Advertisement

Kinetic Regulation of Catalytic and Transport Activities in Sarcoplasmic Reticulum ATPase

  • Giuseppe Inesi
  • Leopoldo de Meis

Abstract

The cytoplasmic Ca2+ concentration is generally several orders of magnitude lower than that of extracellular fluids. This gradient must be maintained by energy-dependent transport mechanisms located in the cell membrane. In addition, intracellular membranous structures may form compartments which serve as Ca2+ sinks and reservoirs inside the cell. In some tissues, in which specific functional controls require rapid Ca2+ delivery to, and sequestration from, the cytoplasm, these intracellular systems are developed to a highly differentiated and prominent degree. A prime example is the sarcoplasmic reticulum (SR) of fast striated muscles. The membrane of the sarcoplasmic reticulum can be isolated in vesicular form from muscle homogenates by differential centrifugation. When suspended in a medium containing ATP and Mg2+, these vesicles reduce the Ca2+ concentration of the medium from 10−4 M to less than 10−7 M, which is the level found in the cytosol of living muscle cells in a resting state. This was discovered, independently, by Hasselbach and Makinose (1962) and Ebashi and Lipman (1962).

Keywords

Sarcoplasmic Reticulum Calcium Binding Dependent ATPase Sarcoplasmic Reticulum Membrane Sarcoplasmic Reticulum Vesicle 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Allen, D., Blinks, J., and Prendergast, F., 1977, Aequorin luminescence: Relation of light emission to calcium concentration—A calcium-independent component, Science 195:996–998.PubMedGoogle Scholar
  2. Barlogie, B., Hasselbach, W., and Makinose, M., 1971, Activation of calcium efflux by ADP and inorganic phosphate, FEBS Leu. 12:267–268.Google Scholar
  3. Bastide, F., Meissner, G., Fleischer, S., and Post, R. L., 1973, Similarity of the active site of phosphorylation of the ATPase for transport of sodium and potassium ions in kidney to that for transport of calcium ions in sarcoplasmic reticulum of muscle, J. Biol. Chem. 248:8385–8391.PubMedGoogle Scholar
  4. Beil, F., Chak, D., and Hasselbach, W., 1977, Phosphorylation from inorganic phosphate and ATP synthesis of sarcoplasmic membranes, Eur. J. Biochem. 81:151–164.PubMedGoogle Scholar
  5. Boyer, P., de Meis, L., and Carvalho, M., 1977, Dynamic reversal of enzyme carboxyl group phosphorylation as the basis of the oxygen exchange catalyzed by sarcoplasmic reticulum adenosine triphosphatase, Biochemistry 16:136–140.PubMedGoogle Scholar
  6. Cantley, L., 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.PubMedGoogle Scholar
  7. Cantley, L. C., Cantley, L. G., and Josephson, L., 1978, A characterization of vanadate interactions with the (Na,K)-ATPase. Mechanistic and regulatory implications, J. Biol. Chem. 253:7361–7368.PubMedGoogle Scholar
  8. Carvalho, A., 1966, Binding of cations by microsomes from rabbit skeletal muscle, J. Cell. Physiol. 67:73–84.PubMedGoogle Scholar
  9. Carvalho, A., 1972, Binding and release of cations by sarcoplasmic reticulum before and after removal of lipid, Eur. J. Biochem. 27:491–502.PubMedGoogle Scholar
  10. Carvalho, M., de Souza, D., and de Meis, L., 1976, On a possible mechanism of energy conservation in sarcoplasmic reticulum membrane, J. Biol. Chem. 251:3629–3636.PubMedGoogle Scholar
  11. Chaloub, R., Guimaraes-Motta, H., Verjovski-Almeida, S., de Meis, L., and Inesi, G., 1979, Sequential reactions in P, utilization for ATP synthesis by sarcoplasmic reticulum, J. Biol. Chem. 254:9464–9468.PubMedGoogle Scholar
  12. Champeil, P., Bastide, F., Taupin, C., and Gary-Bobo, C. M., 1976, Spin labelled sarcoplasmic reticulum vesicles: Ca’ -induced spectral change, FEBS Letters 63:270–272.PubMedGoogle Scholar
  13. Chevallier, J., and Buton, R., 1971, Calcium binding to the sarcoplasmic reticulum of rabbit skeletal muscle, Biochemistry 10:2733–2737.PubMedGoogle Scholar
