase inhibitor found in ATP derived from muscle, J. Biol. Chem. 252: 7421–7423.
Cantley, L. C., Cantley, L. G., and Josephson, L., 1978a, A characterization of vanadate interactions with the (Na,K)-ATPase. Mechanistic and regulatory implications, J. Biol. Chem. 253: 7361–7368.
Cantley, L. C., Gelles, J., and Josephson, L., 1978b, Reaction of (Na-K)-ATPase with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole: Evidence for an essential tyrosine at the active site, Biochemistry 17: 418–425.
Cantley, L. C., Resh, M., and Guidotti, G., 1978c, Vanadate inhibits the red cell (Na+,K+)ATPase from the cytoplasmic side, Nature 272: 552–554.
Carilli, C. T., Farley, R. A., Perlman, D. M., and Cantley, L. C., 1982, The active site structure of Nat -and K+-stimulated ATPase. Location of a specific fluorescein isothiocyanate reactive site, J. Biol. Chem. 257: 5601–5606.
Castro, J., and Farley, R. A., 1979, Proteolytic fragmentation of the catalytic subunit of the sodium and potassium adenosine triphosphatase. Alignment of tryptic and chymotryptic fragments and location of sites labelled with ATP and iodoacetate, J. Biol. Chem. 254: 2221–2228.
Cavieres, J. D., 1980, Extracellular sodium stimulates ATP—ADP exchange by the sodium pump, J. Physiol. 308: 57 P.
Cavieres, J. D., 1983, Ouabain-sensitive ATP—ADP exchange and Na-ATPase of resealed red cell ghosts, Curr. Top. Membr. Trans., 19: 677–681.
Cavieres, J. D., and Ellory, J. C., 1975, Allosteric inhibition of the sodium pump by external sodium, Nature 255: 338–340.
Cavieres, J. D., and Ellory, J. C., 1982, The target size for ATP—ADP exchange and Na-ATPase activities of a purified Na,K-ATPase preparation, J. Physiol. 332: 120 P.
Cavieres, J. D., and Glynn, I. M., 1979, Sodium—sodium exchange through the sodium pump: The roles of ATP and ADP, J. Physiol. 297: 637–645.
Chipperfield, A. R., 1983, Stimulation and inhibition by plasma of ouabain-sensitive sodium efflux in human red blood cells Curr. Top. Membr. Trans. 19: 1013–1016.
Chipperfield, A. R., and Whittam, R., 1976, The connexion between the ion-binding sites of the sodium pump, J. Physiol. 260: 371–385.
Churchill, L., Peterson, G. L., and Hokin, L. E., 1979, The large subunit of (sodium + potassium)-activated adenosine triphosphatase from the electroplax of Electrophorus electricus is a glycoprotein, Biochem. Biophys. Res. Commun. 90: 488–490.
Clarkson, E. M., and Maizels, M., 1952, Distribution of phosphatases in human erythrocytes, J. Physiol. 116: 112–128.
Cleland, W. W., 1970, Steady-state kinetics, in: The Enzymes, Vol. 2 ( P. D. Boyer, ed.), Academic Press, New York, pp. 1–65.
Cohn, W. E., and Cohn, E. T., 1939, Permeability of red corpuscles of the dog to sodium ion, Proc. Soc. Exp. Biol. Med. 41: 445–449.
Collins, J. H., Forbush, B., Lane, L. K., Ling, E., Schwarz, A., and Zot, A., 1982, Purification and characterization of an (Na’ + K)-ATPase proteolipid labeled with a photoaffinity derivative of ouabain, Biochim. Biophys. Acta 686: 7–12.
Craig, W. S., and Kyte, J., 1980, Stoichiometry and molecular weight of the minimum asymmetric unit of canine renal sodium and potassium ion-activated adenosine triphosphatase, J. Biol. Chem. 255: 6262–6269.
Czerwinski, A., Gitelman, H. J., and Welt, L. G., 1967, A new member of the ATPase family, Am. J. Physiol. 213: 786–792.
Dahl, J. L., and Hokin, L. E., 1974, The sodium-potassium adenosinetriphosphatase, Annu. Rev. Biochem. 43: 327–356.
Dahms, A. S., and Boyer, P. D., 1973, Occurrence and characteristics of 180 exchange reactions catalyzed by sodium-and potassium-dependent adenosine triphosphatases, J. Biol. Chem. 248: 3155–3162.
Dahms, A. S., and Miara, J. E., 1983, 31P(18O)-NMR kinetic analysis of the oxygen-18 exchange reaction between inorganic phosphate and water catalyzed by the (Na’,K“)-ATPase, Curr. Top. Membr. Trans. 19:371–375.
Dahms, A. S., Kanazawa, T., and Boyer, P. D., 1973, Source of the oxygen in the C-O-P linkage of the acyl phosphate in transport adenosine triphosphatases, J. Biol. Chem. 248: 6592–6595.
Danowski, T. S., 1941, The transfer of potassium across the human blood cell membrane, J. Biol. Chem. 139: 693–705.
Dean, R. B., 1941, Theories of electrolyte equilibrium in muscle, Biol. Symp. 3: 331–348.
Degani, C., Dahms, A. S., and Boyer, P. D., 1974, Characterization of acyl phosphate in transport ATPases by a borohydride reduction method, Ann. N. Y. Acad. Sci. 242: 77–79.
Deguchi, N., Jargensen, P. L., and Maunsbach, A. B., 1977, Ultrastructure of the sodium parison of thin sectioning, negative staining and freeze-fracture of purified, membrane-bound (Na’,K+)- ATPase, J. Cell Biol. 75: 619–634.
De Pont, J. J. H. H. M., Schoot, B. M., Van Prooijen-Van-Eeden, A., and Bonting, S. L., 1977, An essential arginine residue in the ATP-binding centre of (Na’ + K’)-ATPase, Biochim. Biophys. Acta 482: 213–227.
De Weer, P., 1970, Effects of intracellular 5’ADP and orthophosphate on the sensitivity of sodium efflux from squid axon to external sodium and potassium, J. Gen. Physiol. 56: 583–620.
De Weer, P., Kennedy, B. G., and Abercrombie, R. F., 1979, Relationship between the Na: K exchanging and Na: Na exchanging modes of operation of the sodium pump, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. N$rby, eds.), Academic Press, London, pp. 503–515.
De Weer, P., Breitwieser, G. E., Kennedy, B. G., and Smith, H. G., 1983, ADP—ATP exchange in internally dialysed squid giant axons, Curr. Top. Membr. Trans. 19: 665–669.
Dissing, S., and Hoffman, J. F., 1983, Anion-coupled Na efflux mediated by the Na: K pump in human red blood cells, Curr. Top. Membr. Trans. 19: 693–695.
Dixon, J. F., and Hokin, L. E., 1974, Studies in the characterization of the sodium—potassium adenosine triphosphatase. Purification and properties of the enzyme from the electric organ of Electrophorus electricus, Arch. Biochem. 163: 749–758.
Dixon, J. F., and Hokin, L. E., 1978, A simple procedure for the preparation of highly purified (sodium + potassium) adenosine triphosphatase from the rectal salt gland of Squalus acanthias and the electric organ of Electrophorus electricus, Anal. Biochem. 86: 378–385.
Drapeau, P., and Blostein, R., 1980, Interactions of K+ with (Na,K)-ATPase: Orientation of K+-phosphatase sites studied with inside-out red cell membrane vesicles, J. Biol. Chem. 255: 7827–7834.
Dudding, W. F., and Winter, C. G., 1971, On the reaction sequence of the K’-dependent acetyl phosphatase activity of the Na+ pump, Biochim. Biophys. Acta 241: 650–660.
Dunham, E. T., and Glynn, I. M., 1961, Adenosine triphosphatase activity and the active movements of alkali metal ions, J. Physiol. 156: 274–293.
Eisner, D. A., and Richards, D. E., 1981, The interaction of potassium ions and ATP on the sodium pump of resealed red cell ghosts, J. Physiol. 319: 403–418.
Eisner, D. A., and Richards, D. E., 1982, Inhibition of the sodium pump by inorganic phosphate in resealed red cell ghosts, J. Physiol. 326: 1–10.
Eisner, D. A., and Richards, D. E., 1983, Stimulation and inhibition by ATP and orthophosphate of the potassium—potassium exchange in resealed red cell ghosts, J. Physiol. 335: 495–506.
Ellory, J. C., Green, J. R., Jarvis, S. M., and Young, J. D., 1979, Measurement of the apparent molecular volume of membrane-bound transport systems by radiation inactivation, J. Physiol. 295: 10–11 P.
Erdmann, E., and Schoner, W., 1973, Ouabain-receptor interactions in (Na+ + K*)-ATPase preparations from different tissues and species. Determination of kinetic constants and dissociation constants, Biochim. Biophys. Acta 307: 386–398.
Erdmann, E., and Schoner, W., 1974, Ouabain-receptor interactions in (Na+ + K*)-ATPase preparations. IV. The molecular structure of different cardioactive steroids and other substances and their affinity to the glycoside receptor, Naunyn-Schmiedebergs Arch. Pharmacol. 283: 335–356.
Esmann, M., 1980, Concanavalin A-Sepharose purification of soluble Na,K-ATPase from rectal glands of the spiny dogfish, Anal. Biochem. 108: 83–85.
Esmann, M., and Klodos, I., 1983, Sulphydryl groups of Na,K-ATPase: Effects of N-ethyl-maleimide on phosphorylation from ATP in the presence of Na+ + Mgt+, Curr. Top. Membr. Trans. 19: 349–352.
Esmann, M., Skou, J. C., and Christiansen, C., 1979, Solubilization and molecular weight determination of Na,K-ATPase from rectal glands of Squalus Acanthias, Biochim. Biophys. Acta 567: 410–420.
Esmann, M., Christiansen, C., Karlsson, K-A., Hansson, G. C., and Skou, J. C., 1980, Hydrodynamic properties of solubilized (Na+ + K+)-ATPase from rectal glands of Squalus acanthias, Biochim. Biophys. Acta 603: 1–12.
Fahn, S., Hurley, M. R., Koval, G. J., and Albers, R. W., 1966a, Sodium—potassium-activated adenosine triphosphatase of Electrophorus electric organ. II. Effects of N-ethylmaleimide and other sulfhydryl reagents, J. Biol. Chem. 241: 1890–1895.
Fahn, S., Koval, G. J., and Albers, R. W., 1966b, Sodium—potassium-activated adenosine triphosphatase of Electrophorus electric organ. I. An associated sodium-activated transphosphorylation, J. Biol. Chem. 241: 1882–1889.
Fahn, S., Koval, G. J., and Albers, R. W., 1966b, Sodium-potassium-activated adenosine triphosphatase of Electrophorus electric organ. I. An associated sodium-activated transphosphorylation, J. Biol. Chem. 241:1882–1889.
Fenn, W. O., and Cobb, D. M., 1936, Electrolyte changes in muscle during activity, Am. J. Physiol. 115: 345–356.
Fishman, M. C., 1979, Endogenous digitalis-like activity in mammalian brain, Proc. Natl. Acad. Sci. USA 76: 4661–4663.
Flatman, P. W., and Lew, V. L., 1981, The magnesium dependence of sodium-pump-mediated sodium-potassium and sodium-sodium exchange in intact human red cells, J. Physiol. 315: 421–446.
Forbush, B., 1982, Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla, J. Biol. Chem. 257: 12678–12684.
Forbush, B., and Hoffman, J. F., 1979, Evidence that ouabain binds to the same large polypeptide chain of dimeric Na,K-ATPase that is phosphorylated by P,, Biochemistry 18: 2308–2315.
