Skip to main content
SpringerLink
Log in

Effects of Cardiac Glycosides on Na+, K+-ATPase

  • Chapter
Cardiac Glycosides

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 56 / 1))

Abstract

The inhibitory action of cardiac glycosides on active Na + and K + transport across the cell membrane had been demonstrated in the early 1950 s (Schatzmann, 1953; see Hajdu and Leonard, 1959). Thus, with the discovery of Na +, K+-ATPase (Skou, 1957; Hess and Pope, 1957), the effect of these glycosides on the enzyme activity was examined and a specific inhibition was observed (Post et al., 1960; Skou, 1960; see Fig. 1). The interaction of cardiac glycosides with the enzyme, and its possible relationship to the pharmacologic or toxic actions of these agents have been extensively studied during the last two decades (see the following review articles: Glynn, 1964; Repke, 1964, 1965; Skou, 1965; Langer, 1971, 1972a; Lee and Klaus, 1971; Smith and Haber, 1973; Schwartz et al., 1975; Akera and Brody, 1976, 1977; Akera, 1977; Brody and Akera, 1977; Langer, 1977; Okita, 1977; Wallick et al., 1977).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Ahmed, K., Judah, J.D.: On the action of strophanthin G. Can. J. Biochem. 43, 877–880 (1965)

    CAS  Google Scholar 

  • Akera, T.: Quantitative aspects of the interaction between ouabain and (Na ++K+)-activated ATPase in vitro. Biochim. Biophys. Acta (Amst.) 249, 53–62 (1971)

    CAS  Google Scholar 

  • Akera, T.: Membrane adenosinetriphosphatase: A digitalis receptor? Science 198, 569–574 (1977)

    PubMed  CAS  Google Scholar 

  • Akera, T., Brody, T.M.: Membrane adenosine triphosphatase: The effect of potassium on the formation and dissociation of the ouabain-enzyme complex. J. Pharmacol. Exp. Ther. 176, 545–557 (1971)

    PubMed  CAS  Google Scholar 

  • Akera, T., Brody, T.M.: Inotropic action of digitalis and ion transport. Life Sci. 18, 135–142 (1976)

    PubMed  CAS  Google Scholar 

  • Akera, T., Brody, T.M.: The role of Na+, K+-ATPase in the inotropic action of digitalis. Pharmacol. Rev. 29, 187–220 (1977)

    CAS  Google Scholar 

  • Akera, T., Cheng, V.-J.K.: A simple method for the determination of affinity and binding site concentration in receptor binding studies. Biochim. Biophys. Acta (Amst.) 470, 412423 (1977)

    Google Scholar 

  • Akera, T., Larsen, F.S., Brody, T.M.: The effect of ouabain on sodium-and potassium-activated adenosine triphosphatase from the hearts of several mammalian species. J. Pharmacol. Exp. Ther. 170, 17–26 (1969)

    PubMed  CAS  Google Scholar 

  • Akera, T., Larsen, F.S., Brody, T.M.: Correlation of cardiac sodium-and potassium-activated adenosine triphosphatase activity with ouabain-induced inotropic stimulation. J. Pharmacol. Exp. Ther. 173, 145–151 (1970)

    PubMed  CAS  Google Scholar 

  • Akera, T., Hook, J.B., Tobin, T., Brody, T.M.: Cardiac glycoside sensitivity of (Na + K+)-activated ATPase in new-born rats. Res. Commun. Chem. Pathol. Pharmacol. 4, 699–706 (1972)

    PubMed  CAS  Google Scholar 

  • Akera, T., Baskin, S.I., Tobin, T., Brody, T.M.: Ouabain: Temporal relationship between the inotropic effect and the in vitrobinding to, and dissociation from, (Na ++K+)-activated ATPase. Naunyn-Schmiedebergs Arch. Pharmacol. 277, 151–162 (1973)

    CAS  Google Scholar 

  • Akera, T., Brody, T.M., So, R.H.-M., Tobin, T., Baskin, S.I.: Factors and agents that in-fluence cardiac glycoside-Na+, K +-ATPase interaction. Ann. N.Y. Acad. Sci. 242, 617–634 (1974a)

    CAS  Google Scholar 

  • Akera, T., Tobin, T., Gatti, A., Shieh, I.-S., Brody, T.M.: Effect of potassium on the conformational state of the complex of ouabain with sodium-and potassium-dependent adenosine triphosphatase. Mol. Pharmacol. 10, 509–518 (1974b)

    CAS  Google Scholar 

  • Akera, T., Bennet, R.T., Olgaard, M.K., Brody, T.M.: Cardiac Na+, K+-adenosine triphosphatase inhibition by ouabain and myocardial sodium: A computer simulation. J. Pharmacol. Exp. Ther. 199, 287–297 (1976a)

    CAS  Google Scholar 

  • Akera, T., Ku, D., Tobin, T., Brody, T.M.: The complexes of ouabain with sodium and potassium activated adenosine triphosphatase formed with various ligands: Relationship to the complex formed in the beating heart. Mol. Pharmacol. 12, 101–114 (1976b)

    CAS  Google Scholar 

  • Akera, T., Ku, D., Brody, T.M.: Lack of effect on brain stem and cerebral cortex Na+, K+-ATPase during heart block produced by chronic digoxin treatment. Eur. J. Pharmacol. 45, 243–249 (1977a)

    CAS  Google Scholar 

  • Akera, T., Olgaard, M.K., Temma, K., Brody, T.M.: Development of the positive inotropic action of ouabain: Effects of transmembrane sodium movement. J. Pharmacol. Exp. Ther. 203, 675–684 (1977b)

    CAS  Google Scholar 

  • Akera, T., Temma, K., Wiest, S.A., Brody, T.M.: Reduction of the equilibrium binding of cardiac glycosides and related compounds to Na+, K+-ATPase as a possible mechanism for the potassium-induced reversal of their toxicity. Naunyn-Schmiedebergs Arch. Pharmacol. 304, 157–165 (1978)

    CAS  Google Scholar 

  • Akera, T., Brody, T.M., Wiest, S.A.: Saturable adenosine 5’-triphosphate-independent binding of (3H)-ouabain to brain and cardiac tissue in vitro. Brit. J. Pharmacol. 65, 403–409 (1979a)

    CAS  Google Scholar 

  • Akera, T., Choi, Y.R., Yamamoto, S.: Potassium-induced changes in Na, K-ATPase: Influences on the interaction between cardiac glycosides and enzyme. In: Na, K-ATPase: Structure and Kinetics. Skou, J.C., Nerby, J.G. (eds.), pp. 405–420. London: Academic Press 1979b

    Google Scholar 

  • Akera, T., Wiest, S.A., Brody, T.M.: Differential effect of potassium on the action of di- goxin and digoxigenin in guinea-pig heart. Eur. J. Pharmacol. 57, 343–351 (1979c)

    CAS  Google Scholar 

  • Akera, T., Yamamoto, S., Chubb, J., McNish, R., Brody, T.M.: Biochemical basis for the low sensitivity of the rat heart to digitalis. Naunyn-Schmiedebergs Arch. Pharmacol. 308, 81–88 (1979d)

    CAS  Google Scholar 

  • Albers, R.W., Koval, G.J., Siegel, G.J.: Studies on the interaction of ouabain and other cardioactive steroids with sodium-potassium-activated adenosine triphosphatase. Mol. Pharmacol. 4, 324–336 (1968)

    CAS  Google Scholar 

  • Allen, D.G., Blinks, J R • Calcium transients in aequorin-injected frog cardiac muscle. Nature (Lond.) 273, 509–513 (1978)

    CAS  Google Scholar 

  • Allen, J.C., Schwartz, A.: A possible biochemical explanation for the insensitivity of the rat to cardiac glycosides. J. Pharmacol. Exp. Ther. 168, 42–46 (1969)

    PubMed  CAS  Google Scholar 

  • Allen, J.C., Schwartz, A.: Effects of potassium, temperature, and time on ouabain interaction with the cardiac Na+, K+-ATPase: Further evidence supporting an allosteric site. J. Mol. Cell. Cardiol. 1, 39–45 (1970)

    PubMed  CAS  Google Scholar 

  • Allen, J.C., Schwartz, A.: Human cardiac Na+, K+-ATPase: A pharmacologic receptor for cardiac glycosides. Cardiovasc. Res. Center Bull. 10, 133–141 (1972)

    Google Scholar 

  • Allen, J.C., Besch, H.R. Jr., Glick, G., Schwartz, A.: The binding of tritiated ouabain to sodium-and potassium-activated adenosine triphosphatase and cardiac relaxing system of perfused dog heart. Mol. Pharmacol. 6, 441–443 (1970a)

    CAS  Google Scholar 

  • Allen, J.C., Lindenmayer, G.E., Schwartz, A.: An allosteric explanation for ouabain-induced time-dependent inhibition of sodium, potassium-adenosine triphosphatase. Arch. Biochem. Biophys. 141, 322–328 (1970b)

    CAS  Google Scholar 

  • Allen, J.C., Harris, R.A., Schwartz, A.: The nature of the transport ATPase-digitalis complex. I. Formation and reversibility in the presence and absence of a phosphorylated enzyme. Biochem. Biophys. Res. Commun. 42, 366–370 (1971a)

    CAS  Google Scholar 

  • Allen, J.C., Harris, R.A., Schwartz, A.: The nature of the transport ATPase-digitalis complex. II. Some species differences and ouabain “exchange” characteristics. J. Mol. Cell. Cardiol. 3, 297–300 (1971b)

    CAS  Google Scholar 

  • Allen, J.C., Martines-Maldonado, M., Eknoyan, G., Suki, W.N., Schwartz, A.: Relation between digitalis binding in vivo and inhibition of sodium, potassium-adenosine triphosphatase in canine kidney. Biochem. Pharmacol. 20, 73–80 (1971c)