  14. Chiesi, M., and Inesi, G., 1979, The use of quench reagents for resolution of single transport cycles in sarcoplasmic reticulum, J. Biol. Chem. 254:10370–10377.PubMedGoogle Scholar
  15. Chiesi, M., and Inesi, G., 1980, Adenosine triphosphate dependent fluxes of manganese and hydrogen ions in sarcoplasmic reticulum vesicles, Biochemistry 19:2912–2918.PubMedGoogle Scholar
  16. Chiu, V., and Haynes, D., 1977, High and low affinity Ca2+ binding to sarcoplasmic reticulum—use of a high-affinity fluorescent calcium indicator, Biophys. J. 18:3–22.PubMedGoogle Scholar
  17. Chiu, V., and Haynes, D., 1980, Rapid kinetic studies of active Ca2+ transport in sarcoplasmic reticulum, J. Membr. Biol. 56:219–239.PubMedGoogle Scholar
  18. Coan, C., and Inesi, G., 1977, Calcium dependent effect of ATP on spin-labeled sarcoplasmic reticulum, J. Biol. Chem. 252:3044–3049.PubMedGoogle Scholar
  19. Degani, C., and Boyer, P., 1973, A borohydride reduction method for characterization of the acyl phosphate linkage in proteins and its application to sarcoplasmic reticulum adenosine triphosphatase, J. Biol. Chem. 248:8222–8226.PubMedGoogle Scholar
  20. de Meis, L., 1969, Ca2+ uptake and acetyl phosphatase of skeletal muscle microsomes, J. Biol. Chem. 244:3733–3739.PubMedGoogle Scholar
  21. de Meis, L., 1971, Allosteric inhibition by alkali ions of the Ca2+ uptake and adenosine triphosphatase activity of skeletal muscle microsomes, J. Biol. Chem. 246:4764–4773.PubMedGoogle Scholar
  22. de Meis, L., 1976, Regulation of steady state level of phosphoenzyme ATP synthesis in sarcoplasmic reticulum vesicles during reversal of the Ca2+ pump, J. Biol. Chem. 251:2055–2062.PubMedGoogle Scholar
  23. de Meis, L., and Hasselbach, W., 1971, Acetylphosphate as substrate for Ca2+ uptake in skeletal muscle microsomes, J. Biol. Chem. 246:4759–4763.PubMedGoogle Scholar
  24. de Meis, L., and Boyer, P., 1978, Induction by nucleotide triphosphate hydrolysis of a form of sarcoplasmic reticulum ATPase capable of medium phosphate–oxygen exchange in presence of calcium, J. Biol. Chem. 253:1556–1559.PubMedGoogle Scholar
  25. de Meis, L., and Carvalho, M., 1974, Role of the Ca2+ concentration gradient in the adenosine 5’triphosphate-inorganic phosphate exchange catalyzed by sarcoplasmic reticulum, Biochemistry 13:5032–5038.PubMedGoogle Scholar
  26. de Meis, L., and de Mello, M. C. F., 1973, Substrate regulation of membrane phosphorylation and calcium transport in the sarcoplasmic reticulum, J. Biol. Chem. 248:3691–3701.PubMedGoogle Scholar
  27. de Meis, L., and Inesi, G., 1982, ATP synthesis by sarcoplasmic reticulum ATPase following Ca2+, pH, temperature, and water activity jumps, J. Biol. Chem. 257:1289–1294.PubMedGoogle Scholar
  28. de Meis, L., and Masuda, H., 1974, Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate through two different reactions, Biochemistry 13:2057–2062.PubMedGoogle Scholar
  29. de Meis, L., and Sorenson, M., 1975, ATP–P, exchange and membrane phosphorylation in sarcoplasmic reticulum vesicles: Activation by silver in the absence of a Ca2+ concentration gradient, Biochemistry 14:2739–2744.PubMedGoogle Scholar
  30. de Meis, L., and Tume, R., 1977, A new mechanism by which an H2+ concentration gradient drives the synthesis of adenosine triphoshate, pH jump, and adenosine triphosphate synthesis by the Ca2+-dependent adenosine triphosphatase of sarcoplasmic reticulum, Biochemistry 16:4455–4463.PubMedGoogle Scholar
  31. de Meis, L., and Vianna, A., 1979, Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum, Annu. Rev. Biochem. 48:275–292.PubMedGoogle Scholar
  32. de Meis, L., Martins, O., and Alves, E., 1980, Role of water, H2+s and temperature on the synthesis of ATP by the sarcoplasmic reticulum ATPase in the absence of a Ca2+ gradient, Biochemistry 19:4252–4261.PubMedGoogle Scholar