Forbush, B., Kaplan, J. H., and Hoffman, J. F., 1978, Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na,K-ATPase, Biochemistry 17: 3667–3676.
Forgac, M., and Chin, G., 1981, K -independent active transport of Na-by the (Na’ + K)-stimulated adenosine triphosphatase, J. Biol. Chem. 256: 3645–3646.
Fortes, P. A. G., Moczydlowski, E. G., Yagi, A., and Lee, J. A., 1981, Na, K-ATPase structure and mechanism studied with site-directed fluorescent probes, Proc. Vllthlnternational Biophysics Congress, p. 66. IUPAB.
Foster, D., and Ahmed, K., 1976, Na’-dependent phosphorylation of rat brain (Na’ + K+)-ATPase. Possible non-equivalent activation sites for Na-, Biochim. Biophys. Acta 429: 258–273.
Freytag, J. W., and Reynolds, J. A., 1981, Polypeptide molecular weights of the (Na’,K’)-ATPase from porcine kidney medulla, Biochemistry 20: 7211–7214.
Froehlich, J. P., Albers, R. W., Koval, G. J., Goebel, R., and Berman, M., 1976, Evidence for a new intermediate state in the mechanism of (Na’ + K+)-adenosine triphosphatase, J. Biol. Chem. 251: 2186–2188.
Froehlich, J. P., Hobbs, A. S., and Albers, R. W., 1983, Evidence for parallel pathways of phosphoenzyme formation in the mechanism of ATP hydrolysis by Electrophorus (Na,K)-ATPase, Curr. Top. Membr. Trans. 19: 513–535.
Fujita, M., Ohta, H., Kawai, K., Matsui, H., and Nakao, M., 1972, Differential isolation of microvillous and basolateral plasma membranes from intestinal mucosa: Mutually exclusive distribution of digestive enzymes and ouabain-sensitive ATPase, Biochim. Biophys. Acta 274: 336–347.
Fukushima, Y., and Nakao, M., 1980, Changes in affinity of Nat-and K+-transport ATPase for divalent cations during its reaction sequence, J. Biol. Chem. 255: 7813–7819.
Fukushima, Y., and Nakao, M., 1981, Transient state in the phosphorylation of sodium-and potassium-transport adenosine triphosphatase by adenosine triphosphate, J. Biol. Chem. 256: 9136–9143.
Fukushima, Y., and Post, R. L., 1978, Binding of divalent cation to phosphoenzyme of sodium-and potassium-transport adenosine triphosphatase, J. Biol. Chem. 253: 6853–6862.
Fukushima, Y., and Tonomura, Y., 1973, Two kinds of high energy phosphorylated intermediate, with and without bound ADP, in the reaction of Na’-K’-dependent ATPase, J. Biochem. (Tokyo) 74: 135–142.
Fukushima, Y., and Tonomura, Y., 1975, The pre-steady state of Na’-K’-dependent ATPase after addition of Na’ ions. Transition of the phosphorylated intermediate from an ADP-sensitive to an ADP-insensitive form, J. Biochem. Tokyo 78: 749–755.
Gache, C., Rossi, B., and Lazdunski, M., 1976, (Na,K)-activated adenosine triphosphatase of axonal membranes, cooperativity and control. Steady-state analysis, Eur. J. Biochem. 65:293–306.
Garay, R. P., and Garrahan, P. J., 1973, The interaction of sodium and potassium with the sodium pump in red cells, J. Physiol. 231: 297–325.
Garay, R. P., and Garrahan, P. J., 1975, The interaction of adenosine triphosphate and inorganic phosphate with the sodium pump in red cells, J. Physiol. 249: 51–67.
Gardos, G., 1954, Akkumulation der Kaliumionen durch menschliche Blutkörperchen, Acta Physiol. Hung. 6: 191–199.
Garrahan, P. J., and Garay, R. P., 1976, The distinction between simultaneous and sequential models for sodium and potassium transport, Curr. Top. Membr. Trans. 8: 29–97.
Garrahan, P. J., and Glynn, I. M., 1967a, The behavior of the sodium pump in red cells in the absence of external potassium, J. Physiol. 192: 159–174.
Garrahan, P. J., and Glynn, I. M., 1967b, The sensitivity of the sodium pump to external sodium, J. Physiol. 192: 175–188.
Garrahan, P.J., and Glynn, I. M., 1967c, Factors affecting the relative magnitudes of the sodium: potassium and sodium: sodium exchanges catalysed by the sodium pump, J. Physiol. 192: 189–216.
Garrahan, P. J., and Glynn, I. M., 1967d, The stoichiometry of the sodium pump, J. Physiol. 192: 217–235.
Garrahan, P. J., and Glynn, I. M., 1967e, The incorporation of inorganic phosphate into adenosine triphosphate by reversal of the sodium pump, J. Physiol. 192: 237–257.
Garrahan, P. J., and Rega, A. F., 1972, Potassium activated phosphatase from human red blood cells. The effects of p-nitrophenylphosphate on cation fluxes, J. Physiol. 233: 595–617.
Garrahan, P. J., Pouchan, M. I., and Rega, A. F., 1970, Potassium activated phosphatase from human red blood cells. The effects of adenosine triphosphate, J. Membr. Biol. 3: 26–42.
Garrahan, P. J., Horenstein, A. H., and Rega, A. F., 1979, The interaction of ligands with the Na,KATPase during Na-ATPase activity, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. Nrby, eds.), Academic Press, London, pp. 261–274.
Garrahan, P. J., Rossi, R. C., and Rega, A. F., 1982, The interaction of IC-,Na’, Mg’, and ATP with the (Na,K)ATPase, Ann. N. Y. Acad. Sci., 402: 239–251.
Giotta, G. J., 1975, Native (Na’ + K)-dependent adenosine triphosphatase has two trypsin-sensitive sites, J. Biol. Chem. 250: 5159–5164.
Giotta, G. J., 1976, Quaternary structure of (Na’ + K’)-dependent adenosine triphosphatase, J. Biol. Chem. 251: 1247–1252.
Gitler, C., and Bercovici, T., 1980, Use of lipophilic photoactivatable reagents to identify the lipid-embedded domain of membrane proteins, Ann. N. Y. Acad. Sci. 346: 199–211.
Glynn, I. M., 1956, Sodium and potassium movements in human red cells, J. Physiol. 134: 278–310.
Glynn, I. M., 1957, The action of cardiac glycosides on sodium and potassium movements in human red cells, J. Physiol. 136: 148–173.
Glynn, I. M., 1962, Activation of adenosinetriphosphatase activity in a cell membrane by external potassium and internal sodium, J. Physiol. 160: 18–19 P.
Glynn, I. M., 1963, “Transport adenosinetriphosphatase” in electric organ. The relation between ion transport and oxidative phosphorylation, J. Physiol. 169:452–465.
Glynn, I. M., 1969, The effects of cardiac glycosides on metabolism and ion fluxes, in: Digitalis ( C. Fisch and B. Surawicz, eds.), Grune & Stratton, New York, pp. 30–42.
Glynn, I. M., 1982, Occluded-ion forms of the Na,K-ATPase, Ann. N. Y. Acad. Sci. 402: 287–288.
Glynn, I. M., 1984, The electrogenic sodium pump, in: Electrogenic Transport: Fundamental Principles and Physiological Implications ( M. P. Blaustein and M. Lieberman, eds.), Raven Press, New York, pp. 33–48.
Glynn, I. M., and Hoffman, J. F., 1971, Nucleotide requirements for sodium—sodium exchange catalysed by the sodium pump in human red cells, J. Physiol. 218: 239–256.
Glynn, I. M., and Karlish, S. J. D., 1975, The sodium pump, Annu. Rev. Physiol. 37: 13–55.
Glynn, I. M., and Karlish, S. J. D., 1976, ATP hydrolysis associated with an uncoupled sodium flux through the sodium pump: Evidence for allosteric effects of intracellular ATP and extracellular sodium, J. Physiol. 256: 465–496.
Glynn, I. M., and Karlish, S. J. D., 1982, Conformational changes associated with K’ transport by the Na’/K’-ATPase, in: Membranes and Transport, Vol. I ( A. N. Martinosi, ed.), Plenum Press, New York, pp. 529–536.
Glynn, I. M., and Lew, V. L., 1970, Synthesis of adenosine triphosphate at the expense of downhill cation movements in intact human red cells, J. Physiol. 207: 393–402.
Glynn, I. M., and Richards, D. E., 1982, Occlusion of rubidium ions by the sodium-potassium pump: Its implications for the mechanism of potassium transport, J. Physiol. 330: 17–43.
Glynn, I. M., and Richards, D. E., 1983, The existence and role of occluded-ion forms of Na,K-ATPase, Curr. Top. Membr. Trans. 19: 625–638.
Glynn, I. M., and Rink, T. J., 1982, Hypertension and inhibition of the sodium pump: A strong link but in which chain? Nature 300: 576–577.
Glynn, I. M., Lew, V. L., and Lüthi, V., 1970, Reversal of the potassium entry mechanism in red cells, with and without reversal of the entire pump cycle, J. Physiol. 207: 371–391.
Glynn, I. M., Hoffman, J. F., and Lew, V. L., 1971, Some “partial reactions” of the sodium pump, Phil. Trans. R. Soc.
Glynn, I. M., Karlish, S. J. D., Cavieres, J. D., Ellory, J. C., Lew, V. L., and Jsrgensen, P. L., 1974, The effects of an antiserum to Na-,K+-ATPase on the ion transporting and hydrolytic activities of the enzyme, Ann. N. Y. Acad. Sci. 242: 357–371.
Glynn, I. M., Karlish, S. J. D., and Yates, D. W., 1979, The use of formycin nucleotides to investigate the mechanism of Na,K-ATPase, in: Na,K-ATPase: Structure and Kinetics ( J. C. Skou and J. G. Norby, eds.), Academic Press, London, pp. 101–113.
Glynn, I. M., Hara, Y., and Richards, D. E., 1983a, Trapping of sodium ions by a phosphorylated form of the sodium-potassium pump (Na,K-ATPase), J. Physiol., 339: 56–57 P.
Glynn, I. M., Howland, J. L., and Richards, D. E., 1983b, Orthophosphate plus magnesium causes the rapid release of only 50% of rubidium ions occluded in the unphosphorylated Na, K-ATPase, J. Physiol. 343: 94 P.
Glynn, I. M., Hara, Y., and Richards, D. E., 1984, The occlusion of sodium ions within the mammalian sodium-potassium pump: its role in sodium transport. J. Physiol. 351: 531–547
Godfraind, T., and Hernandez, G. C., 1981, Properties of a digitalis-like factor extracted from guinea-pig brain, Arch. Int. Pharmacodvn. Ther. 250: 316–317.
Goldin, S. M., 1977, Active transport of sodium and potassium ions by the sodium and potassium ion-activated adenosine triphosphatase from renal medulla. Reconstitution of the purified enzyme into a well-defined in vitro transport system, J. Biol. Chem. 252: 5630–5642.
Gonzalez, E., and Zambrano, F., 1983, Possible role of sulphatide in K + -activated phosphatase activity, Biochim. Biophys. Acta 728: 66–72.
Grantham, J. J., and Glynn, I. M., 1979, Renal Na,K-ATPase: Determinants of inhibition by vanadium, Am. J. Physiol. 236 (6): F530 - F535.
Grisham, C. M., 1979, Characterization of essential arginine residues in sheep kidney (Na+ + K+)ATPase, Biochem. Biophys. Res. Commun. 88: 229–236.