    CAS  Google Scholar 

  • Allen, J.C., Entman, M.L., Schwartz, A.: The nature of the transport adenosine triphos-phatase-digitalis complex. VIII. The relationship between in vivo-formed (3H-ouabainNa+, K +-adenosine triphosphatase) complex and ouabain-induced positive inotropism. J. Pharmacol. Exp. Ther. 192, 105–112 (1975)

    PubMed  CAS  Google Scholar 

  • Asano, Y., Liberman, U.A., Edelman, I.S.: Thyroid thermogenesis: Relationships between Na+-dependent respiration and Na +K+-adenosine triphosphatase activity in rat skeletal muscle. J. Clin. Invest. 57, 368–379 (1976)

    PubMed  CAS  Google Scholar 

  • Ash, A.S.F., Schwartz, A.: Sodium-plus-potassium ion-activated adenosine triphosphatase in a heavy-membrane fraction isolated from rat skeletal muscle. Biochem. J. 118, 20P–21P (1970)

    Google Scholar 

  • Baker, P.F., Willis, J.S.: On the number of sodium pumping sites in cell membranes. Biochim. Biophys. Acta (Amst.) 183, 646–649 (1969)

    CAS  Google Scholar 

  • Baker, P.F., Willis, J.S.: Potassium ions and the binding of cardiac glycosides to mammalian cells. Nature (Lond.) 226, 521–523 (1970)

    CAS  Google Scholar 

  • Baker, P.F., Willis, J S • Inhibition of the sodium pump in squid giant axons by cardiac glycosides: The dependence on extracellular ions and metabolism. J. Physiol. (Lond.) 224, 463–475 (1972)

    CAS  Google Scholar 

  • Balasubramanian, V., McNamara, D.B., Singh, J.N., Dhalla, N.S.: Biochemical basis of heart function. X. Reduction in the Na+-K+-stimulated ATPase activity in failing rat heart due to hypoxia. Can. J. Physiol. Pharmacol. 51, 504–510 (1973)

    PubMed  CAS  Google Scholar 

  • Barnett, R.E.: Effect of monovalent cations on the ouabain inhibition of the sodium and potassium ion activated adenosine triphosphatase. Biochemistry 9, 4644–4648 (1970)

    PubMed  CAS  Google Scholar 

  • Baskin, S.I., Akera, T., Puckett, C.R., Brody, S.L., Brody, T.M.: Effect of potassium canrenoate on cardiac functions and (Na+ + K +)-activated ATPase. Proc. Soc. Exp. Biol. Med. 143, 495–498 (1973)

    PubMed  CAS  Google Scholar 

  • Beauge, L.A., Adragna, N.: The kinetics of ouabain inhibition and the partition of rubidium influx in human red blood cells. J. Gen. Physiol. 57, 576–592 (1971)

    PubMed  CAS  Google Scholar 

  • Beard, N.A., Rouse, W., Somerville, A.R.: Cardiotonic steroids: Correlation of sodium-potassium adenosine triphosphate inhibition and ion transport in vitro with inotropic activity and toxicity in dogs. Br. J. Pharmacol. 54, 65–74 (1975)

    PubMed  CAS  Google Scholar 

  • Beller, G.A., Conroy, J., Smith, T.W.: Ischemia-induced alterations in myocardial (Na++K+)-ATPase and cardiac glycoside binding. J. Clin. Invest. 57, 341–350 (1976)

    PubMed  CAS  Google Scholar 

  • Bentfeld, M., Lüllmann, H., Peters, T., Proppe, D.: Interdependence of ion transport and the action of ouabain in heart muscle. Brit. J. Pharmacol. 61, 19–27 (1977)

    CAS  Google Scholar 

  • Bergelson, L.D., Barsukov, L.I.: Topological asymmetry of phospholipids in membranes. Science 197, 224–230 (1977)

    PubMed  CAS  Google Scholar 

  • Besch, H.R. Jr., Schwartz, A.: On the mechanism of action of digitalis. J. Mol. Cell. Cardiol. 1, 195–199 (1970)

    Google Scholar 

  • Besch, H.R. Jr., Allen, J.C., Glick, G., Schwartz, A.: Correlation between the inotropic action of ouabain and its effects on subcellular enzyme systems from canine myocardium. J. Pharmacol. Exp. Ther. 171, 1–12 (1970)

    PubMed  CAS  Google Scholar 

  • Besch, H.R. Jr., Jones, L.R., Watanabe, A.M.: Intact vesicles of canine cardiac sarcolemma: Evidence from vectorial properties of Na+, K+-ATPase. Circ. Res. 39, 586–595 (1976)

    CAS  Google Scholar 

  • Blaustein, M.P.: Sodium-calcium exchange and the regulation of cell calcium in muscle fi-bers. Physiologist 19, 525–540 (1976)

    PubMed  CAS  Google Scholar 

  • Blood, B.E., Noble, D.: Glycoside induced inotropism of the heart — more than one mechanism? J. Physiol. (Lond.) 266, 76P–78P (1977)

    Google Scholar 

  • Bluschke, V., Bonn, R., Greeff, K.: Increase in the (Na+ + K +)-ATPase activity in heart muscle after chronic treatment with digitoxin or potassium defficient diet. Europ. J. Pharmacol. 37, 189–191 (1976)

    CAS  Google Scholar 

  • Bodemann, H.H., Hoffman, J.F.: 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 (1976a)

    CAS  Google Scholar 

  • Bodemann, H.H., Hoffman, J.F.: 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 (1976b)

    CAS  Google Scholar 

  • Bonn, R., Greeff, K.: The effect of chronic administration of digitoxin on the activity of the myocardial (Na + K)-ATPase in guinea-pigs. Arch. Int. Pharmacodyn. 233, 53–64 (1978)

    CAS  Google Scholar 

  • Borsch-Galetke, E., Dransfeld, H., Greeff, K.: Specific activity and sensitivity of strophanthin of the Na++K+-activated ATPase in rats and guinea-pigs with hypoadrenalism. Naunyn-Schmiedebergs Arch. Pharmacol. 274, 74–80 (1972)

    CAS  Google Scholar 

  • Böttcher, H., Fischer, K., Proppe, D.: Untersuchungen über die Wirkung von Digoxigeninmono-, -bis-and -tridigitoxosid am Herz-Lungen-Präparat der Katze. Basic. Res. Cardiol. 70, 279–291 (1975)

    Google Scholar 

  • Boutagy, J., Gelbart, A., Thomas, R.: Cardenolide analogues. IV. Inhibition of Na+, K+-ATPase. Aust. J. Pharmaceut. Sci. NS2, 41–46 (1973)

    Google Scholar 

  • Brennan, F.J., McCans, J.L., Chiong, M.A., Parker, J.O.: Effects of ouabain on myocardial potassium and sodium balance in man. Circulation 45, 107–113 (1972)

    PubMed  CAS  Google Scholar 

  • Brody, T.M., Akera, T.: Relations among Na+, K+-ATPase activity, sodium pump activity, transmembrane sodium movement, and cardiac contractility. Fed. Proc. 36, 2219–2224 (1977)

    CAS  Google Scholar 

  • Brown, T.E., Acheson, G.H., Grupp, G.: The saturated-lactone glycoside dihydro-ouabain: Effects on potassium balance of the dog heart. J. Pharmacol. Exp. Ther. 136, 107–113 (1962)

    PubMed  CAS  Google Scholar 

  • Byrne, J.E., Dresel, P.E.: The effect of temperature and calcium concentration on the action of ouabain in quiescent rabbit atria. J. Pharmacol. Exp. Ther. 166, 354–363 (1969)

    PubMed  CAS  Google Scholar 

  • Caldwell, R.W., Nash, C.B.: Comparison of effects of aminosugar cardiac glycosides with ouabain and digoxin on Na+, K +-adenosine triphosphatase and cardiac contractile force. J. Pharmacol. Exp. Ther. 204, 141–148 (1977)

    Google Scholar 

  • Chang, C.C., Trosko, J.E., Akera, T.: Characterization of ultraviolet light-induced ouabainresistant mutations in Chinese hamster cells. Mutation Res. 51, 85–98 (1978)

    PubMed  CAS  Google Scholar 

  • Charnock, J.S., Potter, H.A.: The effect of Mg’ and ouabain on the incorporation of P32 from ATV’ into Na+- and K+-activated adenosine triphosphatase. Arch. Biochem. Biophys. 134, 42–47 (1969)

    CAS  Google Scholar 

  • Charnock, J.S., Rosenthal, A.S., Post, R.L.: Studies of the mechanism of cation transport. II. A phosphorylated intermediate in the cation stimulated enzymic hydrolysis of adenosine triphosphate. Aust. J. Exp. Biol. 41, 675–686 (1963)

    CAS  Google Scholar 

  • Charnock, J.S., Almeida, A.F., To, R.: Temperature-activity relationships of cation activation and ouabain inhibition of (Na+ +K+)-ATPase. Arch. Biochem. Biophys. 167, 480487 (1975)

    Google Scholar 

  • Charnock, J.S., Simonson, L.P., Almeida, A.F.: Variation in sensitivity of the cardiac glycoside receptor characteristics of (Na + + K+)-ATPase to lipolysis and temperature. Biochim. Biophys. Acta (Amst.) 465, 77–92 (1977)

    CAS  Google Scholar 

  • Choi, Y.R., Akera, T.: Kinetic studies on the interaction between ouabain and (Na +, K+)-ATPase. Biochim. Biophys. Acta (Amst.) 481, 648–659 (1977)