  33. de Souza, D., and de Meis, L., 1976, Calcium and magnesium regulation of phosphorylation by ATP and ITP in sarcoplasmic reticulum vesicles, J. Biol. Chem. 251:6355–6359.PubMedGoogle Scholar
  34. Dupont, Y., 1977, Kinetics and regulation of sarcoplasmic reticulum ATPase, Eur. J. Biochem. 72:185–190.PubMedGoogle Scholar
  35. Dupont, Y., 1980, Occlusion of divalent cations in the phosphorylated calcium pump of sarcoplasmic reticulum, Eur. J. Biochem. 109:231–238.PubMedGoogle Scholar
  36. Dupont, Y., 1982, Low-temperature studies of the sarcoplasmic reticulum calcium pump mechanism of calcium binding, Biochim. Biophys. Acta 688:75–87.PubMedGoogle Scholar
  37. Dupont, Y., and Bennett, N., 1982, Vanadate inhibition of the Ca2+-dependent conformational change of the sarcoplasmic reticulum Ca2+-ATPase, FEBS Lett. 139:237–240.PubMedGoogle Scholar
  38. Dupont, Y., and Leigh, J., 1978, Transient kinetics of sarcoplasmic reticulum Ca + Mg ATPase studied by fluorescence, Nature 273:396–398.PubMedGoogle Scholar
  39. Ebashi, S., 1961, Calcium binding activity of vesicular relaxing factor, J. Biochem. (Tokyo) 50:236–244.Google Scholar
  40. Ebashi, S., and Lipmann, F., 1962, Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle, J. Cell Biol. 14:389–400.PubMedGoogle Scholar
  41. Fabiato, A., and Fabiato, F., 1979, Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells, J. Physiol. (Paris) 75:463–505.Google Scholar
  42. Fiehn, W., and Migala, A., 1971, Calcium binding to sarcoplasmic membranes, Eur. J. Biochem. 20:245–248.PubMedGoogle Scholar
  43. Friedman, Z., and Makinose, M., 1970, Phosphorylation of skeletal muscle microsomes by acetylphosphate, FEBS Letters 11:69–72.PubMedGoogle Scholar
  44. Froehlich, J., and Taylor, E., 1976, Transient state kinetic effects of calcium ion on sarcoplasmic reticulum adenosine triphosphatase, J. Biol. Chem. 251:2307–2315.PubMedGoogle Scholar
  45. Gattass, C., and de Meis, L., 1975, Ca2+-dependent inhibitory effects of Na and K` on Ca++ -transport in sarcoplasmic reticulum vesicles, Biochim. Biophys. Acta 389:506–515.PubMedGoogle Scholar
  46. Guimaraes-Motta, H., and de Meis, L., 1980, Pathway for ATP synthesis by sarcoplasmic reticulum ATPase, Arch. Biochem. Biophys. 203:395–403.Google Scholar
  47. Hammes, G., 1982, Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis, Proc. Natl. Acad. Sci. USA 79:6881–6884.PubMedGoogle Scholar
  48. Hasselbach, W., 1964, Relating factor and the relaxation of muscle, Progress in Biophysics and Mol. Biol. 14:167–222.Google Scholar
  49. Hasselbach, W., 1978, The reversibility of the sarcoplasmic calcium pump, Biochim. Biophys. Acta 515:23–53.PubMedGoogle Scholar
  50. Hasselbach, W., and Makinose, M., 1962, ATP and active transport, Biochem. Biophys. Res. Commun. 7:132–136.PubMedGoogle Scholar
  51. Haynes, D., 1983, Computer modeling of the Ca2+ -Mg++-ATPase pump of skeletal sarcoplasmic reticulum, Biophys. J. 41:233.Google Scholar
  52. Hill, T., and Eisenberg, E., 1981, Can free energy transduction be localized at some crucial part of the enzymatic cycle?, Quart. Rev. Biophys. 14:1–49.Google Scholar
  53. Hill, T., and Inesi, G., 1982, Equilibrium cooperative binding of calcium and protons by sarcoplasmic reticulum ATPase, Proc. Natl. Acad. Sci. USA 79:3978–3982.PubMedGoogle Scholar
  54. Holloway, J., and Reilley, C., 1960, Metal chelate stability constants of aminopolycarboxylate ligands, Anal. Chem. 32:249–256.Google Scholar
  55. Ikemoto, N., 1974, The calcium binding sites involved in the regulation of the purified adenosine triphosphatase of the sarcoplasmic reticulum, J. Biol. Chem. 249:649–651.PubMedGoogle Scholar
  56. Ikemoto, N., 1975, Transport and inhibitory calcium binding sites on the ATPase enzyme isolated from the sarcoplasmic reticulum, J. Biol. Chem. 250:7219–7224.PubMedGoogle Scholar