Grisham, C. M., 1982, Ion-transporting ATPases. Characterizing structure and function with paramagnetic probes, in: Membranes and Transport, Vol. 1 ( A. N. Martonosi, ed.), Plenum, New York, pp. 585–592.
Grisham, C. M., and Hutton, W., 1978, Lithium-7 NMR as a probe of monovalent cation sites at the active (Na+ + K+)-ATPase from kidney, Biochem. Biophys. Res. Commun. 81: 1406–1411.
Grosse, R., Eckert, K., Malur, J., and Repke, K. R. H., 1978, Analysis of function-related interactions of ATP, sodium and potassium ions with Na+- and K+-transporting ATPase studied with a thiol reagent as tool, Acta Biol. Med. Ger. 37: 83–96.
Grosse, R., Rapoport, T., Malur, J., Fischer, J., and Repke, K. R. H., 1979, Mathematical modelling of ATP, K and Na’ interactions with (Na“ + K+)-ATPase occurring under equilibrium conditions, Biochim. Biophys. Acta 550: 500–514.
Gruber, K. A., Whitaker, J.M., and Buckalew, V. M., 1983, Immunochemical approaches to the isolation of an endogenous digoxin-like factor. Curr. Top. Membr. Trans. 19: 917–921.
Haase, W., and Koepsell, H., 1979, Substructure of membrane-bound Na’-K’-ATPase protein, Pflügers Arch. 381: 127–135.
Hall, C., and Ruoho, A., 1980, Ouabain-binding-site photoaffinity probes that label both subunits of Nat,K+-ATPase, Proc. Natl. Acad. Sci. USA 77: 4529–4533.
Hamlyn, J. M., Ringel, R., Schaeffer, J., Levinson, P. D., Hamilton, B. P., Kowarski, A. A., and Blaustein, M. P., 1982, A circulating inhibitor of (Nat + K’)ATPase associated with essential hypertension, Nature 300: 650–652.
Hansen, O., 1971, The relationship between g-strophanthin-binding capacity and ATPase activity in plasma membrane fragments from ox brain, Biochim. Biophys. Acta 233: 122–132.
Hansen, O., 1976, Nonuniform population of g-strophanthin-binding sites of (Na’ + K’)-activated ATPase. Apparent conversion to uniformity by K’, Biochim. Biophys. Acta 433: 383–392.
Hansen, O., Jensen, J., and Norby, J. G., 1971, Mutual exclusion of ATP, ADP, and g-strophanthin binding to NaK-ATPase, Nature 234: 122–124.
Hansen, O., Jensen, J., and Ottolenghi, P., 1979, Na,K-ATPase: The uncoupling of its ATPase and pnitrophenyl phosphatase activities by thimerosal, in: Na,K-ATPase: Structure and Kinetics ( J. C. Skou and J. G. Norby, eds.), Academic Press, London, pp. 217–226.
Hansson, C. G., Karlsson, K-A., and Samuelsson, B. E., 1978, The identification of sulfatides in human erythrocyte membrane and their relation to sodium-potassium dependent adenosine triphosphatase, J. Biochem. (Tokyo) 83: 813–819.
Hara, Y., and Nakao, M., 1979, Detection of sodium binding to Na’,K“-ATPase with a sodium sensitive electrode, in: Cation Flux across Biomembranes ( Y. Mukohata and L. Packer, eds.), Academic Press, New York, pp. 21–28.
Hara, Y., and Nakao, M., 1981, Sodium ion discharge from pig kidney Nat,K’-ATPase. Nat-dependency of the E1P E2P equilibrium in the absence of KC1, J. Biochem. (Tokyo) 90: 923–931.
Hara, S., Hara, Y., Nakao, T., and Nakao, M., 1981, Ligand-dependent reactivity of (Na’ + K+)-ATPase with showdomycin, Biochim. Biophys. Acta 644: 53–61.
Harris, J. E., 1941, The influence of the metabolism of human erythrocytes on their potassium content, J. Biol. Chem. 141: 579–595.
Harris, E. J., and Maizels, M., 1951, The permeability of human red cells to sodium, J. Physiol. 113: 506–524.
Hart, W. M., and Titus, E. O., 1973a, Isolation of a protein component of sodium-potassium transport adenosine triphosphatase containing ligand-protected sulfhydryl groups, J. Biol. Chem. 248: 1365–1371.
Hart, W. M., and Titus, E. O., 1973b, Sulfhydryl groups of sodium–potassium transport adenosine triphosphatase. Protection by physiological ligands and exposure by phosphorylation, J. Biol. Chem. 248: 4674–4681.
Hastings, D. F., and Reynolds, J. A., 1979a, Non-ionic detergent solubilized Na,K-ATPase from shark rectal glands-molecular weight and peptide stoichiometry of the active complex, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. N$rby, eds.), Academic Press, London, pp. 15–20.
Hastings, D. F., and Reynolds, J. A., 1979b, Molecular weight of (Nat,K’)ATPase from shark rectal gland, Biochemistry 18: 817–821.
Hastings, D., and Skou, J. C., 1980, Potassium binding to the (Na+ + K+)-ATPase, Biochim. Biophys. Acta 601: 380–385.
Haupert, G. T., 1983, Endogenous glycoside-like substances, Curr. Top. Membr. Transport 19:843–855. Haupert, G. T., and Sancho, J. M., 1979, Sodium transport inhibitor from bovine hypothalamus, Proc. Natl. Acad. Sci. USA 76: 4658–4660.
Hayashi, Y., Kimimura, M., Homareda, H., and Matsui, H., 1977, Purification and characteristics of (Nat,K“)-ATPase from canine kidney by zonal centrifugation in sucrose density gradient, Biochim. Biophys. Acta 482: 185–196.
Hebert, H., Jorgensen, P. L., Skriver, E., and Maunsbach, A. B., 1982, Crystallization patterns of membrane-bound (Nat + K+)-ATPase, Biochim. Biophys. Acta 689: 571–574.
Hegyvary, C., 1975, Covalent labeling of the digitalis-binding component of plasma membranes, Mol. Pharmacol. 11: 588–594.
Hegyvary, C., and Jsrgensen, P. L., 1981, Conformational changes of renal sodium plus potassium iontransport adenosine triphosphatase labelled with fluorescein, J. Biol. Chem. 256: 6296–6303.
Hegyvary, C., and Post, R. L., 1971, Binding of adenosine triphosphate to sodium and potassium ionstimulated adenosine triphosphatase, J. Biol. Chem. 246: 5234–5240.
Heinz, A., Rubinson, K. A., and Grantham, J. J., 1982, The transport and accumulation of oxyvanadium compounds in human erythrocytes in vitro, J. Lab. Clin. Med. 100: 593–612.
Henderson, G. R., and Askari, A., 1976, Transport ATPase: Thimerosal inhibits the Na+,K’-dependent ATPase activity without diminishing the Na“ -dependent ATPase activity, Biochem. Biophys. Res. Commun. 69: 499–505.
Henderson, G. R., and Askari, A., 1977, Transport ATPase: Further studies on the properties of the thimerosal-treated enzyme, Arch. Biochem. Biophys. 182: 221–226.
Henderson, G. R., Huang, W., and Askari, A., 1979, Transport ATPase—the different modes of inhibition of the enzyme by various mercury compounds, Biochem. Pharmacol. 28: 429–433.
Heppel, L. A., 1940, The diffusion of radioactive sodium into the muscles of potassium-deprived rats, Am. J. Physiol. 128: 449–454.
Hexum, T., Samson, F. E., and Himes, R. H., 1970, Kinetic studies of (Nat + K + Mg2’)-ATPase, Biochim. Biophys. Acta 212: 322–331.
Hilden, S., and Hokin, L. E., 1975, Active potassium transport coupled to active sodium transport in vesicles reconstituted from purified sodium and potassium ion-activated adenosine triphosphatase from the rectal gland of Squalus acanthias, J. Biol. Chem. 250: 6296–6303.
Hobbs, A. S., Albers, R. W., and Froehlich, J. P., 1980, Potassium-induced changes in phosphorylation and dephosphorylation of (Na+ + K+)-ATPase observed in the transient state, J. Biol. Chem. 255: 3395–3402.
Hobbs, A. S., Froehlich, J. P., and Albers, R. W., 1983, Inhibition by vanadate of the reactions catalyzed by the Na’ plus K’-stimulated ATPase: A transient state kinetic characterization, J. Biol. Chem. 255: 3724–3727.
Hodgkin, A. L., and Keynes, R. D., 1955, Active transport of cations in giant axons from Sepia and Loligo, J. Physiol. 128: 28–60.
Hoffman, J. F., 1966, The red cell membrane and the transport of sodium and potassium, Am. J. Med. 41: 666–680.
Hoffman, P. G., and Tosteson, D. C., 1971, Active sodium and potassium transport in high potassium and low potassium sheep red cells, J. Gen. Physiol. 58: 438–466.
Hokin, L. E., 1974, Purification and properties of the (sodium + potassium)-activated adenosine triphosphatase and reconstitution of sodium transport, Ann. N. Y. Acad. Sci. 242: 12–23.
Hokin, L. E., Dahl, J. L., Deupree, J. D., Dixon, J. F., Hackney, J. F., and Perdue, J. F., 1973, Studies on the characterization of the sodium—potassium transport adenosine triphosphatase. X. Purification of the enzyme from rectal gland of Squalus acanthias, J. Biol. Chem. 248: 2593–2605.
Homareda, H., and Matsui, H., 1982, Interaction of sodium and potassium ions with Na’,K’-ATPase. II. General properties of ouabain-sensitive K’ binding, J. Biochem (Tokyo) 92: 219–231.
Hopkins, B. E., Wagner, H., and Smith, T. W., 1976, Sodium-and potassium-activated adenosine triphosphatase of the nasal salt gland of the duck (Anas platyrhynchos). Purification characterization, and NH2-terminal amino acid sequence of the phosphorylating polypeptide, J. Biol. Chem. 251: 4365–4371.
Horowicz, P., Taylor, J. W., and Waggoner, D. M., 1970, Fractionation of sodium efflux in frog sartorius muscles by strophanthidin and removal of external sodium, J. Gen. Physiol. 55: 401–425.
Huang, W-H., and Askari, A., 1981, Phosphorylation-dependent cross-linking of the a-subunits in the presence of Ca’ and o-phenanthroline, Biochim. Biophys. Acta 645: 54–58.
Inturrisi, C. E., and Titus, E., 1968, Kinetics of oligomycin inhibition of sodium-and-potassium-activated adenosine triphosphatase from beef brain, Mol. Pharmacol. 4: 591–599.
Israel, Y., and Titus, E. O., 1967, A comparison of microsomal (Na’ + K’)-ATPase with K’-acetylphosphatase, Biochim. Biophys. Acta 139: 450–459.
Jackson, R. L., Verkleij, A. J., Van Zoelen, E. J. J., Lane, L. K., Schwartz, A., and Van Deenen, L. L. M., 1980, Asymmetric incorporation of Na“,K”-ATPase into phospholipid vesicles, Arch. Biochem. Biophys. 200: 269–278.
Järnefelt, J., 1962, Properties and possible mechanism of the Na’ and K’ -stimulated microsomal adenosine triphosphatase, Biochim. Biophys. Acta 59: 643–654.
Jensen, J., and Ottolenghi, P., 1976, Adenosine diphosphate binding to sodium-plus-potassium ion-dependent adenosine triphosphatase. The role of lipid in nucleotide-potassium ion interplay, Biochem. J. 159: 815–817.