    CAS  Google Scholar 

  • Choi, Y.R., Akera, T.: Membrane (Na + + K +)-ATPase of canine brain, heart, and kidney: Tissue dependent differences in kinetic properties and the influence of purification procedures. Biochim Biophys. Acta (Amst.) 508, 313–327 (1978)

    CAS  Google Scholar 

  • Clark, A.F., Swanson, P.D., Stahl, W.L.: Increase in dissociation rate constants of cardiotonic steroid-brain (Na + + K+)-ATPase complexes by reduction of unsaturated lactone. J. Biol. Chem. 250, 9355–9359 (1975)

    PubMed  CAS  Google Scholar 

  • Clausen, T., Hansen, O.: Ouabain binding and Na + -K + transport in rat muscle cells and adipocytes. Biochim. Biophys. Acta (Amst.) 345, 387–404 (1974)

    CAS  Google Scholar 

  • Cohen, I., Daut, J., Noble, D.: An analysis of the actions of low concentrations of ouabain on membrane currents in Purkinje fibres. J. Physiol. (Lond.) 260, 75–103 (1976)

    CAS  Google Scholar 

  • Curfman, G.D., Crowley, T.J., Smith, T.W.: Thyroid-induced alterations in myocardial sodium-and potassium-activated adenosine triphosphatase, monovalent cation active transport, and cardiac glycoside binding. J. Clin. Invest. 59, 586–590 (1977)

    PubMed  CAS  Google Scholar 

  • DePont, J.J.H.H.M., Bonting, S.L.: The role of phospholipids in Na-K-ATPase. In: Bazan, N.G., Brenner, R.R., Guisto, N.M. (eds.). Function and biosynthesis of lipids, pp. 219224. New York: Plenum Publ. Corp. 1977

    Google Scholar 

  • DePover, A., Godfraind, T.: Sensitivity to cardiac glycosides of (Na + K) ATPase prepared from human heart, guinea-pig heart, and guinea-pig brain. Arch. Int. Pharmacodyn. Ther. 221, 339–341 (1976)

    CAS  Google Scholar 

  • Dhalla, N.S., Singh, J.N., Fedelesova, M., Balasubramanian, V., McNamara, D.B.: Biochemical basis of heart function. XII. Sodium-potassium stimulated adenosine triphosphatase activity in the perfused heart made to fail by substrate-lack. Cardiovasc. Res. 8, 227–236 (1974)

    CAS  Google Scholar 

  • Dransfeld, H., Greeff, K., Berger, H., Cautius, V.: Die verschiedene Empfindlichkeit der Na++K+-aktivierten ATPase des Herz-and Skeletmuskels gegen k-Strophanthin. Naunyn-Schmiedebergs Arch. Pharmacol. 254, 225–234 (1966)

    CAS  Google Scholar 

  • Dransfeld, H., Greeff, K., Schorn, A., Ting, B.T.: Calcium uptake in mitochondria and vesicles of heart and skeletal muscle in presence of potassium, sodium, k-strophanthin, and pentobarbital. Biochem. Pharmacol. 18, 1335–1345 (1969)

    CAS  Google Scholar 

  • Dudding, W.F., Winter, C.G.: On the reaction sequence of the K+-dependent acetyl phos-phatase activity of the Na+ pump. Biochim. Biophys. Acta (Amst.) 241, 650–660 (1971)

    CAS  Google Scholar 

  • Dunham, E.T., Glynn, I.M.: Adenosine triphosphatase activity and the active movements of alkali metal ions. J. Physiol. (Lond.) 156, 274–293 (1961)

    CAS  Google Scholar 

  • Dutta, S., Goswami, S., Datta, D.K., Lindower, J.O., Marks, B.H.: The uptake and binding of six radiolabeled cardiac glycosides by guinea-pig hearts and by isolated sarcoplasmic reticulum. J. Pharmacol. Exp. Ther. 164, 10–21 (1968)

    PubMed  CAS  Google Scholar 

  • Ebner, F., Reiter, M.: The dependence on contraction frequency of the positive inotropic effect of dihydro-ouabain. Naunyn-Schmiedebergs Arch. Pharmacol. 300, 1–9 (1977)

    CAS  Google Scholar 

  • Edelman, I.S.: Thyroidal regulation of renal energy metabolism and (Na+ + K +)-activated adenosine triphosphatase activity. Med. Clin. N. Amer. 59, 605–614 (1975)

    PubMed  CAS  Google Scholar 

  • Entman, M.L., Allen, J.C., Schwartz, A.: Calcium-ouabain interaction in a “microsomal” membrane fraction containing Na, K+-ATPase activity and calcium binding activity. J. Mol. Cell. Cardiol. 4, 435–441 (1972)

    PubMed  CAS  Google Scholar 

  • Erdmann, E., Hasse, W.: Quantitative aspects of ouabain binding to human erythrocyte and cardiac membranes. J. Physiol. (Lond.) 251, 671–682 (1975)

    CAS  Google Scholar 

  • Erdmann, E., Schoner, W.: Ouabain-receptor interactions in (Na+K+)-ATPase preparations from different tissues and species. Determination of kinetic constants and dissociation constants. Biochim. Biophys. Acta (Amst.) 307, 386–398 (1973a)

    CAS  Google Scholar 

  • Erdmann, E., Schoner, W.: Ouabain-receptor interactions in (Na+ + K +)-ATPase preparations. II. Effects of cations and nucleotides on rate constants and dissociation constants. Biochim. Biophys. Acta (Amst.) 330, 302–315 (1973b)

    CAS  Google Scholar 

  • Erdmann, E., Schoner, W.: Ouabain-receptor interactions in (Na+ +K+)-ATPase preparations. III. On the stability of the ouabain receptor against physical treatment, hydrolases, and SH reagents. Biochim. Biophys. Acta (Amst.) 330, 316–324 (1973c)

    CAS  Google Scholar 

  • Erdmann, E., Schoner, W.: Ouabain-receptor intüractions 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 (1974a)

    CAS  Google Scholar 

  • Erdmann, E., Schoner, W.: Eigenschaften des Rezeptors für Herzglykoside. Klin. Wochenschr. 52, 705–718 (1974b)

    CAS  Google Scholar 

  • Erdmann, E., Bolte, H.-D., Luderitz, B.: The (Na+ + K +)-ATPase activity of guinea pig heart muscle in potassium deficiency. Arch. Biochem. Biophys. 145, 121–125 (1971)

    CAS  Google Scholar 

  • Erdmann, E., Bolte, H.-D., Schoner, W.: Cardiac glycoside receptor in potassium depletion. Recent Adv. in studies on cardiac structure and metabolism. Basic functions of cations in myocardial activity. Fleckenstein, A., Dhalla, N.S. (eds.), Vol. 5, pp. 351–358. Baltimore: University Park Press 1975

    Google Scholar 

  • Erdmann, E., Patzelt, R., Schoner, W.: The cardiac glycoside receptor: Its properties and its correlation to nucleotide binding sites, phosphointermediate, and (Na + + K +)- ATPase activity. Recent Adv. in studies on cardiac structure and metabolism. The Sarcolemma. Roy, P-E., Dhalla, N.S. (eds.), Vol. 9, pp. 329–335. Baltimore: University Park Press 1976a

    Google Scholar 

  • Erdmann, E., Philipp, G., Tanner, G.: Ouabain-receptor interactions in (Na + + K +)-ATPase preparations. A contribution to the problem of nonlinear Scatchard plots. Biochim. Biophys. Acta (Amst.) 455, 287–296 (1976b)

    CAS  Google Scholar 

  • Erlij, D., Elizalde, A.: Rapidly reversible inhibition of frog muscle sodium pump caused by cardiotonic steroids with modified lactone rings. Biochim. Biophys. Acta (Amst.) 345, 49–54 (1974)

    CAS  Google Scholar 

  • Flasch, H., Heinz, N.: Correlation between inhibition of (Na+ + K +)-membrane-ATPase and positive inotropic activity of cardenolides in isolated papillary muscles of guinea pig. Naunyn-Schmiedebergs Arch. Pharmacol. 304, 37–44 (1978)

    CAS  Google Scholar 

  • Forbush, B., Kaplan, J.H., Hoffman, J.F.: 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 (1978)

    PubMed  CAS  Google Scholar 

  • Fricke, U.: Lack of interaction of spironolactone with ouabain in guinea pig isolated heart muscle praparations. Eur. J. Pharmacol. 49, 363–371 (1978)

    PubMed  CAS  Google Scholar 

  • Fricke, U., Klaus, W.: Die Reversibilität der Wirkung von Digitoxin, Strophanthidin und Strophanthidin-3-bromazetat am Papillarmuskel und einer mikrosomalen Na+-K+-aktivierbaren ATPase des Meerschweinchens. Experientia 25, 685–686 (1969)

    PubMed  CAS  Google Scholar 

  • Fricke, U., Klaus, W.: Comparative studies of the influence of various K+ concentrations on the action of k-strophanthidin, digitoxin, and strophanthidin-3-bromoacetate on papillary muscle and on membrane-ATPase of guinea pig hearts. Eur. J. Pharmacol. 15, 1–7 (1971a)

    CAS  Google Scholar 

  • Fricke, U., Klaus, W.: Über die Wirkung von Strophanthidin-3-bromacetat am Papillarmuskel des Meerschweinchens. Naunyn-Schmiedebergs Arch. Pharmacol. 268, 192–199 (1971b)

    CAS  Google Scholar 

  • Fricke, U., Klaus, W.: Die Haftung verschiedener Cardenolide am Papillarmuskel und einer mikrosomalen ATPase des Meerschweinchenherzens. Naunyn-Schmiedebergs Arch. Pharmacol. 268, 200–209 (1971c)

    CAS  Google Scholar 

  • Fricke, U., Klaus, W.: Evidence for two different Na+-dependent (3H)-ouabain binding sites of a Na+-K+-ATPase of guinea-pig hearts. Brit. J. Pharmacol. 61, 423–428 (1977)