  57. Ikemoto, N., 1976, Behavior of the Ca2+ transport sites linked with the phosphorylation reaction of ATPase purified from the sarcoplasmic reticulum, J. Biol. Chem. 251:7275–7277.PubMedGoogle Scholar
  58. Ikemoto, N., 1982, Structure and function of the calcium pump protein of sarcoplasmic reticulum, Annu. Rev. Physiol. 44:297–317.PubMedGoogle Scholar
  59. Ikemoto, N., Morgan, T., and Yamada, S., 1978, Ca2+ controlled conformational states in the Ca2+ transport enzyme of sarcoplasmic reticulum, J. Biol. Chem. 253:8027–8033.PubMedGoogle Scholar
  60. Inesi, G., 1981, The sarcoplasmic reticulum of skeletal and cardiac muscle, in: Cell and Muscle Motility, Vol. 1 (R. Dowben and J. Shay, eds.), Plenum Publishing Corporation, New York, pp. 63–97.Google Scholar
  61. Inesi, G., and Almendares, J., 1968, Interaction of fragmented sarcoplasmic reticulum with 14C-ADP, 14C- ATP, and 32P-ATP. Effect of Ca and Mg, Arch. Biochem. Biophys. 126:733–735.PubMedGoogle Scholar
  62. Inesi, G., and Scarpa, A., 1972, Fast kinetics of adenosine triphosphate Ca2+ uptake by frequented sarcoplasmic reticulum, Biochemistry 11:356–359.PubMedGoogle Scholar
  63. Inesi, G., and Hill, T., 1983, The calcium and proton dependence of sarcoplasmic reticulum ATPase, Biophys. J., in press.Google Scholar
  64. Inesi, G., Goodman, J. J., and Watanabe, S., 1967, Effect of diethyl ether on the ATPase activity and calcium uptake of fragmented sarcoplasmic reticulum of rabbit skeletal muscle, J. Biol. Chem. 242:4637–4643.PubMedGoogle Scholar
  65. Inesi, G., Lewis, D., and Murphy, A., 1984, Interdependence of H+, Ca2+ and P, (or vanodate) sites in sarcoplasmic reticulum ATPase, J. Biol. Chem. (in press).Google Scholar
  66. Inesi, G., Maring, E., Murphy, A., and McFarland, B., 1970, A study of the phosphorylated intermediate in sarcoplasmic reticulum ATPase, Arch. Biochem. Biophys. 138:285–294.PubMedGoogle Scholar
  67. Inesi, G., Kurzmack, M., Coan, C., and Lewis, D., 1980a, Cooperative calcium binding and ATPase activation in sarcoplasmic reticulum vesicles, J. Biol. Chem. 255:3025–3031.Google Scholar
  68. Inesi, G., Kurzmack, M., Nakamoto, R., de Meis, L., and Bernhard, S., 1980b, Uncoupling of calcium control and phosphohydrolase activity in sarcoplasmic reticulum vesicles, J. Biol. Chem. 255:6040–6043Google Scholar
  69. Inesi, G., Watanabe, T., Coan, C., and Murphy, A., 1983, The mechanism of sarcoplasmic reticulum ATPase, Ann. N.Y. Acad. Sci. 402:515–534.Google Scholar
  70. Inesi, G., Lewis, D., and Murphy, A. J., 1984, Interdependence of H+, Ca2+, and P, (or vanadate) sites in sarcoplasmic reticulum ATPase, J. Biol. Chem. 259:996–1003.PubMedGoogle Scholar
  71. Jencks, W., 1980, The utilization of binding energy in coupled vectorial processes, Adv. Enzymol. 51:75–106.PubMedGoogle Scholar
  72. Kalbitzer, H., Stehlik, D., and Hasselbach, W., 1978, Binding of calcium and magnesium to sarcoplasmicreticulum vesicles as studied by manganese electron-paramagnetic resonance, Eur. J. Biochem. 82:245–255.PubMedGoogle Scholar
  73. Kanazawa, T., 1975, Phosphorylation of solubilized sarcoplasmic reticulum by orthophosphate and its thermodynamic characteristics—the dominant role of entropy in the phosphorylation, J. Biol. Chem. 250:113–119.PubMedGoogle Scholar
  74. Kanazawa, T., and Boyer, P., 1973, Occurrence and characteristics of a rapid exchange of phosphate–oxygen catalyzed by sarcoplasmic reticulum vesicles, J. Biol. Chem. 248:3163–3172.PubMedGoogle Scholar
  75. Kanazawa, T., Yamada, S., Yamamoto, T., and Tonomura, Y., 1971, Reaction mechanism of the Ca - dependent ATPase of sarcoplasmic reticulum from skeletal muscle: V. Vectorial requirements for calcium and magnesium ions of three partial reations of ATPase: Formation and decomposition of a phosphorylated intermediate ATP-formation from ADP and the intermediate, J. Biochem. (Tokyo) 70:95–123.Google Scholar