Jensen, J., and Ottolenghi, P., 1983, Binding of Rb’ and ADP to a potassium-like form of Na,K-ATPase, Curr. Top. Membr. Trans. 19: 223–227.
Jensen, J., Nrby, J. G., and Ottolenghi, P., 1979, Is there a relationship between ATP-binding capacity and enzyme activity in thimerosal-treated Na,K-ATPase? in: Na,K-ATPase: Structure and Kinetics (J.C. Skou and J. G. N?rby, eds.), Academic Press, London, pp. 227–230.
Jöbsis, F. F., and Vreman, H. J., 1963, Inhibition of a Na’ and K’ stimulated adenosinetriphosphatase by oligomycin, Biochim. Biophys. Acta 73: 346–348.
Johannsson, A., Smith, G. A., and Metcalfe, J. C., 1981, The effect of bilayer thickness on the activity of (Na’ pl K’)-ATPase, Biochim. Biophys. Acta 641: 416–421.
J¢rgensen, P. L., 1974a, Purification and characterization of (Na’ + K’)-ATPase. III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by SDS, Biochim. Biophys. Acta 356: 36–52.
Jsensen, P. L., 1974b, Purification and characterization of (Na+ + K+)-ATPase. IV. Estimation of the purity and of the molecular weight and polypeptide content per enzyme unit in preparations from the outer medulla of the rabbit kidney, Biochim. Biophys. Acta 356:53–67.
Jsensen, P. L., 1975a, Purification and characterization of (Na’ + K’)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool, Biochim. Biophys. Acta 401: 399–415.
Jsgensen, P. L., 1975b, Isolation and characterization of the components of the sodium pump, Q. Rev. Biophys. 7: 239–274.
Jorgensen, P. L., 1977, Purification and characterization of (Na’ + K’)-ATPase. VI. Differential tryptic modification of catalytic functions of the purified enzyme in presence of NaCI and KC1, Biochim. Biophys. Acta 466: 97–108.
Jorgensen, J. C., 1982, Mechanism of the Na,K+ pump. Protein structure and conformations of the pure (Na+ + K+)-ATPase, Biochim. Biophys. Acta 694: 27–68.
Jorgensen, P. L., and Anner, B. M., 1979, Purification and characterization of (Na’ + K+)-ATPase. VIII. Altered Na+: K’ transport ratio in vesicles reconstituted with purified (Na+ + K+)-ATPase that has been selectively modified with trypsin in presence of NaCI, Biochim. Biophys. Acta 555: 485–492.
Jorgensen, P. L., and Karlish, S. J. D., 1980, Defective conformational response in a selectively trypsinized (Na+ + K +)-ATPase studied with tryptophan fluorescence, Biochim. Biophys. Acta 597: 305–317.
Jorgensen, P. L., and Klodos, I., 1978, Purification and characterization of (Na’ + K+)-ATPase. VII. Tryptic degradation of the Na-form of the enzyme protein resulting in selective modification of dephosphorylation reactions of the (Na“ + K+)-ATPase, Biochim. Biophys. Acta 507: 8–16.
Jorgensen, P. L., and Petersen, T., 1982, High-affinity 86Rb-binding and structural changes in the a-subunit of Na’,K“-ATPase as detected by tryptic digestion and fluorescence analysis, Biochim. Biophys. Acta 705: 38–47.
Jorgensen, P. L., and Skou, J. C. 1971, Purification and characterization of (Na+ + K+)-ATPase. I. Influence of detergents on the activity of (Na+ + K+)-ATPase in preparations from the outer medulla of rabbit kidney, Biochim. Biophys. Acta 233: 366–380.
Jorgensen, P. L., Hansen, O., Glynn, I. M., and Cavieres, J. D., 1973, Antibodies to pig kidney (Na+ + K+)ATPase inhibit the Na+ pump in human red cells provided they have access to the inner surface of the cell membrane, Biochim. Biophys. Acta 291: 795–800.
Jorgensen, P. L., Karlish, S. J. D., and Gitler, C., 1982a, Evidence for the organization of the transmembrane segments of (Na,K)-ATPase based on labeling lipid-embedded and surface domains of the a-subunit, J. Biol. Chem. 257: 7435–7442.
Jorgensen, P. L., Skriver, E., Hebert, H., and Maunsbach, A. B., 1982b, Structure of the Na,K-pump: Crystallization of pure membrane-bound Na,K-ATPase and identification of functional domains of the a-subunit, Ann. N. Y. Acad. Sci. 402: 207–224.
Jorgensen, P. L., Karlish, S. J. D., and Gitler, C.,1983, Organization of the transmembrane segments of Na,K-ATPase. Labeling of lipid embedded and surface domains of the a-subunit and its tryptic fragments with [125I]-iodonaphthylazide, [32P]-ATP, and photolabeled ouabain, Curr. Top Membr. Trans. 19:127–130.
Judah, J. D., Ahmed, K., and McLean, A. E. M., 1962, Ion transport and phosphoproteins of human red cells, Biochim. Biophys. Acta 65: 472–480.
Kanazawa, T., Saito, M., and Tonomura, Y., 1967, Properties of a phosphorylated protein as a reaction intermediate of the Na + K sensitive ATPase, J. Biochem. (Tokyo) 61: 555–566.
Kanazawa, T., Saito, M., and Tonomura, Y., 1970, Formation and decomposition of a phosphorylated intermediate in the reaction of Na*-K+ dependent ATPase, J. Biochem. (Tokyo) 67: 693–711.
Kaniike, K., Erdmann, E., and Schoner, W., 1973, ATP binding to (Na’ + K+)-activated ATPase, Biochim. Biophys. Acta 298: 901–905.
Kaniike, K., Lindenmayer, G. M., Wallick, E. T., Lane, L. K., and Schwartz, A., 1976, Specific sodium-22 binding to a purified sodium + potassium adenosine triphosphatase. Inhibition by ouabain, J. Biol. Chem. 251: 4794–4796.
Kapakos, J. G., and Steinberg, M., 1982, Fluorescent labeling of (Na + K)-ATPase by 5-iodoacetamidofluorescein, Biochim. Biophys. Acta 693: 493–496.
Kaplan, J. H., 1982, Sodium pump mediated ATP—ADP exchange. The sided effects of sodium and potassium ions, J. Gen. Physiol. 80: 915–937.
Kaplan, J. H., 1983, Na pump catalysed ATP: ADP exchange in red blood cells: The effects of intracellular and extracellular Na and K ions, Curr. Top. Membr. Trans. 19: 671–675.
Kaplan, J. H., and Hollis, R. J., 1980, External Na dependence of ouabain-sensitive ATP—ADP exchange initiated by photolysis of intracellular caged-ATP in human red cell ghosts, Nature 288: 587–589.
Karlish, S. J. D., 1980, Characterization of conformational changes in (Na,K)ATPase labeled with fluorescein at the active site, J. Bioenerg. Biomembr. 12: 111–135.
Karlish, S. J. D., and Glynn, I. M., 1974, An uncoupled efflux of sodium ions from human red cells, probably associated with Na-dependent ATPase activity, Ann. N. Y. Acad. Sci. 242: 461–470.
Karlish, S. J. D., and Pick, U., 1981, Sidedness of the effects of sodium and potassium ions on the conformational state of the sodium-potassium pump, J. Physiol. 312: 505–529.
Karlish, S. J. D., and Stein, W. D., 1982a, Passive rubidium fluxes mediated by Na-K-ATPase reconstituted into phospholipid vesicles when ATP- and phosphate-free, J. Physiol. 328: 295–316.
Karlish, S. J. D., and Stein, W. D., 1982b, Effects of ATP or phosphate on passive rubidium fluxes mediated by Na-K-ATPase reconstituted into phospholipid vesicles, J. Physiol. 328: 317–331.
Karlish, S. J. D., and Yates, D. W., 1978, Tryptophan fluorescence of (Na* + K’)-ATPase as a tool for study of the enzyme mechanism, Biochim. Biophys. Acta 527: 115–130.
Karlish, S. J. D., Jorgensen, P. L., and Gitler, C. 1977, Identification of a membrane-embedded segment of the large polypeptide chain of (Nat,K*)ATPase, Nature 269: 715–717.
Karlish, S. J. D., Yates, D. W., and Glynn, I. M., 1978a, Elementary steps of the (Na- + K*)-ATPase mechanism, studied with formycin nucleotides, Biochim. Biophys. Acta 525: 230–251.
Karlish, S. J. D., Yates, D. W., and Glynn, I. M., 1978b, Conformational transitions between Na*-bound and K*-bound forms of (Na + K“)-ATPase, studied with formycin nucleotides, Biochim. Biophys. Acta 525: 252–264.
Karlish, S. J. D., Beaugé, L. A., and Glynn, I. M., 1979, Vanadate inhibits (Na* + K*)ATPase by blocking a conformational change of the unphosphorylated form, Nature 282: 333–335.
Karlish, S. J. D., Lieb, W. R., and Stein, W. D., 1982, Combined effects of ATP and phosphate on rubidium exchange mediated by Na-K-ATPase reconstituted into phospholipid vesicles, J. Physiol. 328: 333–350.
Kennedy, B. G., and De Weer, P., 1976, Relationship between Na: K and Na: Na exchange by the sodium pump of skeletal muscle, Nature 268: 165–167.
Kennedy, B. G., Lunn, G., and Hoffman, J. F., 1983, Effect of intracellular adenine nucleotides on sodium pump catalyzed Na: Na and Na: K exchanges, Curr. Top. Memb. Trans. 19: 683–686.
Kepner, G. R., and Macey, R. I., 1968, Membrane enzyme systems. Molecular size determinations by radiation inactivation, Biochim. Biophys. Acta 163: 188–203.
Keynes, R. D., 1954, The ionic fluxes in frog muscle, Proc. R. Soc. B. 142: 359–382.
Keynes, R. D., and Steinhardt, R. A., 1968, The components of the Na efflux in frog muscle, J. Physiol. 198: 581–600.
Klevickis, C., and Grisham, C. M., 1982, Phosphorus-31 nuclear magnetic resonance studies of the conformation of an adenosine 5’-triphosphate analogue at the active site of (Na* + K)-ATPase from kidney medulla, Biochemistry 21: 69–79.
Klodos, I., and Ncy, J. G., 1979, Effect of K and Li on intermediary steps in the Na,K-ATPase reaction, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. N?rby, eds.), Academic Press, London, pp. 331–342.
Klodos, I., and Skou, J. C., 1975, The effect of Mg’* and chelating agents on intermediary steps of the reaction of Na,K-activated ATPase, Biochim. Biophys. Acta 391: 474–485.
Klodos, I., and Skou, J. C., 1977, The effect of chelators on Mg’, Na* -dependent phosphorylation of (Na* + K)-activated ATPase, Biochim. Biophys. Acta 481: 667–679.
Klodos, I., Nsrby, J. G., and Plesner, I. W., 1981, The steady-state kinetic mechanism of ATP hydrolysis catalysed by membrane-bound (Na* + K+)-ATPase from ox brain. II. Kinetic characterization of phosphointermediates, Biochim. Biophys. Acta 643: 463–482.
Koepsell, H., 1979, Conformational changes of membrane-bound (Nat + K *)-ATPase as revealed by trypsin digestion, J. Membr. Biol. 48: 69–94.
Koepsell, H., Hulla, F. W., and Fritzsch, G., 1982, Different classes of nucleotide binding sites in the (Na* + K+)-ATPase studied by affinity labeling and nucleotide-dependent SH-group modifications, J. Biol. Chem. 257: 10733–10741.