    CAS  Google Scholar 

  • Fricke, U., Klaus, W.: Sodium-dependent cardiac glycoside binding: Experimental evidence and hypothesis. Brit. J. Pharmacol. 62, 255–257 (1978)

    CAS  Google Scholar 

  • Fricke, U., Hollborn, U., Klaus, W.: Inotropic action, myocardial uptake, and subcellular distribution of ouabain, digoxin, and digitoxin in isolated rat hearts. Naunyn-Schmiedebergs Arch. Pharmacol. 288, 195–214 (1975)

    CAS  Google Scholar 

  • Fujino, S., Kawagishi, S., Eguchi, N., Tanaka, M.: Binding site of ouabain in cardiac muscle cell and its positive inotropic effect in cat. Jpn. J. Pharmacol. 21, 423–425 (1971)

    CAS  Google Scholar 

  • Gardner, J.D., Kiino, D.R.: Ouabain binding and cation transport in human erythrocytes. J. Clin. Invest. 52, 1845–1851 (1973)

    PubMed  CAS  Google Scholar 

  • Gervais, A., Lane, L.K., Anner, B.M., Lindenmayer, G.E., Schwartz, A.: A possible molecular mechanism of the action of digitalis. Ouabain action on calcium binding to sites associated with a purified sodium-potassium-activated adenosine triphosphatase from kidney. Circ. Res. 40, 8–14 (1977)

    CAS  Google Scholar 

  • Glitsch, H.G.: Hemmung der elektrogenen Na-Pumpe am Meerschweinchenvorhof durch Digitoxigenin. Pflügers Arch. 335, 243–251 (1972)

    PubMed  CAS  Google Scholar 

  • Glitsch, H.G.: An effect of the electrogenic sodium pump on the membrane potential in beating guinea-pig atria. Pflügers Arch. 344, 169–180 (1973)

    PubMed  CAS  Google Scholar 

  • Glynn, I.M.: The action of cardiac glycosides on ion movements. Pharmacol. Rev. 16, 381–407 (1964)

    CAS  Google Scholar 

  • Godfraind, T.: The therapeutic mode of action of cardiac glycosides. Arch. Int. Pharmacodyn. Ther. 206, 384–388 (1973)

    PubMed  CAS  Google Scholar 

  • Godfraind, T., Ghysel-Burton, J.: Binding sites related to ouabain-induced stimulation or inhibition of the sodium pump. Nature (Lond.) 265, 165–166 (1977)

    CAS  Google Scholar 

  • Goodman, S.L., Wheeler, K.P.: Ouabain binding to phospholipid-dependent adenosine triphosphatase. Biochem. J. 169, 313–320 (1977)

    Google Scholar 

  • Goldman, R.H., Coltart, D.J., Friedman, J.P., Nola, G.T., Berke, D.K., Schweizer, E., Harrison, D.C.: The inotropic effects of digoxin in hyperkalemia. Relation to (Na, K+)ATPase inhibition in the intact animal. Circulation 48, 830–838 (1973)

    PubMed  CAS  Google Scholar 

  • Goldman, R.H., Coltart, D.J., Schweizer, E., Snidow, G., Harrison, D.C.: Dose response in vivo to digoxin in nonno-and hyperkalaemia: Associated biochemical changes. Cardiovasc. Res. 9, 515–523 (1975)

    CAS  Google Scholar 

  • Grobecker, V.H., Piechowski, U., Greeff, K.: Die Wirkung des k-Strophanthins und Digitonins auf den lonentransport und die Membran-ATPase der Erythrocyten von Menschen, Meerschweinchen und Ratten. Med. Exp. 9, 273–282 (1963)

    CAS  Google Scholar 

  • Gubitz, R.H., Akera, T., Brody, T.M.: Control of brain slice respiration by (Na+ + K +)- activated adenosine triphosphatase and the effects of enzyme inhibitors. Biochim. Biophys. Acta (Amst.) 459, 263–277 (1977)

    CAS  Google Scholar 

  • Hajdu, S., Leonard, E.: The cellular basis of cardiac glycoside action. Pharmacol. Rev. 11, 173–209 (1959)

    CAS  Google Scholar 

  • Hall, R.J., Gelbart, A., Silverman, M., Goldman, R.H.: Studies on digitalis-induced arrhythmias in glucose-and insulin-induced hypokalemia. J. Pharmacol. Exp. Ther. 201, 711–722 (1977)

    PubMed  CAS  Google Scholar 

  • Hansen, O.: The relationship between g-strophanthin-binding capacity and ATPase activity in plasma-membrane fragments from ox brain. Biochim. Biophys. Acta (Amst.) 233, 122–132 (1971)

    CAS  Google Scholar 

  • Hansen, O.: Non-uniform populations of g-strophanthin binding sites of (Na ++K+)-activated ATPase: Apparent conversion to uniformity by K Biochim. Biophys. Acta (Amst.) 433, 383–392 (1976)

    CAS  Google Scholar 

  • Hansen, O.: The effect of sodium on inorganic phosphate-and paranitrophenyl phosphate-facilitated ouabain binding to (Na ++K+)-activated ATPase. Biochim Biophys. Acta (Amst.) 511, 10–22 (1978)

    CAS  Google Scholar 

  • Hansen, O., Jensen, J., Norby, J.G.: Mutual exclusion of ATP, ADP, and g-strophanthin binding to NaK-ATPase. Nature New Biol. 234, 122–124 (1971)

    PubMed  CAS  Google Scholar 

  • Harris, W.E., Swanson, P.D., Stahl, W.L.: Ouabain binding sites and the (Na+, K+)ATPase of brain microsomal membranes. Biochim. Biophys. Acta (Amst.) 298, 680–689 (1973)

    CAS  Google Scholar 

  • Haustein, K.-O.: Studies on cardioactive steroids. I. Structure-activity relationships on the isolated atrium. Pharmacology 11, 117–126 (1974)

    PubMed  CAS  Google Scholar 

  • Haustein, K.-O., Hauptmann, J.: Studies on cardioactive steroids. Pharmacology 11, 129138 (1974)

    Google Scholar 

  • Hegyvary, C.: Covalent labeling of the digitalis-binding component of plasma membranes. Mol. Pharmacol. 11, 588–594 (1975)

    CAS  Google Scholar 

  • Hegyvary, C.: Ouabain binding and phosphorylation of (Na ++K+)-ATPase treated with N-ethylmaleimide or oligomycin. Biochim. Biophys. Acta (Amst.) 422, 365–379 (1976)

    CAS  Google Scholar 

  • Hegyvary, C.: Alterations of cardiac NaK-ATPase by the thyroid state in the rat. Res. Commun. Chem. Path. Pharmacol. 17, 689–702 (1977)

    CAS  Google Scholar 

  • Hegyvary, C., Post, R.L.: Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase. J. Biol. Chem. 246, 5234–5240 (1971)

    PubMed  CAS  Google Scholar 

  • Heinen, E., Noack, E.: Effects of k-strophanthin and digitoxigenin on contractile force, calcium content and exchange in guinea-pig isolated atria. Naunyn-Schmiedebergs Arch. Pharmacol. 275, 359–371 (1972)

    CAS  Google Scholar 

  • Hess, H.H., Pope, A.: Effect of metal cations on adenosine triphosphatase activity of rat brain. Fed. Proc. 16, 196 (1957)

    Google Scholar 

  • Hilden, S., Rhee, H.M., Hokin, L.E.: Sodium transport by phospholipid vesicles containing purified sodium and potassium ion-activated adenosine triphosphatase. J. Biol. Chem. 249, 7432–7440 (1974)

    PubMed  CAS  Google Scholar 

  • Hoffman, J.F.: The red cell membrane and the transport of sodium and potassium. Am. J. Med. 41, 666–680 (1966)

    PubMed  CAS  Google Scholar 

  • Hoffman, J.F.: The interaction between tritiated ouabain and the Na-K pump in red blood cells. J. Gen. Physiol. 54, 343S–350S (1969)

    Google Scholar 

  • Hokin, L.E., Dahl, J.L., Deupree, J.D., Dixon, J.F., Hackney, J.F., Perdue, J.F.: Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. X. Purification of the enzyme from the rectal gland of Squalus acanthias. J. Biol. Chem. 248, 2593–2605 (1973)

    PubMed  CAS  Google Scholar 

  • Hougen, T.J., Smith, T.W Inhibition of myocardial monovalent cation active transport by subtoxic doses of ouabain in the dog. Circ. Res. 42, 856–863 (1978)

    CAS  Google Scholar 

  • Huang, W., Askari, A.: Transport ATPase of erythrocyte membrane: Sensitivities of Na, K+-ATPase and K+-phosphatase activities to ouabain. Arch. Biochem. Biophys. 175, 185–189 (1976)

    CAS  Google Scholar 

  • Inagaki, C., Lindenmayer, G.E., Schwartz, A.: Effects of sodium and potassium on binding of ouabain to the transport adenosine triphosphatase. J. Biol. Chem. 249, 5135–5140 (1974)

    PubMed  CAS  Google Scholar 

  • Jones, L.R., Besch, H.R. Jr., Watanabe, A.M.: Significance of a cardiac microsomal Na plus K+-stimulated ATPase apparently insensitive to ouabain. Fed. Proc. 35, 833 (1976)

    Google Scholar 

  • Jorgensen, P.L.: Purification of Nat, K+-ATPase: Active site determination and criteria of purity. Ann. N.Y. Acad. Sci. 242: 36–52 (1974)

    PubMed  CAS  Google Scholar 

  • Jorgensen, P.L.: Purification and characterization of (Nat, 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 (Amst.) 401, 399–415 (1975)