  76. Knowles, A., and Racker, E., 1975, Formation of adenosine triphosphate from P, and adenosine diphosphate by purified Ca2+ -adenosine triphosphatase, J. Biol. Chem. 250:1949–1951.PubMedGoogle Scholar
  77. Kolassa, N., Punzengruber, C., Suko, J., and Makinose, M., 1979, Mechanism of calcium-independent phosphorylation of sarcoplasmic reticulum ATPase by orthophosphate, FEBS Lett. 108:495–500.PubMedGoogle Scholar
  78. Kurzmack, M., and Inesi, G., 1977, The initial phase of calcium uptake and ATPase activity of sarcoplasmic reticulum vesicles, FEBS Leu. 74:35–37.Google Scholar
  79. Kurzmack, M., Verjovski-Almeida, S., and Inesi, G., 1977, Detection of an initial burst of calcium translocation in sarcoplasmic reticulum, Biochem. Biophys. Res. Commun. 78:772–776.PubMedGoogle Scholar
  80. Kurzmack, M., Inesi, G., Tal, N., and Bernhard, S., 1981, Transient-state kinetic studies on the mechanism of furylacryloylphosphatase-coupled calcium ion transport with sarcoplasmic reticulum adenosine triphosphatase, Biochemistry 20:486–491.PubMedGoogle Scholar
  81. Lacapere, J., Gingold, M., Champeil, P., and Guillain, F., 1981, Sarcoplasmic reticulum ATPase phosphorylation from inorganic phosphate in the absence of a calcium gradient: Steady state and fluorescence studies, J. Biol. Chem. 256:2302–2306.PubMedGoogle Scholar
  82. Madeira, V., 1978, Proton gradient formation during transport of Ca++ by sarcoplasmic reticulum, Arch. Biochem. Biophys. 185:316–325.PubMedGoogle Scholar
  83. Makinose, M., 1966, Die Nucleosid-triphosphat, nucleosid-diphosphat-transphosphorylase-aktivitat der Vesikel des sarkoplasmatischen reticulums, Biochem. Zeitschrift 345:80–86.Google Scholar
  84. Makinose, M., 1967, Gibt es zwei phosphorylierte intermediate des aktiven calcium-transportes in den membranen des sarcoplasmatischen reticulums?, Pfluger’s Arch. Ges. Physiol. 294:82–83.Google Scholar
  85. Makinose, M., 1969, The phosphorylation of the membrane protein of the sarcoplasmic vesicles during active calcium transport, Eur. J. Biochem. 10:74–82.PubMedGoogle Scholar
  86. Makinose, M., 1971, Calcium efflux dependent formation of ATP from ADP and orthophosphate by the membranes of the sarcoplasmic vesicles, FEBS Leu. 12:269–270.Google Scholar
  87. Makinose, M., 1972, Phosphoprotein formation during osmo-chemical energy conversion in the membrane of the sarcoplasmic reticulum, FEBS Lett. 25:113–115.PubMedGoogle Scholar
  88. Makinose, M., and Hasselbach, W., 1965, Der einfluss von oxalat auf den calcium-transport isolierter vesikel des sarkoplasmatischen reticulum, Biochem. Zeitschrift 343:360–382.Google Scholar
  89. Makinose, M., and Hasselbach, W., 1971, ATP synthesis by the reverse of the sarcoplasmic calcium pump, FEBS Lett. 12:271–272.PubMedGoogle Scholar
  90. Makinose, M., and The, R., 1965, Calcium-akkumulation und nucleosidtriphosphat-spaltung durch die vesikel des sarkoplasmatischen reticulum, Biochem. Zeitschrift 343:383–393.Google Scholar
  91. Martin, D., and Tanford, C., 1981, Phosphorylation of (Ca2+)-ATPase by inorganic phosphate: van’t Hoff analysis of enthalpy changes, Biochemistry 20:4597–4603.PubMedGoogle Scholar
  92. Martonosi, A., 1969, Sarcoplasmic reticulum. VII. Properties of a phosphoprotein intermediate implicated in calcium transport, J. Biol. Chem. 244:613–620.PubMedGoogle Scholar
  93. Martonosi, A., 1971, The structure and function of sarcoplasmic reticulum membranes, in: Biomembranes, Vol. 1 (L. Manson, ed.), Plenum Press, New York, pp. 191–256.Google Scholar
  94. Martonosi, A., and Feretos, R., 1964, Sarcoplasmic reticulum: I. The uptake of Ca++ by sarcoplasmic reticulum fragments, J. Biol. Chem. 239:648–658.PubMedGoogle Scholar
  95. Martonosi, A., Lagwinska, E., and Oliver, M., 1974, Elementary processes in the hydrolysis of ATP by sarcoplasmic reticulum membranes, Ann. N.Y. Acad. Sci. 227:549–567.PubMedGoogle Scholar