Koyal, D., Rao, S. N., and Askari, A., 1971, Studies on the partial reactions catalyzed by the (Nat + K*)- activated ATPase. I. Effects of simple anions and nucleotide triphosphates on the alkali-cation specificity of the p-nitrophenylphosphatase, Biochim. Biophys. Acta 225: 11–19.
Kracke, G. R., 1983, Absence of ouabain-like activity of the Na,K-ATPase inhibitor in guinea pig brain extract. Curr. Top. Membr. Trans. 19: 927–930.
Kudoh, F., Nakamura, S., Yamaguchi, M., and Tonomura, Y., 1979, Binding of ouabain to Na+K+dependent ATPase during the ATPase reaction. Evidence for a dimer structure of the ATPase, J. Biochem. (Tokyo) 86: 1023–1028.
Kuriki, Y., and Racker, E., 1976, Inhibition of (Na+ + K+)-adenosine triphosphatase and its partial reactions by quercetin, Biochemistry 15: 4951–4956.
Kuriki, Y., Halsey, J., Biltonen, R., and Racker, E., 1976, Calorimetric studies of the interactions of magnesium and phosphate with (Na+ + K+)ATPase: Evidence for a ligand induced conformational change in the enzyme, Biochemistry 15: 4956–4961.
Kyte, J., 1971, Purification of the sodium-and potassium-dependent adenosine triphosphatase from canine renal medulla, J. Biol. Chem. 246: 4157–4165.
Kyte, J., 1972, Properties of the two polypeptides of sodium-and potassium-dependent adenosine triphosphatase, J. Biol. Chem. 247: 7642–7649.
Kyte, J., 1975, Structural studies of sodium and potassium ion-activated adenosine triphosphatase. The relationship between molecular structure and the mechanism of active transport, J. Biol. Chem. 250: 7443–7449.
Kyte, J., 1976a, Immunoferritin determination of the distribution of (Na+ + K+)ATPase over the plasma membranes of renal convoluted tubules. I. Distal segment, J. Cell Biol. 68: 287–303.
Kyte, J., 1976b, Immunoferritin determination of the distribution of (Na+ + K+)ATPase over the plasma membranes of renal convoluted tubules. II. Proximal segment, J. Cell Biol. 68: 304–318.
Lane, L. K., Copenhaver, J. H., Lindenmayer, G. E., and Schwartz, A., 1973, Purification and characterization of, and [3H]ouabain binding to the transport adenosine triphosphatase from outer medulla of canine kidney, J. Biol. Chem. 248: 7197–7200.
Lant, A. F., Priestland, R. N., and Whittam, R., 1970, The coupling of downhill ion movements associated with reversal of the Na pump in human red cells, J. Physiol. 207: 291–301.
Lacis, P. C., and Letchworth, P. E., 1962, Cation influence on inorganic phosphate production in human erythrocytes, J. Cell. Comp. Physiol. 60: 229–234.
Lee, K. H., and Blostein, R., 1980, Red cell sodium fluxes catalysed by the sodium pump in the absence of K+ and ADP, Nature 285: 338–339.
Lew, V. L., and Beaugé, L. A., 1979, Passive cation fluxes in red cell membranes, in: Membrane Transport in Biology, ( G. Giebisch, D. C. Tosteson, and H. H. Ussing, eds.), Springer-Verlag, Berlin, pp. 81–115.
Lew, V. L., Glynn, I. M., and Ellory, J. C., 1970, Net synthesis of ATP by reversal of the sodium pump, Nature 225: 865–866.
Lew, V. L., Hardy, M. A., and Ellory, J. C., 1973, The uncoupled extrusion of Na+ through the Na+ pump, Biochim. Biophys. Acta 323: 251–266.
Liang, S-M., and Winter, C. G., 1977, Digitonin-induced changes in subunit arrangement in relation to some in vitro activities of the (Na+,K+)-ATPase, J. Biol. Chem. 252: 8278–8284.
Lin, M. H., and Akera, T., 1978, Increased (Na+,K+)-ATPase concentrations in various tissues of rats caused by thyroid hormone treatment, J. Biol. Chem. 253: 723–726.
Lindenmayer, G. E., and Schwartz, A., 1973, Nature of the transport adenosine triphosphatase digitalis complex. IV. Evidence that sodium—potassium competition modulates the rate of ouabain interaction with (Na“ + K+) adenosine triphosphatase during enzyme catalysis, J. Biol. Chem. 248: 1291–1300.
Lindenmayer, G. E., Laughter, A. H., and Schwartz, A., 1968, Incorporation of inorganic phosphate-32 into a Na+,K+-ATPase preparation: Stimulation by ouabain, Arch. Biochem. Biophys. 127: 187–192.
Lopez, V., Stevens, T., and Lindquist, R. N., 1976, Vanadium ion inhibition of alkaline phosphatasecatalyzed phosphate ester hydrolysis, Arch. Biochem. Biophys. 175: 31–38.
Lowe, A. G., and Reeve, L. A., 1983, Pre-steady state hydrolysis of ATP and enzyme phosphorylation in the Na,K-ATPase, Curr. Top. Membr. Trans. 19: 577–580.
Lowe, A. G., and Smart, J. W., 1977, The pre-steady-state hydrolysis of ATP by porcine brain (Na+ + K+)-dependent ATPase, Biochim. Biophys. Acta 481: 695–705.
Macara, I. G., Kustin, K., and Cantley, L. C., 1980, Glutathione reduces cytoplasmic vanadate. Mechanism and physiological implications, Biochim. Biophys. Acta 629: 95–106.
MacGregor, G. A., Fenton, S., Alaghband-Zadeh, J., Markandu, N., Roulston, J. E., and De Wardener, H., 1981, Evidence for a raised concentration of a circulating sodium transport inhibitor in essential hypertension, Br. Med. J. 283: 1355–1357.
Maizels, M., and Patterson, J. H., 1940, Survival of stored blood after transfusion, Lancet 2:417–420. Mârdh, S., 1975a, Bovine brain Nat,K+-stimulated ATP phosphohydrolase studied by a rapid-mixing technique. K+-stimulated liberation of [32P]orthophosphate from [32P]phosphoenzyme and resolution of the dephosphorylation into two phases, Biochim. Biophys. Acta 391: 448–463.
Mârdh, S., 1975b, Bovine brain Na +,K + -stimulated ATP phosphohydrolase studied by a rapid-mixing technique. Detection of a transient [32P]phosphoenzyme formed in the presence of potassium ions, Biochim. Biophys. Acta 391: 464–473.
Mârdh, S., and Lindahl, S., 1977, On the mechanism of sodium-and potassium-activated adenosine triphosphatase. Time course of intermediary steps examined by computer simulation of transient kinetics, J. Biol. Chem. 252: 8058–8061.
Mârdh, S., and Post, R. L., 1977, Phosphorylation from adenosine triphosphate of sodium-and potassium-activated adenosine triphosphatase. Comparison of enzyme-ligand complexes as precursors to the phosphoenzyme, J. Biol. Chem. 252: 633–638.
Mârdh, S., and Zetterqvist, O., 1972, Phosphorylation of bovine brain Na,K-stimulated ATP phosphohydrolase by adenosine-[32P]triphosphate studied by a rapid-mixing technique, Biochim. Biophys. Acta 255: 231–238.
Mârdh, S., and Zetterqvist, O., 1974, Phosphorylation and dephosphorylation reactions of bovine brain (Nat -K“)-stimulated ATP phosphohydrolase studied by a rapid-mixing technique, Biochim. Biophys. Acta 350: 473–483.
Masiak, S. J., and D’Angelo, G., 1975, Effects of N-acetylimidazole on human erythrocyte ATPase activity. Evidence for a tyrosyl residue at the ATP-binding site of the (Na + K+)-dependent ATPase, Biochim. Biophys. Acta 382: 83–91.
Matchett, P. A., and Johnson, J. A., 1954, Inhibition of Na and K transport in frog sartorii in the presence of ouabain, Fed. Proc. 13: 384.
Matsui, H., and Homareda, H., 1982, Interaction of sodium and potassium ions with Nat,K“-ATPase. I. Ouabain-sensitive alternative binding of three Na+ or two K+ to the enzyme, J. Biochem. (Tokyo) 92: 193–217.
Matsui, H., and Schwartz, A., 1968, A mechanism of cardiac glycoside inhibition of the (Nat + K+)-dependent ATPase from cardiac tissue, Biochim. Biophys. Acta 151: 655–663.
Matsui, H., Hayashi, Y., Homareda, H., and Kimimura, M., 1977, Ouabain-sensitive 42K binding to,K * -ATPase purified from canine kidney outer medulla, Biochem. Biophys. Res. Commun. 75: 373–380.
Matsui, H., Hayashi, Y., Homareda, H., and Taguchi, M., 1983, Stoichiometrical binding of ligands to less than 160 K Daltons of Na’,K+-ATPase, Curr. Top. Membr. Trans. 19: 145–148.
Maunsbach, A. B., Deguchi, N., and Jsrgensen, P. L., 1978, Ultrastructure of purified Na,K-ATPase, in: FEBS Symp. A4, Membrane Proteins, Vol. 45 ( P. Nicholls, J. V. Moller, P. L. Jcrgensen, and A. J. Moody, eds.), Pergamon, New York, pp. 173–181.
Maunsbach, A. B., Skriver, E., and Jrgensen, P. L., 1979, Ultrastructure of purified Na,K-ATPase membranes, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. Nrby, eds.), Academic Press, London, pp. 3–13.
Maunsbach, A. B., Skriver, E., and J¢rgensen, P. L., 1983, Electron microscope analysis of protein distribution in purified, membrane-bound Na,K-ATPase, Curr. Top. Membr. Trans. 19, in press.
Mercer, R. W., and Dunham. P. B., 1981, Membrane-bound ATP fuels the Na/K pump. Studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes, J. Gen. Physiol. 78: 547–568.
Moczydlowski, E. G., and Fortes, P. A. G., 1981a, Characterization of 2’3’-O-(2,4,6-trinitrocyclohexadienylidene) adenosine 5’-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP, J. Biol. Chem. 256: 2346–2356.
Moczydlowski, E. G., and Fortes, P. A. G., 1981b, Inhibition of sodium and potassium adenosine triphosphatase by 2’3’-O-(2,4,6-trinitrocyclohexadienylidene) adenine nucleotides. Implications for the structure and mechanism of the Na: K pump, J. Biol. Chem. 256: 2357–2366.
Mone, M.D. and Kaplan, J.H., 1983, Cation activation of Na,K-ATPase after treatment with thimerosal, Curr. Top. Membr. Trans. 19: 465–469.
Mullins, L. J., and Brinley, F. J., 1969, Potassium fluxes in dialyzed squid axons, J. Gen. Physiol. 53: 704–740.
Mullins, L. J., Fenn, W. O., Noonan, T. R., and Haege, L., 1941, Permeability of erythrocytes to radioactive potassium, Am. J. Physiol. 135: 93–101.
Munakata, H., Schmid, K., Collins, J. H., Zot, A., Lane, L. K., and Schwartz, A., 1982, The a and 13 subunits of lamb kidney Na,K-ATPase are both glycoproteins, Biochem. Biophys. Res. Commun. 107: 229–231.
Munson, K. B.; 1981, Light dependent inactivation of (Na + K+)-ATPase with a new photoaffinity reagent, chromium arylazido-ß-alanyl ATP, J. Biol. Chem. 256:3223-3230.
Nagai, K., and Yoshida, H., 1966, Biphasic effects of nucleotides on potassium dependent phosphatase, Biochim. Biophys. Acta 128: 410–412.