    CAS  Google Scholar 

  • Jorgensen, P.L., Skou, J.C.: Purification and characterization of (Na ++K+)-ATPase. I. The influence of detergents on the activity of (Na+ +K+)-ATPase in preparations from the outer medulla of rabbit kidney. Biochim. Biophys. Acta (Amst.) 233, 366–380 (1971)

    CAS  Google Scholar 

  • Jorgensen, P.L., Hansen, O., Glynn, I.M., Cavieres, J.D.: 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 (Amst.) 291, 795–800 (1973)

    CAS  Google Scholar 

  • Kim, N.D., Bailey, L.E., Dresel, P.E.: Correlation of the subcellular distribution of digoxin with the positive inotropic effect. J. Pharmacol. Exp. Ther. 181, 377–385 (1972)

    PubMed  CAS  Google Scholar 

  • Köhler, E., Greeff, K.: Der Einfluß des Blut-pH auf die Toxicität herzwirksamer Glycoside. Res. Exp. Med. 159, 65–74 (1972)

    Google Scholar 

  • Ku, D., Akera, T., Pew, C.L., Brody, T.M.: Cardiac glycosides: Correlation among Na+, K+-ATPase, sodium pump and contractility in the guinea pig heart. Naunyn-Schmiedebergs Arch. Pharmacol. 285, 185–200 (1974)

    CAS  Google Scholar 

  • Ku, D.D., Akera, T., Tobin, T., Brody, T.M.: Comparative species studies on the effect of monovalent cations and ouabain on cardiac Na, K+-ATPase and contractile force. J. Pharmacol. Exp. Ther. 197, 458–469 (1976)

    PubMed  CAS  Google Scholar 

  • Ku, D.D., Akera, T., Brody, T.M., Weaver, L.C.: Chronic digoxin treatment on canine myocardial Na+, K+-ATPase. Naunyn-Schmiedebergs Arch. Pharmacol. 301, 39–47 (1977)

    CAS  Google Scholar 

  • Kyte, J.: Phosphorylation of a purified (Na + + K +) adenosine triphosphatase. Biochem. Biophys. Res. Commun. 43, 1259–1265 (1971)

    CAS  Google Scholar 

  • Kyte, J.: The titration of the cardiac glycoside binding site of the (Na+ + K +)-adenosine triphosphatase. J. Biol. Chem. 247, 7634–7641 (1972)

    PubMed  CAS  Google Scholar 

  • Kyte, J.: The reactions of sodium and potassium ion-activated adenosine triphosphatase with specific antibodies. J. Biol. Chem. 249, 3652–3660 (1974)

    PubMed  CAS  Google Scholar 

  • Lane, L.K., Copenhaver, J.H. Jr., Lindenmayer, G.E., Schwartz, A.: 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 (1973)

    PubMed  CAS  Google Scholar 

  • Lane, L.K., Anner, B.M., Wallick, E.T., Ray, M.V., Schwartz, A.: Effect of phospholipase A treatment on the partial reactions of and ouabain binding to a purified sodium and potassium activated adenosine triphosphatase. Biochem. Pharmacol. 27, 225–231 (1977)

    Google Scholar 

  • Langer, G.A.: Ion fluxes in cardiac excitation and contraction and their relation to myocardial contractility. Physiol. Rev. 48, 708–757 (1968)

    CAS  Google Scholar 

  • Langer, G.A.: The intrinsic control of myocardial contraction–ionic factors. New Engl. J. Med. 285, 1065–1071 (1971)

    CAS  Google Scholar 

  • Langer, G.A.: Effects of digitalis on myocardial ionic exchange. Circulation 46, 180–187 (1972a)

    CAS  Google Scholar 

  • Langer, G.A.: Myocardial K+ loss and contraction frequency. J. Mol. Cell. Cardiol. 4, 85–86 (1972b)

    CAS  Google Scholar 

  • Langer, G.A.: Relationship between myocardial contractility and the effects of digitalis on ionic exchange. Fed. Proc. 36, 2231–2234 (1977)

    CAS  Google Scholar 

  • Langer, G.A., Serena, S.D.: Effects of strophanthidin upon contraction and ionic exchange in rabbit ventricular myocardium: Relative to control of active state. J. Mol. Cell. Cardiol. 1, 65–90 (1970)

    PubMed  CAS  Google Scholar 

  • Lee, C.O., Fozzard, H.A.: Activities of potassium and sodium ions in rabbit neart muscle. J. Gen. Physiol. 65, 695–708 (1975)

    PubMed  CAS  Google Scholar 

  • Lee, K.S., Klaus, W.: The subcellular basis for the mechanism of inotropic action of cardiac glycosides. Pharmacol. Rev. 23, 193–261 (1971)

    CAS  Google Scholar 

  • Lee, K.S., Yu, D.H.: A study of the sodium-and potassium-activated adenosinetriphosphatase activity of heart microsomal fraction. Biochem. Pharmacol. 12, 1253–1264 (1963)

    CAS  Google Scholar 

  • Lee, K.S., Shin, M.R., Kang, D.H., Chen, K.K.: Studies on the mechanism of cardiac glycoside action. Biochem. Pharmacol. 19, 1055–1069 (1970)

    CAS  Google Scholar 

  • Lelievre, L., Charlemagne, D., Paraf, A.: Plasma membrane studies on drug-sensitive and -resistant cell lines. II. Ouabain sensitivity of (Na + + K +)stimulated Mg’ -ATPase. Biochim. Biophys. Acta (Amst.) 455, 277–286 (1976)

    CAS  Google Scholar 

  • Lin, M.H., Akera, T.: Increased (Na+, K+)-ATPase concentrations in various tissues of rats caused by thyroid hormone treatment. J. Biol. Chem. 253, 723–726 (1978)

    PubMed  CAS  Google Scholar 

  • Lin, M.H., Romsos, D.R., Akera, T., Leveille, G.A.: Na+, K+-ATPase enzyme units in skeletal muscle from lean and obese mice. Biochem. Biophys. Res. Commun. 80, 398–404 (1978)

    CAS  Google Scholar 

  • Lindenmayer, G.E., Schwartz, A.: Conformational changes induced in Na+, K+-ATPase by ouabain through a K+-sensitive reaction: Kinetic and spectroscopic studies. Arch. Biochem. Biophys. 140, 371–378 (1970)

    CAS  Google Scholar 

  • Lindenmayer, G.E., Schwartz, A.: 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 (1973)

    PubMed  CAS  Google Scholar 

  • Lindenmayer, G.E., Laughter, A.H., Schwartz, A.: Incorporation of inorganic phosphate-32 into a Na+ + K+-ATPase preparation: Stimulation by ouabain. Arch. Biochem. Biophys. 127, 187–192 (1968)

    CAS  Google Scholar 

  • Lishko, V.K., Malysheva, M.K., Grevisirskaya, T.I.: The interaction of the (Na +, K+)-ATPase of erythrocyte ghosts with ouabain. Biochim. Biophys. Acta (Amst.) 288, 103–106 (1972)

    CAS  Google Scholar 

  • Lo, C.S., Edelman, I.S.: Effect of triiodothyronine on the synthesis and degradation of renal cortical (Na+ + K +)-adenosine triphosphatase. J. Biol. Chem. 251, 7834–7840 (1976)

    PubMed  CAS  Google Scholar 

  • Lo, C.S., August, T.R., Liberman, U.A., Edelman, I.S.: Dependence of renal (Na+ +K+)-adenosine triphosphatase activity on thyroid status. J. Biol. Chem. 251, 7826–7833 (1976)

    PubMed  CAS  Google Scholar 

  • Löhr, E., Makoski, H.B., Gobbeler, T., Strötges, M.W.: Beitrag zu der Membranpermeabilität von Cardiaca (g-Strophanthin, Digoxin, Oxyfedrin) auf Grund von Mikroautoradiographien am Meerschweinchenherzen. Arzneim. Forsch. (Drug Res.) 21, 921–927 (1971)

    Google Scholar 

  • Lüllmann, H., Peters, T.: Action of cardiac glycosides on the excitation-contraction coupling in heart muscle. Prog. Pharmacol. 2, 5–57 (1979)

    Google Scholar 

  • Lüllmann, H., Peters, T.: Studies on the site of action of cardiac glycosides. In: Digitalis. Storstein, O. (ed.), p. 125. Oslo: Gyldendal Norsk Forlag 1974

    Google Scholar 

  • Lüllmann, H., Peters, T.: On the sarcolemmal site of action of cardiac glycosides. Recent Adv. in studies on cardiac structure and metabolism. The sarcolemma. Roy, P.-E., Dhalla, N.S. (eds.), Vol. 9, pp. 311–328. Baltimore: University Park Press 1976

    Google Scholar 

  • Lüllmann, H., Peters, T., Preuner, J., Rüther, T.: Influence of ouabain and dihydroouabain on the circular dichroism of cardiac plasmalemmal microsomes. Naunyn-Schmiedebergs Arch. Pharmacol. 290, 1–19 (1975)

    Google Scholar 

  • Malur, J., Repke, K.R.H.: Modelluntersuchungen über die Beteiligung einer WasserstoffBrücken-Bindung an der Komplexbildung zwischen Cardenolidverbindungen and Na + K+-aktivierter, Mg’ -abhängiger Adenosintriphosphat-Phosphohydrolase. Acta Biol. Med. Ger. 24, K67—K72 (1970)

    Google Scholar 

  • Matsui, H., Schwartz, A.: Kinetic analysis of ouabain-K + and Na + interaction on a Na+, K+-dependent adenosinetriphosphatase from cardiac tissue. Biochem. Biophys. Res. Commun. 25, 147–152 (1966)