  96. Masuda, H., and de Meis, L., 1973, Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions, Biochemistry 12:4581–4585.PubMedGoogle Scholar
  97. Masuda, H., and de Meis, L., 1977, Effect of temperature on the Ca++ transport ATPase of sarcoplasmic reticulum, J. Biol. Chem. 252:8567–8571.PubMedGoogle Scholar
  98. Meissner, G., 1973, ATP and Ca2+ binding by the Ca2+ pump protein of sarcoplasmic reticulum, Biochim. Biophys. Acta 298:906–926.PubMedGoogle Scholar
  99. Meissner, G., Conner, G., and Fleischer, S., 1973, Isolation of sarcoplasmic reticulum by zonal centrifugation and purification of Ca2+ -pump and Ca2+-binding proteins, Biochim. Biophys. Acta 298:246–269.PubMedGoogle Scholar
  100. Murphy, A., 1978, Effects of divalent cations and nucleotides on the reactivity of the sulfhydryl groups of sarcoplasmic reticulum membranes, J. Biol. Chem. 253:385–389.PubMedGoogle Scholar
  101. Nakamura, Y., and Tonomura, Y., 1978, Reaction mechanism of p-nitrophenylphosphatase of sarcoplasmic reticulum, J. Biochem. (Tokyo) 83:571–583.Google Scholar
  102. Neet, K., and Green, N., 1977, Kinetics of the cooperativity of the Ca++ -transporting adenosine triphosphatase of sarcoplasmic reticulum and the mechanism of the ATP interaction, Arch. Biochem. Biophys. 178:588–597.PubMedGoogle Scholar
  103. Ogawa, Y., 1968, The apparent binding constant of glycoletherdiaminetetraacetic acid for calcium at neutral pH, J. Biochem. (Tokyo) 64:255–257.Google Scholar
  104. Pang, D., and Briggs, F., 1977, Effect of calcium and magnesium on binding of beta, gamma-methylene ATP to sarcoplasmic reticulum, J. Biol. Chem. 252:3262–3266.PubMedGoogle Scholar
  105. Pick, U., 1982, The interaction of vanadate ions with the Ca-ATPase from sarcoplasmic reticulum, J. Biol. Chem. 257:6111–6119.PubMedGoogle Scholar
  106. Pick, U., and Karlish, S., 1980, Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labeled selectively with fluorescein, Biochim. Biophys. Acta 626:255–261.PubMedGoogle Scholar
  107. Pickart, C., and Jencks, W., 1982, Slow dissociation of ATP from the calcium ATPase, J. Biol. Chem. 257:5319–5322.PubMedGoogle Scholar
  108. Plank, B., Hellman, G., Punzengruber, C., and Suko, J., 1979, ATP—P; and ITP—P, exchange by cardiac sarcoplasmic reticulum, Biochim. Biophys. Acta 550:259–268.PubMedGoogle Scholar
  109. Prager, R., Punzengruber, C., Kolassa, N., Winkler, F., and Suko, J., 1979, Ionized and bound calcium inside isolated sarcoplasmic reticulum of skeletal muscle and its significance in phosphorylation of adenosine triphosphatase by orthophosphate, Eur. J. Biochem. 97:239–250.PubMedGoogle Scholar
  110. Pucell, A., and Martonosi, A., 1971, Sarcoplasmic reticulum: XIV. Acetylphosphate and carbamylphosphate as energy sources for Ca++ transport, J. Biol. Chem. 246:3389–3397.PubMedGoogle Scholar
  111. Punzengruber, C., Prager, R., Kolassa, N., Winkler, F., and Suko, J., 1978, Calcium gradient-dependent and calcium gradient-independent phosphorylation of sarcoplasmic reticulum by orthophosphate, Eur. J. Biochem. 92:349–359.PubMedGoogle Scholar
  112. Ratkje, S., and Shamoo, A., 1980, ATP synthesis by Ca++ + Mg++ -ATPase in detergent solution at constant Ca++ levels, Biophys. J. 30:523–530.PubMedGoogle Scholar
  113. Rauch, B., Chak, D., and Hasselbach, W., 1977, Phosphorylation by inorganic phosphate of sarcoplasmic membranes, Z. Naturforsch. Part C 32:828–834.Google Scholar
  114. Ribeiro, J., and Vianna, L., 1978, Allosteric modification by K+ of the (Ca2+ ++ Mg++)-dependent ATPase of sarcoplasmic reticulum, J. Biol. Chem. 253:3153–3157.PubMedGoogle Scholar
  115. Ronzani, N., Migala, A., Hasselbach, W., 1979, Comparison between ATP-supported and GTP-supported phosphate turnover of the calcium-transporting sarcoplasmic reticulum membranes, Eur. J. Biochem. 101:593–606.PubMedGoogle Scholar