Nagai, K., Izumi, F., and Yoshida, H., 1966, Studies on potassium dependent phosphatase: Its distribution and properties, J. Biochem (Tokyo) 59: 295–303.
Nagano, K., Fujihara, Y., Hara, Y., and Nakao, M., 1973, ATP as a modulator of Na*,K+,-ATPase, in: Organization of Energy-Transducing Membranes ( M. Nakao and L. Packer, eds.), University of Tokyo Press, Tokyo, pp. 47–61.
Naidoo, B. K., Witty, T. R., Remers, W. A., and Besch, H. R., 1974, Cardiotonic steroids: I. Importance of 14 3-hydroxy in digitoxigenin, J. Pharmcol. Sci. 63: 1391–1394.
Nakao, T., Nakao, M., Nagai, F., Kawai, K., Fujihara, Y., Hara, Y., and Fujita, M., 1973, Purification and some properties of Na,K-transport ATPase. II. Preparations with high specific activity obtained using aminoethyl cellulose chromatography, J. Biochem. (Tokyo) 73: 781–791.
Neufeld, A. H., and Levy, H. M., 1969, A second ouabain-sensitive Na dependent ATPase in brain microsomes, J. Biol. Chem. 244: 6493–6497.
Neufeld, A. H., and Levy, H. M., 1970, The steady state level of phosphorylated intermediate in relation to the two sodium-dependent adenosine triphosphatases of calf brain microsomes, J. Biol. Chem. 245: 4962–4967.
Noble, D., 1980, Mechanisms of action of therapeutic levels of glycosides, Cardiovasc. Res. 14:495–514. Noonan, T. R., Fenn, W. O., and Haege, L., 1940, The distribution of injected radioactive potassium in rats, Am. J. Physiol. 132: 474–488.
NOrby, J. G., 1983, Ligand interactions with the substrate site of Na,K-ATPase: Nucleotides, vanadate and phosphorylation, Curr. Top. Membr. Trans. 19: 281–314.
NOrby, J. G., and Jensen, J., 1971, Binding of ATP to brain microsomal ATPase. Determination of the ATP-binding capacity and the dissociation constant of the enzyme-ATP complex as a function of K concentration, Biochim. Biophys. Acta 233: 104–116.
O’Connor, S. E., and Grisham, C. M., 1980, Distance determination at the active site of kidney (Nat + K+)ATPase by Mn(II) ion electron paramagnetic resonance, FEBS Lett. 118: 303–307.
Ottolenghi, P., 1979, The relipidation of delipidated Na,K-ATPase. An analysis of complex formation with dioleoylphosphatidylcholine and with dioleoylphophatidylethanolamine, Eur. J. Biochem. 99: 113–131.
Ottolenghi, P., and Jensen, J., 1983, The K + -induced apparent heterogeneity of high-affinity nucleotide-binding sites in (Na+ + K+)-ATPase can only be due to the oligomeric structure of the enzyme, Biochim. Biophys. Acta 727 in press.
Ottolenghi, P., Ellory, J. C., and Klein, R., 1983, Radiation inactivation analysis of the partial reactions of NaK activated ATPase, Curr. Top. Membr. Trans. 19 in press.
Overton, E., 1902, Beitrage zur allgemeinen Muskel-und Nervenphysiologie. II. Mittheilung. Ueber die Unentbehrlichkeit von Natrium- (oder Lithium-) Ionen fur den Contractionsact des Muskels, Pflugers Arch. Ges. Physiol. 92: 346–386.
Pachence, J. M., Schoenborn, B. P., and Edelman, I. S., 1983, Low angle neutron scattering analysis of Na/K-ATPase in detergent solution, Biophys. J. 41: 370a.
Patzelt-Wenczler, R., and Mertens, W., 1981, Effects of cations on high-affinity and low-affinity ATP-binding sites of (Na,K)-ATPase as studied by disulfides of thioinosine triphosphate and its analogue, Eur. J. Biochem. 121: 197–202.
Patzelt-Wenczler, R., and Schoner, W., 1981, Evidence for two different reactive sulfhydryl groups in the ATP-binding sites of (Na* + K)-ATPase, Eur. J. Biochem. 114: 79–87.
Perez, B., Miara, J., and Dahms, A. S., 1979, Probes at the medium and intermediate water oxygen exchange reactions of the Na,K-ATPase, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. Nrby, eds.), Academic Press, London, pp. 343-3358.
Perrone, J. R., Hackney, J. F., Dixon, J. F., and Hokin, L. E., 1975, Molecular properties of purified (sodium and potassium)-activated adenosine triphosphatases and their subunits from the rectal gland of Squalus acanthias and the electric organ of Electrophorus electricus, J. Biol. Chem. 250: 4178–4184.
Peters, W. H. M., Du Pont, J. J. H. H. M., Koppers, A., and Bonting, S. L., 1981, Studies on (Na+ + K“)-activated ATPase. XLVII. Chemical composition, molecular weight and molar ratio of the subunits of the enzyme from rabbit kidney outer medulla, Biochim. Biophys. Acta 641: 55–70.
Peterson, G. L., and Hokin, L. E., 1980, Improved purification of brine-shrimp (Anemia saline) (Na + K ’)activated adenosine triphosphatase and amino-acid and carbohydrate analogues of the isolated subunits, Biochem.J. 192: 107–118.
Peterson, G. L., and Hokin, L. E., 1981, Molecular weight and stoichiometry of the sodium-and potassium-activated adenosine triphosphatase subunits, J. Biol. Chem. 256: 3751–3761.
Plesner, L., and Plesner, I. W., 198la, The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ K)-ATPase from ox brain. I. Substrate identity, Biochim. Biophys. Acta 643:449-462.
Plesner, I. W., and Plesner, L., 1981b, The steady state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na- + K’)-ATPase from ox brain. IV. Rate-constant determination, Biochim. Biophys. Acta 648: 231–246.
Plesner, I. W., Plesner, L., N¢rby, J. G., and Klodos, I., 1981, The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. III. A minimal model, Biochim. Biophys. Acta 643: 483–494.
Post, R. L., and Kume, S., 1973, Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase, J. Biol. Chem. 248: 6993–7000.
Post, R. L., and Sen, A. K., 1965, An enzymatic mechanism of active sodium and potassium transport, J. Histochem. 13: 105–112.
Post, R. L., Merritt, C. R., Kinsolving, C. R., and Albright, C. D., 1960, Membrane adenosine triphosphate-dependent sodium and potassium transport across kidney membrane, J. Biol. Chem. 240: 1437–1445.
Post, R. L., Sen, A. K., and Rosenthal, A. S., 1965, A phosphorylated intermediate in adenosine triphosphate-dependent sodium and potassium transport across kidney membranes, J. Biol. Chem. 240: 1437–1445.
Post, R. L., Kume, S., Tobin, T., Orcutt, B., and Sen, A. K., 1969, Flexibility of an active centre in sodium-plus-potassium adenosine triphosphatase, J. Gen. Physiol. 54: 306s - 326s.
Post, R. L., Hegyvary, C., and Kume, S., 1972, Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase, J. Biol. Chem. 247: 6530–66540.
Post, R. L., Kume, S., and Rogers, F. N., 1973, Alternating paths of phosphorylation of the sodium and potassium ion pump of plasma membranes, in: Mechanisms in Bioenergetics ( G. F. Azzone, S. Ernster, E. Papa, N. Quagliariello, and N. Siliprandi, eds.), Academic Press, New York, pp. 203–218.
Post, R. L., Toda, G., and Rogers, F. N., 1975a, Phosphorylation by inorganic phosphate of sodium plus potassium ion transport adenosine triphosphatase. Four reactive states, J. Biol. Chem. 250: 691–701.
Post, R. L., Toda, G., Kume, S., and Taniguchi, K., 1975b, Synthesis of adenosine triphosphate by way of potassium-sensitive phosphoenzyme of sodium, potassium adenosine triphosphatase, J. Supramolec. Struct. 3: 479–497.
Post, R. L., Hunt, D., Walderhaug, M. O., Perkins, R. C., Park, J. H., and Beth, A. H., 1979, Vanadium compounds in relation to inhibition of sodium and potassium adenosine triphosphatase, in: Na,KATPase: Structure and Kinetics (J. C. Skou and J. G. Nrby, eds.), Academic Press, London, pp. 389–401.
Poston, L., Sewell, R. B., Wilkinson, S. P., Richardson, P. J., Williams, R., Clarkson, E. M., MacGregor, G. A., and De Wardener, H. E., 1981, Evidence for a circulating sodium transport inhibitor in essential hypertension, Br. Med. J. 282: 847–849.
Priestland, R. N., and Whittam, R., 1968, The influence of external sodium ions on the sodium pump in erythrocytes, J. Physiol. 109: 369–374.
Proverbio, F., and Hoffman, J. F., 1977, Membrane compartmentalized ATP and its preferential use by the Na,K-ATPase of human red cell ghosts, J. Gen. Physiol. 69: 605–632.
Reeves, A. S., Collins, J. H., and Schwartz, A., 1980, Isolation and characterization of (Na,K)-ATPase proteolipid, Biochem. Biophys. Res. Commun. 95: 1591–1598.
Rega, A. F., Garrahan, P. J., and Pouchan, M. I., 1970, Potassium activated phosphatase from human red blood cells. The asymmetrical effects of K+, Na’, Mg’ + and adenosine triphosphate, J. Membr. Biol. 3: 14–25.
Rempeters, G., and Schoner, W., 1983, Imidazole chloride and Tris chloride substitute for sodium chloride in inducing high affinity AdoPP[NH]P binding to (Na* + K+)-ATPase, Biochim. Biophys. Acta 727: 13–21.
Repke, K. R. H., 1965, Effect of digitalis on membrane adenosine triphosphatase of heart muscle, in: Drugs and Enzymes, Vol. 4 (B. B. Brodie and J. Gillette, eds.), Proc. 2nd Int. Pharmacol. Meet. Prague, 1963, Pergamon Press, Oxford, and Czechoslovak Medical Press, pp. 65–87.
Repke, K. R. H., and Dittrich, F., 1979, Subunit-subunit interaction: Determinant of reactivity and cooperativity of Na,K-ATPase, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. Nrby, eds.), Academic Press, London, pp. 487–500.
Repke, K. R. H., and Portius, H. J., 1966, Analysis of structure activity relationships in cardioactive compounds on the molecular level, in: Scientiae Pharmaceuticae—I, Proc. 25th Congr. Pharmaceut. Sci., Prague, 1965, pp. 39–57.
Repke, K. R. H., and Schon, R., 1973, Flip-Flop model of (Na,K)-ATPase function, Acta Biol. Med. Ger. 31: K19 - K30.
Richards, D. E., Ellory, J. C., and Glynn, I. M., 1981, Radiation inactivation of (Na’ + K+)-ATPase. A small target size for the K+-occluding mechanism, Biochim. Biophys. Acta 648: 284–286.
Robinson, J. D., 1969, Kinetic studies on a brain microsomal adenosine triphosphatase. III. Potassium-dependent phosphatase activity, Biochemistry 8: 3348–3355.
Robinson, J. D., 1970, Phosphatase activity stimulated by Na+ plus K+: Implications for the (Na+ plus K+)-dependent adenosine triphosphatase, Arch. Biochem. Biophys. 139: 164–171.
Robinson, J. D., 1973, Cation sites of the (Na+ + K’)-dependent ATPase. Mechanisms for Nat –induced changes in K+ affinity of the phosphatase activity, Biochim. Biophys. Acta 321: 662–670.
Robinson, J. D., 1974, Nucleotide and divalent cation interactions with the (Na’ + K+)-ependent AT-Pase, Biochim. Biophys. Acta 341: 232–247.