    CAS  Google Scholar 

  • Matsui, H., Schwartz, A.: Mechanism of cardiac glycoside inhibition of the (Na +-K +)-dependent ATPase from cardiac tissue. Biochim. Biophys. Acta (Amst.) 151, 655–663 (1968)

    CAS  Google Scholar 

  • Matsui, H., Hayashi, Y., Homareda, H., Kimimura, M.: Ouabain-sensitive 42K binding to Na +, K+-ATPase purified from canine kidney outer medulla. Biochem. Biophys. Res. Commun. 75, 373–380 (1977)

    CAS  Google Scholar 

  • Mayer, M., Avi-Dor, Y.: Fluorescence of 8-anilino-l-naphthalene-sulfonate bound to ox-brain Nat and K +-stimulated adenosine triphosphatase. Isr. J. Med. Sci. 6, 726–731 (1970)

    PubMed  CAS  Google Scholar 

  • McCans, J.L., Lane, L.K., Lindenmayer, G.E., Butler, V.P. Jr., Schwartz, A.: Effects of an antibody to a highly purified Na+, K+-ATPase from canine renal medulla: Separation of the “holoenzyme antibody” into catalytic and cardiac glycoside receptor-specific components. Proc. Natl. Acad. Sci. U.S.A. 71, 2449–2452 (1974)

    PubMed  CAS  Google Scholar 

  • Michael, L., Wallick, E.T., Schwartz, A.: Modification of (Na +, K+)-ATPase function by purified antibodies to the holoenzyme — effects on enzyme activity and 3H ouabain binding. J. Biol. Chem. 252, 8476–8480 (1977)

    PubMed  CAS  Google Scholar 

  • Michael, L., Pitts, B.J.R., Schwartz, A.: Is pump stimulation associated with positive inotropy of the heart? Science 200, 1287–1289 (1978)

    PubMed  CAS  Google Scholar 

  • Murthy, R.V., Kidwai, A.M., Daniel, E.E.: Dissociation of contractile effect and binding and inhibition of Na +-K +-adenosine triphosphatase by cardiac glycosides in rabbit myometrium. J. Pharmacol. Exp. Ther. 188, 575–581 (1974)

    PubMed  CAS  Google Scholar 

  • Nagai, K., Lindenmayer, G.E., Schwartz, A.: Direct evidence for the conformational nature of the Na, K -ATPase system: Fluorescence and circular dichroism studies. Arch. Biochem. Biophys. 139, 252–254 (1970)

    CAS  Google Scholar 

  • Nagatomo, T., Jarmakani, J.M., Philipson, K.D., Nakazawa, M.: Effect of anoxia on membrane-bound ATPase and K+-p-nitrophenyl phosphatase activities in rabbit heart. J. Mol. Cell. Cardiol. 10, 981–989 (1978)

    PubMed  CAS  Google Scholar 

  • Nâidoo, B.K., Witty, T.R., Remers, W.A., Besch, H.R. Jr.: Cardiotonic steroids: I Impor- tance of 14ß-hydroxy group in digitoxigenin. J. Pharm. Sci. 63, 1391–1394 (1974)

    PubMed  Google Scholar 

  • Nayler, W.G., Stone, J., Carson, V., Chipperfield, D.: Effect of ischemia on cardiac contractility and calcium exchangeability. J. Mol. Cell. Cardiol. 2, 125–143 (1971)

    PubMed  CAS  Google Scholar 

  • Okarma, T.B., Tramell, P., Kalman, S.M.: Inhibition of sodium-and potassium-dependent adenosine triphosphatase by digoxin covalently bound to sepharose. Mol. Pharmacol. 8, 476–480 (1972)

    CAS  Google Scholar 

  • Okita, G.T.: Dissociation of Na, K+-ATPase inhibition from digitalis inotropy. Fed. Proc. 36, 2225–2230 (1977)

    CAS  Google Scholar 

  • Okita, G.T., Richardson, F., Roth-Schechter, B.F.: Dissociation of the positive inotropic action of digitalis from inhibition of sodium-and potassium-activated adenosine triphosphatase. J. Pharmacol. Exp. Ther. 185, 1–11 (1973)

    PubMed  CAS  Google Scholar 

  • Park, M.K., Vincenzi, F.F.: Rate of onset of cardiotonic steroid-induced inotropism: Influence of temperature and beat interval. J. Pharmacol. Exp. Ther. 195, 140–150 (1975)

    PubMed  CAS  Google Scholar 

  • Perrone, J.R., Blostein, R.: Asymmetric interaction of inside-out and right-side-out erythrocyte membrane vesicles with ouabain. Biochim. Biophys. Acta (Amst.) 291, 680–689 (1973)

    CAS  Google Scholar 

  • Pert, C., Snyder, S.: Opiate receptor binding of agonists and antagonists affected differentially by sodium. Mol. Pharmacol. 10, 868–879 (1974)

    CAS  Google Scholar 

  • Peters, T., Raben, R.H., Wassermann, O.: Evidence for a dissociation between positive isotropic effect and inhibition of the Na +-K + -ATPase by ouabain, cassaine, and their alkylating derivatives. Eur. J. Pharmacol. 26, 166–174 (1974)

    PubMed  CAS  Google Scholar 

  • Pitts, B.J.R., Wallick, E.T., Van Winkle, W.B., Allen, J.C., Schwartz, A.: On the lack of isotropy of cardiac glycosides on skeletal muscle: A comparison of Na+, K +-ATPases from skeletal and cardiac muscle. Arch. Biochem. Biophys. 184, 431–440 (1977)

    CAS  Google Scholar 

  • Poole-Wilson, P.A., Langer, G.A.: Glycoside inotropy in the absence of an increase in potassium efflux in the rabbit heart. Circ. Res. 37, 390–395 (1975)

    CAS  Google Scholar 

  • Post, R.L., Merritt, C.R., Kinsolving, C.R., Albright, C.D.: Membrane adenosine triphosphatase as a participant in the active transport of sodium and potassium in the human erythrocyte. J. Biol. Chem. 235, 1796–1802 (1960)

    PubMed  CAS  Google Scholar 

  • Post, R.L., Kume, S., Tobin, T., Orcutt, B., Sen, A.K.: Flexibility of an active center in sodium-plus-potassium adenosine triphosphatase. J. Gen. Physiol. 54, 306S–326S (1969)

    Google Scholar 

  • Prindle, K.H. Jr., Skelton, C.L., Epstein, S.E., Marcus, F.I.: Influence of extracellular potassium concentration on myocardial uptake and inotropic effect of tritiated digoxin. Circ. Res. 28, 337–345 (1971)

    CAS  Google Scholar 

  • Repke, K.: Metabolism of cardiac glycosides. In: Proc. 1 st International Pharmacol. Meeting, vol. 3, pp. 47–73. Oxford: Pergamon Press 1963

    Google Scholar 

  • Repke, K.: Über den biochemischen Wirkungsmodus von Digitalis. Klin. Wochenschr. 42, 157–165 (1964)

    CAS  Google Scholar 

  • Repke, K.: Effect of digitalis on membrane adenosine triphosphatase of cardiac muscle. In: Drugs and enzymes. Proc. 2 nd International Pharmacol. Meeting, Prague. Brodie, B.B., Gillette, J. (eds.), vol. 4, pp. 65–87. Oxford: Pergamon, Prague: Chechoslovak Medical Press 1965

    Google Scholar 

  • Repke, K., Portius, H.J.: Über die Identität der Ionenpumpen-ATPase in der Zellmembran des Herzmuskels mit einem Digitalis-Rezeptorenzym. Experientia 19, 452–458 (1963)

    PubMed  CAS  Google Scholar 

  • Repke, K.R.H., Schön, R.: Flip-flop model of (NaK)-ATPase function. Acta Biol. Med. Germ. 31, K19—K39 (1973)

    Google Scholar 

  • Repke, K., Est, M., Portius, H.J.: Über die Ursache der Speciesunterschiede in der Digitalisempfindlichkeit. Biochem. Pharmacol. 14, 1785–1802 (1965)

    CAS  Google Scholar 

  • Reuter, H.: Exchange of calcium ions in the mammalian myocardium: Mechanisms and physiological significance. Circ. Res. 34, 599–605 (1974)

    Google Scholar 

  • Rhee, H.M., Dutta, S., Marks, B.H.: Cardiac NaK ATPase activity during positive inotro-pic and toxic action of ouabain. Eur. J. Pharmacol. 37, 141–153 (1976)

    PubMed  CAS  Google Scholar 

  • Ross, C.R., Pessah, N.I.: Reversible inhibition of (Nat +K+)-ATPase with a cardiac gly-coside. Eur. J. Pharmacol. 33, 223–226 (1975)

    PubMed  CAS  Google Scholar 

  • Roth-Schechter, B.F., Okita, G.T., Thomas, R.E., Richardson, F.F.: On the positive inotropic action of alkylating bromoacetates of strophanthidin and strophanthidol-(19-H3). J. Pharmacol. Exp. Ther. 171, 13–19 (1970)

    PubMed  CAS  Google Scholar 

  • Ruoho, A., Kyte, J.: Photoaffinity labeling of the ouabain-binding site on (Nat +K+)adenosinetriphosphatase. Proc. Natl. Acad. Sci. U.S.A. 71, 2352–2356 (1974)

    PubMed  CAS  Google Scholar 

  • Ruoho, A.E., Hokin, L.E., Hemingway, R.J., Kupchan, S.M.: Hellebrigenin 3-haloacetates: Potent site-directed alkylators of transport adenosinetriphosphatase. Science 159, 1354–1355 (1968)

    PubMed  CAS  Google Scholar 

  • Sachs, J.R.: Interaction of external K, Na, and cardioactive steroids with the Na-K pump of the human red blood cell. J. Gen. Physiol. 63, 123–143 (1974)