  116. Rossi, B., Leone, F., Gache, C., and Lazdunski, M., 1979, Psuedosubstrates of the sarcoplasmic Ca++ATPase as tools to study the coupling between substrate hydrolysis and Ca2+ transport, J. Biol. Chem. 254:2302–2307.PubMedGoogle Scholar
  117. Scarpa, A., Baldassare, J., and Inesi, G., 1972, The effect of calcium ionophores on fragmented sarcoplasmic reticulum, J. Gen. Physiol. 60:735–749.PubMedGoogle Scholar
  118. Schmid, R., and Reilley, C., 1957, New complexon for titration of calcium in the presence of magnesium, Anal. Chem. 29:264–268.Google Scholar
  119. Schwartzenbach, G., Senn, H., and Anderegg, G., 1957, Komplexone. XXIX. Ein grosse Chelateffekt besonderer Azt., Hely. Chim. Acta 40:1186–1900.Google Scholar
  120. Scofano, H., Vieyra, A., and de Meis, L., 1979, Substrate regulation of the sarcoplasmic reticulum ATPase: Transient kinetic studies, J. Biol. Chem. 254:10227–10231.PubMedGoogle Scholar
  121. Shigekawa, M., and Dougherty, J., 1978a, Reaction mechanism of Ca++-dependent ATP hydrolysis by skeletal muscle sarcoplasmic reticulum in the absence of added alkali metal salts. II. Kinetic properties of the phosphoenzyme formed at the steady state in high Mg++ and low Ca++ concentrations, J. Biol. Chem. 253:1451–1457.Google Scholar
  122. Shigekawa, M., and Dougherty, J., 1978b, Reaction mechanism of Ca++ -dependent ATP hydrolysis by skeletal muscle sarcoplasmic reticulum in the absence of added alkali metal salts. III. Sequential occurrence of ADP-sensitive and ADP-insensitive phosphoenzymes, J. Biol. Chem. 253:1458–1464.Google Scholar
  123. Smith, R., Zinn, K., and Cantley, L., 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.PubMedGoogle Scholar
  124. Sorenson, M., and de Meis, L., 1977, Effects of anions, pH and magnesium on calcium accumulation and release by sarcoplasmic reticulum vesicles, Biochim. Biophys. Acta 465:210–223.PubMedGoogle Scholar
  125. Suko, J., and Hasselbach, W., 1976, Characterization of cardiac sarcoplasmic reticulum ATP—ADP exchange and phosphorylation of the calcium transport ATPase, Eur. J. Biochem. 64:123–130.PubMedGoogle Scholar
  126. Sumida, M., Wang, T., Mandel, F., Froehlich, J., and Schwartz, A., 1978, Transient kinetics of Ca“ transport of sarcoplasmic reticulum, J. Biol. Chem. 253:8772–8777.PubMedGoogle Scholar
  127. Tada, M., Yamamoto, T., and Tonomura, Y., 1978, Molecular mechanism of active calcium transport by sarcoplasmic reticulum, Physiol. Rev. 58:1–79.PubMedGoogle Scholar
  128. Takakuwa, Y., and Kanazawa, T., 1979, Slow transition of phoshoenzyme from ADP-sensitive to ADP-insensitive forms in solubilized Ca+ + Mg++-ATPase of sarcoplasmic reticulum: Evidence for retarded dissociation of Ca++ from the phosphoenzyme, Biochem. Biophys. Res. Commun. 88:1209–1216.PubMedGoogle Scholar
  129. Tanford, C., 1982a, Steady state of an ATP-driven calcium pump: Limitations on kinetic and thermodynamic parameters, Proc. Natl. Acad. Sci. USA 79:6161–6165.Google Scholar
  130. Tanford, C., 1982b, Mechanism of active transport: Free energy dissipation and free energy transduction, Proc. Natl. Acad. Sci. USA 79:6527–6531.Google Scholar
  131. Taylor, J., and Hattan, D., 1979, Biphasic kinetics of ATP hydrolysis by calcium-dependent ATPase of the sarcoplasmic reticulum of skeletal muscle, J. Biol. Chem. 254:440–2407.Google Scholar
  132. The, R., and Hasselbach, W., 1972a, The modification of the reconstituted sarcoplasmic ATPase by monovalent cations, Eur. J. Biochem. 30:318–324.Google Scholar
  133. The, R., and Hasselbach, W., 1972b, Properties of the sarcoplasmic ATPase reconstituted by oleate and lysolecithin after lipid depletion, Eur. J. Biochem. 28:357–363.Google Scholar
  134. Veno, T., and Sekine, T., 1981, A role of H+ flux in active Ca + transport in sarcoplasmic reticulum vesicles. I. Effect of an artificially imposed H+ gradient on Ca++ uptake, J. Biochem. (Tokyo) 89:1239–1246.Google Scholar
  135. Verjovski-Almeida, S., and de Meis, L., 1977, pH-induced changes in the reactions controlled by the low-and high-affinity Ca -binding sites in sarcoplasmic reticulum, Biochemistry 16:329–334.PubMedGoogle Scholar
  136. Verjovski-Almeida, S., and Inesi, G., 1979, Fast-kinetic evidence for an activating effect of ATP on the Ca2+ transport of sarcoplasmic reticulum ATpase, J. Biol. Chem. 254:18–21.PubMedGoogle Scholar
  137. Verjovski-Almeida, S., Kurzmack, M., and Inesi, G., 1978, Partial reactions in the catalytic and transport cycle of sarcoplasmic reticulum ATPase, Biochemistry 17:5006–5013.PubMedGoogle Scholar
  138. Vianna, A., 1975, Interaction of calcium and magnesium in activating and inhibiting the nucleoside triphosphatase of sarcoplasmic reticulum vesicles, Biochim. Biophys. Acta 410:389–406.Google Scholar
  139. Watanabe, T., and Inesi, G., 1982a, Structural effects of substrate utilization on the ATPase chains of sarcoplasmic reticulum, Biochemistry 21:3254–3259.Google Scholar
  140. Watanabe, T., and Inesi, G., 1982b, The use of 2’,3’-O-(2,4,6-trinitrophenyl) adenosine 5’-triphoshate for studies of nucleotide interaction with sarcoplasmic reticulum vesicles, J. Biol. Chem. 257:11510–11516.Google Scholar
  141. Watanabe, T., Lewis, D., Nakamoto, R., Kurzmack, M., Fronticelli, C., and Inesi, G., 1981, Modulation of calcium binding in sarcoplasmic reticulum adenosinetriphosphatase, Biochemistry 20:6617–6625.PubMedGoogle Scholar
  142. Weber, A., 1971a, Regulatory mechanisms of the calcium transport system of fragmented rabbit sarcoplasmic reticulum. I. The effect of accumulated calcium on transport and adenosine triphosphate hydrolysis, J. Gen. Physiol. 57:50–63.Google Scholar
  143. Weber, A., 1971b, Regulatory mechanisms of the calcium transport system of fragmented rabbit sarcoplasmic reticulum. II. Inhibition of outfux in calcium-free media, J. Gen. Physiol. 57:64–70.Google Scholar
  144. Weber, A., Herz, R., and Reiss, I., 1966, Study of the kinetics of calcium transport by isolated fragmented sarcoplasmic reticulum, Biochem. Zeitschrift 345:329–369.Google Scholar
  145. Yamada, S., and Tonomura, Y., 1972, Phosphorylation of the Ca++-Mg++-dependent ATPase of the sarcoplasmic reticulum coupled with cation translocation, J. Biochem. (Tokyo) 71:1101–1104.Google Scholar
  146. Yamada, S., and Tonomura, Y., 1973, Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. IX. Kinetic studies on the conversion of osmotic energy to chemical energy in the sarcoplasmic reticulum, J. Biochem. (Tokyo) 74:1091–1096.Google Scholar
  147. Yamada, S., Sumida, M., and Tonomura, Y., 1972, Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. VIII. Molecular mechanism of the conversion of osmotic energy to chemical energy in the sarcoplasmic reticulum, J. Biochem. (Tokyo) 72:1537–1548.Google Scholar
  148. Yamamoto, T., and Tonomura, Y., 1967, Reaction mechanism of the Ca++ -dependent ATPase of sar- coplasmic reticulum from skeletal muscle. I. Kinetic studies, J. Biochem. (Tokyo) 62:558–575.Google Scholar
  149. Yamamoto, T., and Tonomura, Y., 1968, Reaction mechanism of the Ca++ -dependent ATPase of sarcoplasmic reticulum from skeletal muscle. II. Intermediate formation of phosphoryl protein, J. Biochem. (Tokyo) 64:137–145.Google Scholar
  150. Yates, D., and Duance, V., 1976, The binding of nucleotides and bivalent cations to the calcium-andmagnesium ion-dependent adenosine triphosphatase from rabbit muscle sarcoplasmic reticulum, Biochem. J. 159:719–728.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Giuseppe Inesi
    • 1
  • Leopoldo de Meis
    • 2
  1. 1.Department of Biological ChemistryUniversity of Maryland School of MedicineBaltimoreUSA
  2. 2.Instituto de Ciencias Biomedicas, Departamento de BioquimicaUniversidade Federal do Rio de JaneiroRio de JaneiroBrasil

Personalised recommendations