Robinson, J. D., 1975, Functionally distinct classes of K+ sites on the (Nat + K’)-dependent ATPase, Biochim. Biophys. Acta 384: 250–264.
Robinson, J. D., 1976a, Substrate sites of the (Nat + K+)-dependent ATPase, Biochim. Biophys. Acta 429: 1006–1019.
Robinson, J. D., 1976b, The (Na+ + K’)-dependent ATPase; mode of inhibition of ADP/ATP exchange activity by MgCl2, Biochim. Biophys. Acta 440: 711–722.
Robinson, J. D., 1980, Sensitivity of the (Nat + K+)-ATPase to state-dependent inhibitors: Effects of digitonin and Triton X-100, Biochim. Biophys. Acta 598: 543–553.
Robinson, J. D., 1981, Substituting manganese for magnesium alters certain reaction properties of the (Na’ + K+)-ATPase, Biochim. Biophys. Acta 642: 405–417.
Robinson, J. D., 1982, Tryptic digestion of the (Na + K)-ATPase is both sensitive to and modifies K’ interactions with the enzyme, J. Bioenerg. Biomembr. 14: 319–333.
Robinson, J. D., 1983, Kinetic studies on the (Na+ + K’)-dependent ATPase. Evidence for coexisting sites for Na’, K+ and Mg’, Biochim. Biophys. Acta 727: 63–69.
Robinson, J. D., and Flashner, M. S., 1979, The (Nat + K+)-activated ATPase; enzymatic and transport properties, Biochim. Biophys. Acta 549: 145–176.
Robinson, J. D., and Mercer, R. W., 1981, Vanadate binding to the (Na + K)-ATPase, J. Bioenerg. Biomembr. 13: 205–218.
Robinson, J. D., Flashner, M. S., and Marin, G. K., 1978, Inhibition of the (Na’ + K+)-dependent ATPase by inorganic phosphate, Biochim. Biophys. Acta 509: 419–428.
Rogers, T. B., and Lazdunski, M., 1979a, Photoaffinity labeling of the digitalis receptor in the (sodium + potassium)-activated adenosinetriphosphatase, Biochemistry 18: 135–140.
Rogers, T. B., and Lazdunski, M., 1979b, Photoaffinity labelling of a small protein component of a purified (Na’ + K’)ATPase, FEBS Lett. 98: 373–376.
Rossi, B., Gache, C., and Lazdunski, M., 1978, Specificity and interactions at the cationic sites of the axonal (Na’,K’)-activated adenosinetriphosphatase, Eur. J. Biochem. 85: 561–570.
Rossi, B., Vuilleumier, P., Gache, C., Balerna, M., and Lazdunski, M., 1980, Affinity labeling of the digitalis receptor with p-nitrophenyltriazene-ouabain, a highly specific alkylating agent, J. Biol. Chem. 255: 9936–9941.
Rossi, B., Ponzio, G., and Lazdunski, M., 1982, Identification of the segment of the catalytic subunit of (Na’, K’)ATPase containing the digitalis binding site, EMBO J. 1: 859–861.
Rubinson, K. A., 1981, Concerning the form of biochemically active vanadium, Proc. R. Soc. B. 212: 65–84.
Ruoho, A., and Kyte, J., 1974, Photoaffinity labeling of the ouabain-binding site on (Na’ + K’)adenosinetriphosphatase, Proc. Natl. Acad. Sci. USA 71: 2352–2356.
Sabatini, D., Golman, D., Sabban, E., Sherman, J., Morimoto, T., Kreibich, G., and Adesnik, M., 1982, Mechanisms for the incorporation of protein into the plasma membranes, Cold Spring Harbor Symp. Quant. Biol. XLVI:807–818.
Sachs, J. R., 1967, Competition effects of some cations on active potassium transport in the human red blood cell, J. Clin. Invest. 46: 1433–1441.
Sachs, J. R., 1970, Sodium movements in the human red blood cell, J. Gen. Physiol. 56: 322–341.
Sachs. J. R., 1972, Recoupling the Na-K pump, J. Clin. Invest. 51: 3244–3247.
Sachs, J. R., 1974, Interaction of external K, Na, and cardioactive steroids with Na-K pump of the human red blood cell, J. Gen. Physiol. 63: 123–143.
Sachs, J. R., 1977a, Kinetics of the inhibition of the Na-K pump by external sodium, J. Physiol. 264: 449–470.
Sachs, J. R., 1977b, Kinetic evaluation of the Na-K pump reaction mechanisms, J. Physiol. 273: 489–514.
Sachs, J. R., 1979, A modified consecutive model for the Na,K-pump, in: Na,K-ATPase: Structure and Kinetics ( J. C. Skou and J. G. Ndrby, eds.), Academic Press, London, pp. 463–473.
Sachs, J. R., 1980, The order of release of sodium and addition of potassium in the sodium—potassium pump reaction mechanism, J. Physiol. 302: 219–240.
Sachs, J. R., 1981a, Mechanistic implications of the potassium—potassium exchange carried out by the sodium—potassium pump, J. Physiol. 316: 263–277.
Sachs, J. R., 1981b, Internal potassium stimulates the sodium—potassium pump by increasing cell ATP concentration, J. Physiol. 319: 515–528.
Sachs, J. R., and Welt, L. G., 1967, The concentration dependence of active K transport in the human red blood cell, J. Clin. Invest. 46: 65–76.
Sachs, S., Rose, J. D., and Hirschowitz, B. I., 1967, Acetyl phosphatase in brain microsomes: A partial reaction of Na + K’-ATPase, Arch. Biochem. Biophys. 119: 277–281.
Schatzmann, H. J., 1953, Herzglykoside als Hemmstoffe fur den aktiven Kalium und Natrium Transport durch die Erythrocytenmembran, Helv. Physiol. Acta 11: 346–354.
Schönfeld, W., Schön, R., Menke, K. H., and Repke, K. R. H., 1972, Identification of conformational states of transport ATPase by kinetic analysis of ouabain binding, Acta Biol. Med. Germ. 28: 935–956.
Schoot, B. M., Van Emst-de Vries, S. E., Van Haard, P. M. M., De Pont, J. J. H. H. M., and Bonting, S. L., 1980, Studies on (Na* + K’)-activated ATPase. XLVI. Effect on cation-induced conformational changes on sulthydryl group modification, Biochim. Biophys. Acta 602: 144–154.
Schuurmans Stekhoven, F. M. A. H., and Bonting, S. L., 1981, Transport adenosine triphosphatases: Properties and functions, Physiol. Rev. 61: 1–76.
Schuurmans Stekhoven, F. M. A. H., Swarts, H. G. P., De Pont, J. J. H. H. M., and Bonting, S. L., 1980, Studies in (Na’ + K’)-activated ATPase. XLIV. Single phosphate incorporation during dual phosphorylation by inorganic phosphate and adenosine triphosphate, Biochim. Biophys. Acta 597: 100–111.
Schuurmans Stekhoven, F. M. A. H., Swarts, H. G. P., De Pont, J. J. H. H. M., and Bonting, S. L., 1981, Studies on (Na’ + K’)-activated ATPase. XLV. Magnesium induces two low-affinity non-phosphorylating nucleotide binding sites per molecule, Biochim. Biophys. Acta 649: 533–540.
Schwartz, A., Matsui, H., and Laughter, A. H., 1968, Tritiated digoxin binding to (Na’ + K’)-activated adenosine triphosphatase: Possible allosteric site, Science 160: 323–325.
Schwartz, A., Lindenmayer, G. E., and Allen, J. C., 1975, The sodium-potassium adenosine triphosphatase: pharmacological, physiological, and biochemical aspects, Pharmacol. Rev. 27: 3–134.
Schwartz, A., Whitmer, K., Grupp, G., Grupp, I., Adams, R. J., and Lee, S-W., 1982, Mechanism of action of digitalis: Is the Na,K-ATPase the pharmacological receptor ? Ann. N. Y. Acad. Sci. 402: 253–270.
Sen, A. K., Tobin, T., and Post, R. L., 1969, A cycle for ouabain inhibition of sodium-and potassium-dependent adenosine triphosphatase, J. Biol. Chem. 244: 6596–6604.
Sen, P. C., Kapakos, J. G., and Steinberg, M., 1981, Modification of (Nat + K+)-dependent ATPase by fluorescein isothiocyanate: Evidence for the involvement of different amino groups at different pH values, Arch. Biochem. Biophys. 211: 652–661.
Shaffer, E., Azari, J., and Dahms, A. S., 1978, Properties of the Pi—oxygen exchange reaction catalyzed by (Na+,K+)-dependent adenosine triphosphatase, J. Biol. Chem. 253: 5696–5706.
Shaver, J. L., and Stirling, C., 1978, Ouabain binding to renal tubules of the rabbit, J. Cell Biol. 76: 278–292.
Siegel, G. J., 1979, Revised enzyme reaction model for Na,K-ATPase incorporating consecutive and simultaneous reactions with Na+ and K+, in: Na,K-ATPase: Structure and Kinetics ( J. C. Skou and J. G. NOrby, eds.), Academic Press, London, pp. 287–299.
Siegel, G. J., and Albers, R. W., 1967, Sodium—potassium activated adenosine triphosphatase of Electrophorus electric organ. IV. Modification of responses to sodium and potassium by arsenite plus 2,3dimercaptopropanol, J. Biol. Chem. 242: 4972–4975.
Siegel, G. J., Koval, G. J., and Albers, R. W., 1969, Sodium—potassium-activated adenosine triphosphatase. VI. Characterization of the phosphoprotein formed from orthophosphate in the presence of ouabain, J. Biol. Chem. 244: 3264–3269.
Siegel, G. J., Fogt, S. K., and Iyengar, S., 1973, Characteristics of lead ion-stimulated phosphorylation of Electrophorus electricus electroplax (Na + K+)-adenosine triphosphatase and inhibition of ATP—ADP exchange, J. Biol. Chem. 253: 7207–7211.
Simons, T. J. B., 1974, Potassium: potassium exchange catalysed by the sodium pump in human red cells, J. Physiol. 237: 123–155.
Simons, T. J. B., 1975, The interaction of ATP-analogues possessing a blocked y-phosphate group with the sodium pump in human red cells, J. Physiol. 244: 731–739.
Sjodin, R. A., 1971, The kinetics of Na extrusion in striated muscle as functions of the external sodium and potassium ion concentrations, J. Gen. Physiol. 57: 164–187.
Skou, J. C., 1957, The influence of some cations on an adenosine triphosphatase from peripheral nerves, Biochim. Biophys. Acta 23: 394–401.
Skou, J. C., 1960, Further investigations on a Mg’ + + Nat-activated adenosine triphosphatase, possibly related to the active linked transport of Na+ and K+ across the nerve membrane, Biochim. Biophys. Acta 42: 6–23.
Skou, J. C., 1965, Enzymatic basis for active transport of Na+ and K+ across cell membrane, Physiol. Rev. 45: 596–617.
Skou, J. C., 1971, Sequence of steps in the (Na + K)-activated enzyme system in relation to sodium and potassium transport, Curr. Top. Bioenerg. 4: 357–398.
Skou, J. C., 1974a, Effect of ATP on the intermediary steps of the reaction of the (Na+ + K+)-dependent enzyme system. I. Studied by the use of N-ethylmaleimide inhibition as a tool, Biochim. Biophys. Acta 339: 234–245.
Skou, J. C., 1974b, Effect of ATP on the intermediary steps of the reaction of the (Na+ + K+)-dependent enzyme system. III. Effect on the p-nitrophenylphosphatase activity of the system, Biochim. Biophys. Acta 339: 258–273.
Skou, J. C., 1982, The effect of pH, of ATP and of modification with pyridoxal 5-phosphate on the conformational transition between the Nat-form and the K+-form of the (Nat + K+)-ATPase, Biochim. Biophys. Acta 688: 369–380.
Skou, J. C., and Esmann, M., 1979, Preparation of membrane-bound and of solubilized (Na+ + K“)ATPase from rectal glands of Squalus acanthias. The effect of preparative procedures on purity, specific and molar activity, Biochim. Biophys. Acta 567: 436–114.
Skou, J. C., and Esmann, M., 1980, Effects of ATP and protons on the Na: K selectivity of the (Na+ + K+)ATPase studied by ligand effects on intrinsic and extrinsic fluorescence, Biochim. Biophys. Acta 601: 386–402.
Skou, J. C., and Esmann, M., 1981, Eosin, a fluorescent probe of ATP binding to the (Na* + K“)- ATPase, Biochim. Biophys. Acta 647: 232–240.
Skou, J. C., and Esmann, M., 1983, Effect of magnesium ions on the high-affinity binding of eosin to the (Na* + K*)-ATPase, Biochim. Biophys. Acta 727: 101–107.
Skriver, E., Maunsbach, A. B., and Jsrgensen, P. L., 1980, Ultrastructure of Na,K-transport vesicles reconstituted with purified renal Na,K-ATPase, J. Cell Biol. 86: 746–754.
Skvortsevich, E. G., Panteleeva, N. S., and Pisareva, L. N., 1972, The reaction of oxygen isotope exchange in the system of Na’-K+-dependent ATPase, Proc. Acad. Sci. USSR 206: 240.
Smith, R. L., Zinn, K., and Cantley, L. C., 1980, A study of the vanadate-trapped state of the (Na,K)-ATPase. Evidence against interacting nucleotide site models, J. Biol. Chem. 255: 9852–9859.
Stein, W. D., Lieb, W. R., Karlish, S. J. D., and Eilam, Y., 1973, A model for the active transport of sodium and potassium ions as mediated by a tetrameric enzyme, Proc. Natl. Acad. Sci. USA 70: 275–278.
Steinbach, H. B., 1940, Sodium and potassium in frog muscle, J. Biol. Chem. 133: 695–701.
Steinbach, H. B., 1951, Sodium extrusion from isolated frog muscle, Am. J. Physiol. 167: 284–287.
Steinbach, H. B., 1952, On the sodium and potassium balance of isolated frog muscles, Proc. Natl. Acad. Sci. USA 38: 451–455.
Swann, A. C., 1983, (Na+K)-ATPase of mammalian brain: Effects of temperature on cation and ATP interactions regulating phosphatase activity, Arch. Biochem. Biophys. 221:148–157.
Swann, A. C., and Albers, R. W., 1975, Sodium + potassium-activated ATPase of mammalian brain; regulation of phosphatase activity, Biochim. Biophys. Acta 382: 437–456.
Swann, A. C., and Albers, R. W., 1978, Sodium and potassium ion dependent adenosine triphosphatase of mammalian brain; interactions of magnesium ions with the phosphatase site, Biochim. Biophys. Acta 523: 215–227.
Swann, A. C., and Albers, R. W., 1980, (Na++ K+)-ATPase of mammalian brain: Differential effects on cation affinities of phosphorylation by ATP and acetylphosphate, Arch. Biochem. Biophys. 203:422–427.
Sweadner, K. J., 1979, Two molecular forms of (Na* + K*)-stimulated ATPase in brain. Separation and difference in affinity for strophanthidin, J. Biol. Chem. 254: 6060–6067.
Sweadner, K. J., and Goldin, S. M., 1975, Reconstitution of active ion transport by the sodium and potassium ion-stimulated adenosine triphosphatase from canine brain, J. Biol. Chem. 250: 4022–4024.
Taniguchi, K., and Iida, S., 1972, Two apparently different ouabain binding sites of (Na* + K+)-ATPase, Biochim. Biophys. Acta 288: 98–102.
Taniguchi, K., and Iida, S., 1972, Two apparently different ouabain binding sites of (Na* + K*)-ATPase, Biochim. Biophys. Acta 288: 98–102.
Taniguchi, K., and Post, R. L., 1975, Synthesis of adenosine triphosphate and exchange between inorganic phosphate and adenosine triphosphate in sodium and potassium ion transport adenosine triphosphatase, J. Biol. Chem. 250: 3010–3018.
Taniguchi, K., Suzuki, K., and Iida, S., 1982, Conformational change accompanying transition of ADP-sensitive phosphoenzyme to potassium-sensitive phosphoenzyme of (Na’,K“)-ATPase modified with N-[p-(2-benzimidazolyl)phenyllmaleimide, J. Biol. Chem. 257: 10659–10667.
Tobin, T., and Brody, T. M., 1972, Rates of dissociation of enzyme—ouabain complexes and Kos values in (Na * + K *) adenosine triphosphatase from different species, Biochem. Pharmacol. 21: 1553–1560.
Tobin, T., and Sen, A. K., 1970, Stability and ligand sensitivity of (3H)ouabain binding to (Na* + K“)-ATPase, Biochim. Biophys. Acta 198: 120–131.
Tobin, T., Henderson, R., and Sen. A. K., 1972, Species and tissue differences in the rate of dissociation of ouabain from (Na* + K’)-ATPase, Biochim. Biophys. Acta 274: 551–555.
Tobin, T., Akera, T., Baskin, S. I., and Brody, T. M., 1973, Calcium ion and sodium-and potassium-dependent adenosine triphosphatase: Its mechanism of inhibition and identification of the El-P intermediate, Mol. Pharmacol. 9: 336–349.
Tobin, T., Akera, T., and Brody, T. M., 1974, Studies on the two phosphoenzyme conformations of Na* + K* ATPase, Ann. N. Y. Acad. Sci. 242: 120–132.
Tonomura, Y., and Fukushima, Y., 1974, Kinetic properties of phosphorylated intermediates in the reaction of Na’,K*-ATPase, Ann. N. Y. Acad. Sci. 242: 92–105.
Tosteson, D. C., 1963, Active transport, genetics, and cellular evolution, Fed. Proc. 22: 19–26.
Van Groningen, H. E. M., and Slater, E. C., 1963, The effect of oligomycin on the (Na+ + K’)-activated Mg-ATPase of brain microsomes and erythrocyte membrane, Biochim. Biophys. Acta 73: 527–530.
Van Winkle, W. B., Lane, L. K., and Schwartz, A., 1976, The subunit fine structure of isolated, purified Na’,K’-adenosine triphosphatase, Exp. Cell Rev. 100: 291–296.
Vogel, F., Meyer, H. W., Grosse, R., and Repke, K. R. H., 1977, Electron microscopic visualization of the arrangement of the two protein compounds of (Na’ + K+)-ATPase, Biochim. Biophys. Acta 470: 497–502.
Wallick, E. T., and Schwartz, A., 1974, Thermodynamics of the rate of binding of ouabain to the sodium, potassium adenosine triphosphatase, J. Biol. Chem. 249: 5141–5147.
Whitmer, K. R., Epps, D., and Schwartz, A., 1983, An endogenous inhibitor of Na+,K+-ATPase: “Endodigin,” Curr. Top. Membr. Trans. 19 in press.
Whittam, R., 1962, The asymmetrical stimulation of a membrane adenosine triphosphatase in relation to active cation transport, Biochem. J. 84: 110–118.
Whittam, R., Wheeler, K. P., and Blake, A., 1964, Oligomycin and active transport reactions in cell membranes, Nature 203: 720–724.
Wildes, R. A., Evans, H. J., and Chiu, J., 1973, Effects of cations on the adenosine diphosphate—adenosine triphosphate exchange reaction catalyzed by rat brain microsomes, Biochim. Biophys. Acta 307: 162–168.
Wilson, W. E., Sivitz, W.I., and Hanna, L. T., 1970, Inhibition of calf brain membranal sodium-and potassium-dependent adenosine triphosphatase by cardioactive sterols. A binding site model, Mol. Pharmacol. 6: 449–459.
Winslow, J. W., 1981, The reaction of sulfhydryl groups of sodium and potassium ion-activated adenosine triphosphatase with N-ethylmaleimide. The relationship between ligand-dependent alterations of nucleophilicity and enzymatic conformational states, J. Biol. Chem. 256: 9522–9531.
Winter, C. G., and Moss, A. J., 1979, Ultracentrifugal analysis of the enzymatically active fragments produced by digitonin action on Na,K-ATPase, in: Na,K-ATPase: Structure and Kinetics (J. C. Skou and J. G. N?rby, eds.), Academic Press, London, pp. 25–32.
Woodger, J. H., 1924, A Textbook of Morphology and Physiology for Medical Students, Oxford University Press, Oxford.
Yamaguchi, M., and Post, R. L., 1982, Inhomogeneity of alpha subunits of (Na,K)ATPase from renal outer medulla, Fed. Proc. 41: 673.
Yamaguchi, M., and Tonomura, Y., 1977, Kinetic studies on the ADP—ATP exchange reaction catalyzed by Na’,K+-dependent ATPase. Evidence for the K. S. T. mechanism with two enzyme—ATP complexes and two phosphorylated intermediates of high-energy type, J. Biochem. (Tokyo) 81: 249–260.
Yamaguchi, M., and Tonomura, Y., 1979, Simultaneous binding of three Na+ and two K + ions to Na’,K+-dependent ATPase and changes in its affinities for the ions induced by the formation of a phosphorylated intermediate, J. Biochem. (Tokyo) 86: 509–523.
Yamaguchi, M., and Tonomura, Y., 1980a, Binding of monovalent cations to Na+,K +-dependent ATPase purified from porcine kidney. I. Simultaneous binding of three sodium and two potassium or rubidium ions to the enzyme, J. Biochem. (Tokyo) 88: 1365–1375.
Yamaguchi, M., and Tonomura, Y., 1980b, Binding of monovalent cations to Na+,K+-dependent ATPase purified from porcine kidney. II. Acceleration of transition from a K+-bound form to a Na’-bound form by binding of ATP to a regulatory site of the enzyme, J. Biochem. (Tokyo) 88: 1377–1385.
Yamaguchi, M., and Tonomura, Y., 1980c, Binding of monovalent cations to Na’,K+-dependent ATPase purified from porcine kidney. III. Marked changes in affinities for monovalent cations induced by formation of an ADP-insensitive but not an ADP-sensitive phosphoenzyme, J. Biochem. (Tokyo) 88: 1387–1397.
Yoda, A., and Yoda, S., 1982a, Formation of ADP-sensitive phosphorylated intermediate in the electric eel Na,K-ATPase preparation, Mol. Pharmacol. 22: 693–699.
Yoda, A., and Yoda, S., 1982b, Interaction between ouabain and the phosphorylated intermediate of Na,KATPase, Mol. Pharmacol. 22: 700–705.
Zambrano, F., Morales, M., Fuentes, N., and Rojas, M., 1981, Sulfatide role in the sodium pump, J. Membr. Biol. 63: 71–75.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1985 Plenum Press, New York
About this chapter
Cite this chapter
Glynn, I.M. (1985). The Na+, K+-Transporting Adenosine Triphosphatase. In: Martonosi, A.N. (eds) The Enzymes of Biological Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4601-2_2
Download citation
DOI: https://doi.org/10.1007/978-1-4684-4601-2_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-4603-6
Online ISBN: 978-1-4684-4601-2
eBook Packages: Springer Book Archive