    PubMed  CAS  Google Scholar 

  • Schatzmann, H.J.: Herzglycoside als Hemmstoffe für den aktiven Kalium-und Natrium- transport durch die Erythrocytenmembran. Helv. Physiol. Acta 11, 346–354 (1953)

    CAS  Google Scholar 

  • Scholz, H.: Effect of a “therapeutic” concentration of digitoxigenine on myocardial potassium and sodium content in Ca-poor media. Naunyn-Schmiedebergs Arch. Pharmacol. 273, 434–437 (1972)

    CAS  Google Scholar 

  • Schön, R., Schönfeld, W., Repke, K.R.H.: Zur Charakterisierung des Ouabain-bindenden Konformationszustandes der (Nat +K+)-aktivierten ATPase. Acta Biol. Med. Germ. 24, K61 - K65 (1970)

    Google Scholar 

  • Schön, R., Schönfeld, W., Menke, K.-H., Repke, K.R.H.: Mechanism and role of Na+/ Ca’ competition in (NaK)-ATPase. Acta Biol. Med. Germ. 29, 643–659 (1972)

    Google Scholar 

  • Schönfeld, W., Schön, R., Menke, K.-H., Repke, K.R.H.: Identification of conformational states of transport ATPase by kinetic analysis of ouabain binding. Acta Biol. Med. Germ. 28, 935–956 (1972)

    Google Scholar 

  • Schuurmans Stekhoven, F.M.A.H., DePont, J.J.H.H.M., Bonting, S.L.: Studies on (Na++K+)-activated ATPase. XXXVII. Stabilization by cations of the enzyme-ouabain complex formed with Mg’ and inorganic phosphate. Biochim Biophys. Acta (Amst.) 419, 137–149 (1976)

    CAS  Google Scholar 

  • Schwartz, A.: Is the cell membrane Na+, K +-ATPase enzyme system the pharmacological receptor for digitalis? Circ. Res. 39, 2–7 (1976)

    CAS  Google Scholar 

  • Schwartz, A., Matsui, H., Laughter, A.H.: Tritiated digoxin binding to (Na + + K +)-acti- vated adenosine triphosphatase: Possible allosteric site. Science 160, 323–325 (1968)

    PubMed  CAS  Google Scholar 

  • Schwartz, A., Allen, J.C., Harigaya, S.: Possible involvement of cardiac Na +, K + -adenosine triphosphatase in the mechanism of action of cardiac glycosides. J. Pharmacol. Exp. Ther. 168, 31–41 (1969)

    PubMed  CAS  Google Scholar 

  • Schwartz, A., Wood, J.M., Allen, J.C., Bornet, E.P., Entman, M.L., Goldstein, M.A., Sordahl, L.A., Suzuki, M.: Biochemical and morphologic correlates of cardiac ischemia. I. Membrane system. Am. J. Cardiol. 32, 46–61 (1973)

    CAS  Google Scholar 

  • Schwartz, A., Allen, J.C., Van Winkle, W.B., Munson, R.: Further studies on the correlation between the inotropic action of ouabain and its interaction with the Na+, K+-adenosine triphosphatase: Isolated perfused rabbit and cat hearts. J. Pharmacol. Exp. Ther. 191, 119–127 (1974)

    PubMed  CAS  Google Scholar 

  • Schwartz, A., Lindenmayer, G.E., Allen, J.C.: The sodium-potassium adenosine triphosphatase: Pharmacological, physiological, and biochemical aspects. Pharmacol. Rev. 27, 3–134 (1975)

    CAS  Google Scholar 

  • Sen, A.K., Tobin, T., Post, R.L.: A cycle for ouabain inhibition of sodium-and potassium-dependent adenosine triphosphatase. J. Biol. Chem. 244, 6596–6604 (1969)

    PubMed  CAS  Google Scholar 

  • Sharma, V.K., Banerjee, S.P.: Specific [3H]ouabain binding to rat heart and skeletal muscle: Effects of thyroidectomy. Mol. Pharmacol. 14, 122–129 (1978)

    CAS  Google Scholar 

  • Siegel, G.J., Josephson, J.: Ouabain reaction with microsomal (sodium-plus-potassium)-activated adenosine-triphosphatase: Characteristics of substrate and ion dependencies. Eur. J. Biochem. 25, 323–335 (1972)

    PubMed  CAS  Google Scholar 

  • Siegel, G.J., Koval, G.J., Albers, R.W.: Sodium-potassium-activated adenosine triphosphatase. VI. Characterization of the phosphoprotein formed from orthophosphate in the presence of ouabain. J. Biol. Chem. 244, 3264–3269 (1969)

    PubMed  CAS  Google Scholar 

  • Singh, C.M., Flear, C.T.G., Nandra, A., Ross, D.N.: Electrolyte changes in the human myocardium after anoxic arrest. Cardiology 56, 128–135 (1971)

    PubMed  CAS  Google Scholar 

  • Skou, J.C.: The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim. Biophys. Acta (Amst.) 23, 394–401 (1957)

    CAS  Google Scholar 

  • Skou, J.C.: Further investigations on a Mg++Na+-activated adenosinetriphosphatase, possibly related to the active, linked transport of Na+ and K+ across the nerve membrane. Biochim. Biophys. Acta (Amst.) 42, 6–23 (1960)

    CAS  Google Scholar 

  • Skou, J.C.: Enzymatic basis for active transport of Na and K across cell membrane. Physiol. Rev. 45, 596–617 (1965)

    CAS  Google Scholar 

  • Skou, J.C.: Study on the influence of the concentration of Mg’, Pi, K+, Na+, and Tris on (Mg2++Pi)-supported G-strophanthin binding to (Na + + K +)-activated ATPase from ox brain. Biochim Biophys. Acta (Amst.) 311, 51–66 (1973)

    Google Scholar 

  • Skou, J.C., Hilberg, C.: The effect of cations, G-strophanthin and oligomycin on the labeling from (32P) ATP of the (Na+ + K+)-activated enzyme system and the effect of cations and G-strophanthin on the labeling from (32P) ITP and 32Pi. Biochim. Biophys. Acta (Amst.) 185, 198–219 (1969)

    CAS  Google Scholar 

  • Skou, J.C., Butler, K.W., Hansen, O.: The effect of magnesium, ATP, Pi, and sodium on the inhibition of the (Na + + K +)-activated enzyme system by g-strophanthin. Biochim. Biophys. Acta (Amst.) 241, 443–461 (1971)

    CAS  Google Scholar 

  • Smith, T.W., Haber, E.: Digitalis. New Engl. J. Med. 289, 1125–1129 (1973)

    CAS  Google Scholar 

  • Smith, T.W., Wagner, H. Jr.: Effects of (Na + + K +)-ATPase-specific antibodies on enzy-matic activity and monovalent cation transport. J. Membrane Biol. 25, 341–360 (1975)

    Google Scholar 

  • Smith, T.W., Wagner, H. Jr., Markis, J.E., Young, M.: Studies on the localization of the cardiac glycoside receptor. J. Clin. Invest. 51, 1777–1789 (1972)

    PubMed  CAS  Google Scholar 

  • Smith, T.W., Wagner, H. Jr., Young, M.: Cardiac glycoside interaction with solubilized myocardial sodium-and potassium-dependent adenosine triphosphatase. Mol. Pharmacol. 10, 626–633 (1974)

    CAS  Google Scholar 

  • Stickney, J L Inhibition of 3H-1-norepinephrine uptake by ouabain is species dependent. Res. Commun. Chem. Pathol. Pharmacol. 14, 227–236 (1976)

    CAS  Google Scholar 

  • Swanson, P.D.: Temperature dependence of sodium ion activation of the cerebral microsomal adenosine triphosphatase. J. Neurochem. 13, 229–236 (1966)

    PubMed  CAS  Google Scholar 

  • Sybers, H.D., Helmer, P.R., Murphy, Q.R.: Effect of hypoxia on myocardial potassium balance. Am. J. Physiol. 220, 2047–2050 (1971)

    PubMed  CAS  Google Scholar 

  • Taniguchi, K., Iida, S.: The binding of ouabain to Na + -K +-dependent ATPase treated with phospholipase. Biochim. Biophys. Acta (Amst.) 233, 831–833 (1971)

    CAS  Google Scholar 

  • Taniguchi, K., Iida, S.: Two apparently different ouabain binding sites of (Na + + K +)-ATPase. Biochim. Biophys. Acta (Amst.) 288, 98–102 (1972)

    CAS  Google Scholar 

  • Taniguchi, K., Iida, S.: The role of phospholipids in the binding of ouabain to sodium-and potassium-dependent adenosine triphosphatase. Mol. Pharmacol. 9, 350–359 (1973)

    CAS  Google Scholar 

  • Thomas, R.C.: Electrogenic sodium pump in nerve and muscle cells. Physiol. Rev. 52, 563–594 (1972)

    CAS  Google Scholar 

  • Thomas, R., Boutagy, J., Gelbart, A.: Cardenolide analogs. V. Cardiotonic activity of semi- synthetic analogs of digitoxigenin. J. Pharmacol. Exp. Ther. 191, 219–231 (1974)

    PubMed  CAS  Google Scholar 

  • Tobin, T., Brody, T.M.: Rates of dissociation of enzyme-ouabain complexes and K0.5 values in (Na + + K +) adenosine triphosphatase from different species. Biochem. Pharmacol. 21, 1553–1560 (1972)

    CAS  Google Scholar 

  • Tobin, T., Sen, A.K.: Stability and ligand sensitivity of (3H) ouabain binding to (Na ++ K+)-ATPase. Biochim. Biophys. Acta (Amst.) 198, 120–131 (1970)

    CAS  Google Scholar 

  • Tobin, T., Baskin, S.I., Akera, T., Brody, T.M.: Nucleotide specificity of the Na+-stimulated phosphorylation and (3H) ouabain-binding reactions of (Na + + K +)-dependent adenosine triphosphatase. Mol. Pharmacol. 8, 256–263 (1972a)

    CAS  Google Scholar 

  • Tobin, T., Henderson, R., Sen, A.K.: Species and tissue differences in the rate of dissociation of ouabain from (Na + + K +)-ATPase. Biochim. Biophys. Acta (Amst.) 274, 551–555 (1972b)

    CAS  Google Scholar 

  • Tobin, T., Akera, T., Baskin, S.I., Brody, T.M.: Calcium ion and sodium-and potassium-dependent adenosine triphosphatase: Its mechanism of inhibition and identification of the E1-P intermediate. Mol. Pharmacol. 9, 336–349 (1973a)

    CAS  Google Scholar 

  • Tobin, T., Akera, T., Hogg, R.E., Brody, T.M.: Ouabain binding to sodium-and potassium-dependent adenosine triphosphatase- Inhibition by the ß-y-methylene analogue of adenosine triphosphate. Mol. Pharmacol. 9, 278–281 (1973b)

    CAS  Google Scholar 

  • Tobin, T., Akera, T., Ku, D.: Reversibility of the interaction of strophanthidin bromoacetate with the cardiotonic steroid binding site of sodium-and potassium-dependent adenosine triphosphatase. Mol. Pharmacol. 9, 676–685 (1973c)

    CAS  Google Scholar 

  • Tobin, T., Akera, T., Brody, T.M.: Studies on the two phosphoenzyme conformations of Na++K+-ATPase. Ann. N.Y. Acad. Sci. 242, 120–132 (1974a)

    CAS  Google Scholar 

  • Tobin, T., Akera, T., Lee, C.Y., Brody, T.M.: Ouabain binding to (Na+ +K+)-ATPase: Effects of nucleotide analogues and ethacrynic acid. Biochim. Biophys. Acta (Amst.) 345, 102–117 (1974b)

    CAS  Google Scholar 

  • Tuttle, R.S., Witt, P.N., Farah, A.: Therapeutic and toxic effects of ouabain on K+ fluxes in rabbit atria. J. Pharmacol. Exp. Ther. 137, 24–30 (1962)

    PubMed  CAS  Google Scholar 

  • Vick, R.L., Kahn, J.B.,Jr.: The effects of ouabain and veratridine on potassium movement in the isolated guinea pig heart. J. Pharmacol. Exp. Ther. 121, 389–401 (1957)

    Google Scholar 

  • Wallick, E.T., Schwartz, A.: Thermodynamics of the rate of binding of ouabain to the sodium, potassium adenosine triphosphatase. J. Biol. Chem. 249, 5141–5147 (1974)

    PubMed  CAS  Google Scholar 

  • Wallick, E.T., Dowd, F., Allen, J.C., Schwartz, A.: The nature of the transport adenosine triphosphatase-digitalis complex. VII. Characteristics of ouabagenin-Na+, K+-adenosine triphosphatase interaction. J. Pharmacol. Exp. Ther. 189, 434–444 (1974)

    PubMed  CAS  Google Scholar 

  • Wallick, E.T., Lindenmayer, G.E., Lane, L.K., Allen, J.C., Pitts, B.J.R., Schwartz, A.: Recent advances in cardiac glycoside–Na+, K+-ATPase interaction. Fed. Proc. 36, 2214–2218 (1977)

    CAS  Google Scholar 

  • Weaver, L.C., Akera, T., Brody, T.M.: Digitalis toxicity: Lack of marked effect on brain Na +, K+-adenosine triphosphatase in the cat. J. Pharmacol. Exp. Ther. 200, 638–646 (1977)

    PubMed  CAS  Google Scholar 

  • Whittam, R., Wheeler, K.P., Blake, A.: Oligomycin and active transport reactions in cell membranes. Nature (Lond.) 203, 720–724 (1964)

    CAS  Google Scholar 

  • Whittam, R., Hallam, C., Wattam, D.G.: Observations on ouabain binding and membrane phosphorylation by the sodium pump. Proc. Roy. Soc. London B 193, 217–234 (1976)

    CAS  Google Scholar 

  • Wilbrandt, W.: Zum Wirkungsmechanismus der Herzglykoside. Schweiz. Med. Wochenschr. 85, 315–320 (1955)

    CAS  Google Scholar 

  • Willerson, J.T., Scales, F., Mukherjee, A., Platt, M., Templeton, G.H., Fink, G.S., Buja, L.M.: Abnormal myocardial fluid retention as an early manifestation of ischemic injury. Am. J. Pathol. 87, 159–181 (1977)

    PubMed  CAS  Google Scholar 

  • Wilson, W.E., Sivitz, W.I., Hanna, L.T.: Inhibition of calf brain membranal sodium-and potassium-dependent adenosine triphosphatase by cardioactive sterols. A binding site model. Mol. Pharmacol. 6, 449–459 (1970)

    CAS  Google Scholar 

  • Yamamoto, S., Akera, T., Brody, T.M.: Sodium influx rate and ouabain-sensitive rubidium uptake in isolated guinea pig atria. Biochim. Biophys. Acta (Amst.) 555, 270–284 (1979)

    CAS  Google Scholar 

  • Yoda, A.: Structure-activity relationships of cardiotonic steroids for the inhibition of sodium-and potassium-dependent adenosine triphosphatase. I. Dissociation rate constants of various enzyme-cardiac glycoside complexes formed in the presence of magnesium and phosphate. Mol. Pharmacol. 9, 51–60 (1973)

    CAS  Google Scholar 

  • Yoda, A.: Association and dissociation rate constants of the complexes between various car-diac monoglycosides and Na, K-ATPase. Ann. N.Y. Acad. Sci. 242, 598–616 (1974)

    PubMed  CAS  Google Scholar 

  • Yoda, A.: Binding of digoxigenin to sodium-and potassium-dependent adenosine triphos-phatase. Mol. Pharmacol. 12, 399–408 (1976)

    CAS  Google Scholar 

  • Yoda, A., Hokin, L.E.: On the reversibility of binding of cardiotonic steroids to a partially purified (Na + K)-activated adenosinetriphosphatase from beef brain. Biochem. Biophys. Res. Commun. 40, 880–886 (1970)

    CAS  Google Scholar 

  • Yoda, A., Hokin, L.E.: Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. VIII. Effects of ligands on fluorescence due to interaction of the enzyme with a fluorescent derivative of Hellebrigenin. Mol. Pharmacol. 8, 30–40 (1972)

    CAS  Google Scholar 

  • Yoda, A., Yoda, S.: Structure-activity relationships of cardiotonic steroids for the inhibition of sodium-and potassium-dependent adenosine triphosphatase. III. Dissociation rate constants of various enzyme-cardiac glycoside complexes formed in the presence of sodium, magnesium, and adenosine triphosphate. Mol. Pharmacol. 10, 494–500 (1974a)

    CAS  Google Scholar 

  • Yoda, A., Yoda, S.: Influence of certain ligands on the dissociation rate constants of cardiac glycoside complexes with sodium-and potassium-dependent adenosine triphosphatase. Mol. Pharmacol. 10, 810–819 (1974b)

    CAS  Google Scholar 

  • Yoda, A., Yoda, S.: Structure-activity relationships of cardiotonic steroids for the inhibition of sodium-and potassium-dependent adenosine triphosphatase. V. Dissociation rate constants of digitoxin acetates. Mol. Pharmacol. 11, 653–662 (1975)

    CAS  Google Scholar 

  • Yoda, A., Yoda, S.: Association and dissociation rate constants of the complexes between various cardiac aglycones and sodium-and potassium-dependent adenosine triphosphatase formed in the presence of magnesium and phosphate. Mol. Pharmacol. 13, 352–361 (1977)

    CAS  Google Scholar 

  • Yoda, A., Yoda, S.: Influence of pH on the interaction of cardiotonic steroids with sodium-and potassium-dependent adenosine triphosphatase. Mol. Pharmacol. 14, 624–632 (1978)

    CAS  Google Scholar 

  • Yoda, A., Yoda, S., Sarrif, A.M.: Structure-activity relationships of cardiotonic steroids for the inhibition of sodium-and potassium-dependent adenosine triphosphatase. II. Association rate constants of various enzyme-cardiac glycoside complexes. Mol. Pharmacol. 9, 766–773 (1973)

    CAS  Google Scholar 

  • Yoda, S., Sarrif, A.M., Yoda, A.: Structure-activity relationships of cardiotonic steroids for the inhibition of sodium-and potassium-dependent adenosine triphosphatase. IV. Dissociation rate constants for complexes of the enzyme with cardiac oligodigitoxides. Mol. Pharmacol. 11, 647–652 (1975)

    CAS  Google Scholar 

  • Zavecz, J.H., Dutta, S.: The relationship between Na, K+-ATPase inhibition and cardiac glycoside-induced arrhythmia in dogs. Naunyn-Schmiedebergs Arch. Pharmacol. 297, 91–98 (1977)

    CAS  Google Scholar 

Download references

Authors
  1. T. Akera
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Instituts für Pharmakologie, Universität Düsseldorf, Moorenstrasse 5, D-4000, Düsseldorf, Germany

    Kurt Greeff (Direktor) (Direktor)

Rights and permissions

Reprints and permissions

Copyright information

© 1981 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Akera, T. (1981). Effects of Cardiac Glycosides on Na+, K+-ATPase. In: Greeff, K. (eds) Cardiac Glycosides. Handbook of Experimental Pharmacology, vol 56 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68163-9_14

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-68163-9_14

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-68165-3

  • Online ISBN: 978-3-642-68163-9

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation