Advertisement

Calcium Binding to Troponin C and the Regulation of Muscle Contraction: a Comparative Approach

Part of the Proceedings in Life Sciences book series (LIFE SCIENCES)

Abstract

Muscle contraction consists of the cyclic attachment and detachment of the heads of myosin in the thick filament to actin in the thin filament. The attachment is followed by a change in the angle of myosin-actin attachment, so that the thick and thin filaments slide past each other and contractile force is generated. The energy for this process is supplied by ATP and is released by the interaction of actin with myosin, which activates the ATPase activity of myosin. The regulation of the actin-myosin-ATP interaction has been studied by analyzing the actin-activated myosin ATPase activity, which is the in vitro correlate of muscle contraction (Taylor 1979; Adelstein and Eisenberg 1980).

Keywords

Calcium Binding Thin Filament Myosin Head Rabbit Skeletal Muscle Fast Skeletal Muscle 
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. Adelstein RS, Eisenberg E (1980) Regulation and kinetics of the actin-myosin-ATP interaction. Ann Rev Biochem 49:921–956PubMedCrossRefGoogle Scholar
  2. Babu YS, Sack JS, Greehough TJ, Bugg CE, Means AR, Cook WJ (1985) Three-dimensional structure of calmodulin. Nature (Lond) 315:37–40CrossRefGoogle Scholar
  3. Benzonana G, Kohler L, Stein EA (1974) Regulatory proteins of crayfish tail muscle. Biochim Biophys Acta 638:247–258Google Scholar
  4. Best PM, Donaldson SKB, Kerrick WGL (1977) Tension in mechanically disrupted mammalian cardiac cells: effects of magnesium adenosine triphosphate. J Physiol 265:1–17PubMedGoogle Scholar
  5. Brandt PW, Cox RN, Kawai M (1980) Can the binding of Ca2+ to two regulatory sites on troponin C determine the steep pCa/tension relationship of skeletal muscle? Proc Natl Acad Sci USA 77: 4717–4720PubMedCrossRefGoogle Scholar
  6. Brandt PW, Diamond MS, Schachat FH (1984) The thin filament of vertebrate skeletal muscle cooperatively activates as a unit. J Mol Biol 180:379–384PubMedCrossRefGoogle Scholar
  7. Bremel RD, Weber A (1972) Cooperation within actin filament in vertebrate skeletal muscle. Nature New Biol 238:97–101PubMedGoogle Scholar
  8. Brinley FJ, Scarpa A, Tiffert T (1977) The concentration of ionized magnesium in barnacle muscle fibers. J Physiol 266:545–565PubMedGoogle Scholar
  9. Bullard B, Dabrowska R, Winkelman L (1973) The contractile and regulatory proteins of insect flight muscle. Biochem J 135:277–286PubMedGoogle Scholar
  10. Chalovich JM, Eisenberg E (1982) Inhibition of actomyosin ATPase activity without blocking the binding of myosin to actin. J Biol Chem 257:2432–2437PubMedGoogle Scholar
  11. Chantier P (1982) Retreats from the steric blocking of muscle contraction. Nature (Lond) 198: 120–121CrossRefGoogle Scholar
  12. Collins JH, Potter JD, Horn MJ, Wilshire G, Jackman N (1973) The amino acid sequence of rabbit skeletal muscle troponin C: gene replication and homology with calcium-binding proteins from carp and hake muscle. FEBS Lett 36:268–272PubMedCrossRefGoogle Scholar
  13. Collins JH, Greaser ML, Potter JD, Horn MJ (1977) Determination of the amino acid sequence of troponin C from rabbit skeletal muscle. J Biol Chem 252:6356–6362Google Scholar
  14. Cox JA, Comte M, Stein EA (1981) Calmodulin-free skeletal-muscle troponin C prepared in the absence of urea. Biochem J 195:205–211PubMedGoogle Scholar
  15. Dabrowska R, Sherry JMF, Aromatorio DK, Hartshorne DJ (1978) Modulator protein as a component of the myosin light chain kinase from chicken gizzard. Biochemistry 17:253–258PubMedCrossRefGoogle Scholar
  16. Donaldson SKB, Kerrick WGL (1975) Characterization of effects of Mg2+ on Ca2+- and Sr2+-activated tension generation of skinned skeletal muscle fibers. J Gen Physiol 66:427–444PubMedCrossRefGoogle Scholar
  17. Ebashi S, Endo M (1968) Calcium ions and muscle contraction. Progr Biophys Mol Biol 18:123–183CrossRefGoogle Scholar
  18. Ebashi S, Endo M, Ohtsuki I (1969) Control of muscle contraction. Quart Rev Biophys 2:351–384CrossRefGoogle Scholar
  19. Eisenberg E, Hill TL (1985) Muscle contraction and free energy transduction in biological systems. Science 227:999–1006PubMedCrossRefGoogle Scholar
  20. Eisenberg E, Kielley WW (1974) Troponin-tropomyosin complex. Column chromatography separation and activity of the three active troponin components with and without tropomyosin present. J Biol Chem 249:4742–4748PubMedGoogle Scholar
  21. Endo T, Obinata T (1981) Troponin and its components from ascidian smooth muscle. J Biochem (Tokyo) 89:1599–1608Google Scholar
  22. Evans JS, Levine BA, Leavis PC, Gergely J, Grabarek Z, Drabikowski W (1980) Proton magnetic resonance studies on proteolytic fragments of troponin C. Structural homology with the native protein. Biochim Biophys Acta 623:10–20PubMedGoogle Scholar
  23. Fabiato A, Fabiato F (1975) Effects of magnesium on contractile activation of skinned cardiac cells. J Physiol 249:497–517PubMedGoogle Scholar
  24. Fuchs F (1977) The binding of calcium to glycerinated muscle fibers in rigor. The effect of filament overlap. Biochim Biophys Acta 491:523–531PubMedGoogle Scholar
  25. Fuchs F, Black B (1980) The effects of magnesium ions on the binding of calcium ions to glycerinated rabbit psoas muscle fibers. Biochim Biophys Acta 622:52–62PubMedGoogle Scholar
  26. Godt RE (1974) Calcium-activated tension of skinned muscle fibers of the frog. Dependence on magnesium adenosine triphosphate concentration. J Gen Physiol 63:722–739PubMedCrossRefGoogle Scholar
  27. Goldberg A, Lehman W (1978) Troponin-like proteins from muscles of the scallop, Aequipecten irradians. Biochem J 171:413–418PubMedGoogle Scholar
  28. Goodman M, Pechère JF, Haiech J, Demaille JG (1979) Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins. J Mol Evol 13:331–352PubMedCrossRefGoogle Scholar
  29. Grabarek Z, Drabikowski W, Vinokurov L, Lu RC (1981a) Digestion of troponin C with trypsin in the presence and absence of Ca2+. Identification of cleavage points. Biochim Biophys Acta 671:227–233PubMedGoogle Scholar
  30. Grabarek Z, Drabikowski W, Leavis PC, Rosenfeld SS, Gergely J (1981b) Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity. J Biol Chem 256:13121–13127PubMedGoogle Scholar
  31. Grabarek Z, Grabarek J, Leavis PC, Gergely J (1983) Cooperative binding to the Ca2+-specific sites of troponin C in regulated actin and actomyosin. J Biol Chem 258:14098–14102PubMedGoogle Scholar
  32. Grabarek Z, Leavis PC, Gergely J (1986) Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain. A possible route of information transfer in activation of muscle contraction. J Biol Chem 261:608–613PubMedGoogle Scholar
  33. Graeser ML, Gergely J (1971) Reconstitution of troponin activity from three protein components. J Biol Chem 246:4226–4233Google Scholar
  34. Greene LE, Eisenberg E (1980) Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc Natl Acad Sci USA 77:2616–2620PubMedCrossRefGoogle Scholar
  35. Gupta RK, Moore RD (1980) 31P-NMR studies of intracellular free Mg2+ in intact frog skeletal muscle. J Biol Chem 255:3987–3992PubMedGoogle Scholar
  36. Hanson J (1968) Recent X-ray diffraction studies of muscle. Quart Rev Biophys 1:177–216CrossRefGoogle Scholar
  37. Hanson J, Lowy J (1962) The structure of F-actin and of actin filaments isolated from muscle. J Mol Biol 6:46–60CrossRefGoogle Scholar
  38. Hartshorne DJ, Siemankowski R (1981) Regulation of smooth muscle actomyosin. Ann Rev Physiol 43:519–530CrossRefGoogle Scholar
  39. Haselgrove JC (1972) X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring Harbor Symp Quant Biol 37:341–352Google Scholar
  40. Herzberg O, James MNG (1985a) Structure of the calcium regulatory muscle protein troponin C at 2.8 Å resolution. Nature (Lond) 313:653–659CrossRefGoogle Scholar
  41. Herzberg O, James MNG (1985b) Common structural framework of the two Ca2+/Mg2+ binding loops of troponin C and other Ca2+ binding proteins. Biochemistry 24:5298–5302PubMedCrossRefGoogle Scholar
  42. Herzberg O, Moult J, James MNG (1986) A model for the Ca2+-induced conformational transition of troponin C. A trigger for muscle contraction. J Biol Chem 261:2638–2644PubMedGoogle Scholar
  43. Hill TL (1983) Two elementary models for the regulation of skeletal muscle contraction by calcium. Biophys J 44:383–396PubMedCrossRefGoogle Scholar
  44. Hill TL, Eisenberg E, Chalovich JM (1981) Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin. Biophys J 35:99–112PubMedCrossRefGoogle Scholar
  45. Hincke MT, Sykes BD, Kay CM (1981) Hydrogen-1 nuclear magnetic resonance investigation of bovine cardiac troponin C. Comparison of tyrosyl assignments and calcium-induced structural changes to those of two homologous proteins, rabbit skeletal troponin C and bovine brain calmodulin. Biochemistry 20:3286–3294PubMedCrossRefGoogle Scholar
  46. Hoar PE, Wnuk W, Kerrick WGL (1985) Crayfish troponin C can substitute for the endogenous troponin C of skinned rabbit skeletal muscle fibers. Biophys J 47:61aGoogle Scholar
  47. Holroyde MJ, Robertson SP, Johnson JD, Solaro RJ, Potter JD (1980) The calcium and magnesium binding sites on cardiac troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem 255:11688–11693PubMedGoogle Scholar
  48. Huxley HE (1972) Structural changes in the actin- and myosin-containing filaments of vertebrate striated muscle. Cold Spring Harbor Symp Quant Biol 37:361–376Google Scholar
  49. Irving M (1985) Weak and strong crossbridges. Nature (Lond) 316:292–293CrossRefGoogle Scholar
  50. Johnson JD, Charlton SC, Potter JD (1979) A fluorescence stopped-flow analysis of Ca2+ exchange with troponin C. J Biol Chem 254:3497–3502PubMedGoogle Scholar
  51. Johnson JD, Robinson DE, Robertson SP, Schwartz A, Potter JD (1981) Ca2+ exchange with troponin and the regulation of muscle contraction. In: Grinnel A (ed) The regulation of muscle contraction: excitation-contraction coupling. Acadmic Press, New York, pp 241–259Google Scholar
  52. Kawasaki Y, Van Eerd JP (1972) The effect of Mg2+ on the conformation of the Ca2+-binding component of troponin. Biochim Biophys Res Commun 49:898–905CrossRefGoogle Scholar
  53. Kendrick-Jones J, Scholey JM (1981) Myosin-linked regulatory systems. J Muscle Res Cell Motil 2:347–362CrossRefGoogle Scholar
  54. Kerrick WGL, Bolles LL (1981) Regulation of Ca2+-activated tension in Limulus striated muscle. Pflügers Arch 392:121–124PubMedCrossRefGoogle Scholar
  55. Kerrick WGL, Hoar PE (1985) The effects of nucleotide diphosphate and inorganic phosphate on tension in skinned soleus and smooth muscle cells. Biophys J 47:296a Klee CB, Vanaman TC (1982) Calmodulin. Adv Prot Chem 35:213–321Google Scholar
  56. Konno K (1978) Two calcium regulation systems in squid muscle. Preparation of calcium-sensitive myosin and troponin-tropomyosin. J Biochem (Tokyo) 84:1431–1440Google Scholar
  57. Leavis PC, Gergely J (1984) Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit Rev Biochem 16:235–305PubMedCrossRefGoogle Scholar
  58. Leavis PC, Rosenfeld SS, Gergely J, Grabarek Z, Drabikowski W (1978) Proteolytic fragments of troponin C. J Biol Chem 253:5452–5459PubMedGoogle Scholar
  59. Lehman W (1975) Hybrid troponin reconstituted from vertebrate and arthropod subunits. Nature (Lond) 255:424–426CrossRefGoogle Scholar
  60. Lehman W (1982) The location and periodicity of a troponin-T-like protein in the myofibril of the horseshoe crab. J Mol Biol 154:385–391PubMedCrossRefGoogle Scholar
  61. Lehman W, Ferrell M (1980) Phylogenetic diversity of troponin subunit-C amino acid composition. FEBS Lett 121:273–274PubMedCrossRefGoogle Scholar
  62. Lehman W, Szent-Györgyi AG (1975) Regulation of muscular contraction. Distribution of actin control and myosin control in the animal kingdom. J Gen Physiol 66:1–30PubMedCrossRefGoogle Scholar
  63. Lehman W, Head JF, Grant PW (1980) The stoichimetry and location of troponin I- and troponin C-like proteins in the myofibril of the bay scallop, Aequipecten irradions. Biochem J 187: 447–456PubMedGoogle Scholar
  64. Levine BA, Thornton JM, Fernandes R, Kelly CM, Mercola D (1978) Comparison of the calcium-and magnesium-induced structural changes of troponin C. A proton magnetic resonance study. Biochim Biophys Acta 535:11–24PubMedGoogle Scholar
  65. Lymn RW, Taylor EW (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10:4617–4624PubMedCrossRefGoogle Scholar
  66. Miledi R, Parker I, Schalow G (1977) Measurements of calcium transients in frog muscle by the use of arsenazo (III). Proc R Soc Lond, Ser B 198:201–210Google Scholar
  67. Moews PG, Kretsinger RH (1975) Refinement of the structure of carp muscle calcium binding parvalbumin by model building and difference Fourier analysis. J Mol Biol 91:201–228PubMedCrossRefGoogle Scholar
  68. Murray JM, Weber A (1980) Cooperativity of the calcium switch of regulated rabbit actomyosin system. Mol Cell Biochem 35:11–15CrossRefGoogle Scholar
  69. Murray JM, Weber A, Knox MK (1981) Myosin subfragments binding to relaxed actin filaments and steric model of relaxation. Biochemistry 20:641–649PubMedCrossRefGoogle Scholar
  70. Nagashima H, Asakura S (1982) Studies on a co-operative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment 1. J Mol Biol 155:409–428PubMedCrossRefGoogle Scholar
  71. Nagy B, Gergely J (1979) Extent and localization of conformational changes in troponin C caused by calcium binding. Spectral studies in the presence and absence of 6 M urea. J Biol Chem 254:12732–12737PubMedGoogle Scholar
  72. Pearlstone JR, Carpenter MR, Johnson P, Smillie LB (1976) Amino-acid sequence of tropomyosin-binding component of rabbit skeletal muscle troponin. Proc Natl Acad Sci USA 73:1902–1906PubMedCrossRefGoogle Scholar
  73. Potter JD (1974) The content of troponin, tropomyosin, actin and myosin in rabbit skeletal muscle myofibrils. Arch Biochem Biophys 162:436–441PubMedCrossRefGoogle Scholar
  74. Potter JD, Gergely J (1975) The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem 250:4628–4633PubMedGoogle Scholar
  75. Potter JD, Johnson JD (1982) Troponin. In: Cheung WY (ed) Calcium and cell function Vol II. Academic Press, New York London, pp 145–173Google Scholar
  76. Potter JD, Robertson SP, Johnson JD (1981) Magnesium and regulation of muscle contraction. Fed Proc 49:2653–2656Google Scholar
  77. Regenstein JM, Szent-Györgyi AG (1975) Regulatory proteins of lobster striated muscle. Biochemistry 14:917–925PubMedCrossRefGoogle Scholar
  78. Reid RE, Hodges RS (1980) Cooperativity and calcium/magnesium binding to troponin C and muscle calcium binding parvalbumin: an hypothesis. J Theor Biol 84:401–444PubMedCrossRefGoogle Scholar
  79. Ridgway EB, Gordon AM, Martyn DA (1983) Histeresis in the force-caclium relation in muscle. Science 219:1075–1077PubMedCrossRefGoogle Scholar
  80. Robertson SP, Johnson JD, Potter JD (1981) The time-course of Ca2+ exchange with calmodulin, troponin, parvalbumin, and myosin in response to transient increases in Ca2+. Biophys J 34:559–569PubMedCrossRefGoogle Scholar
  81. Romero-Herrera AE, Cartillo O, Lehmann H (1976) Human skeletal muscle proteins. The primary structure of troponin C. J Mol Evol 8:251–270PubMedCrossRefGoogle Scholar
  82. Sin IL, Fernandes R, Mercola D (1978) Direct identification of the high and low affinity calcium binding sites of troponin C. Biochem Biophys Res Commun 82:1132–1139PubMedCrossRefGoogle Scholar
  83. Smillie LB (1979) Structure and functions of tropomyosins from muscle and non-muscle sources. Trends Biochem Sci 4:151–155CrossRefGoogle Scholar
  84. Solaro RJ, Shiner JS (1976) Modulation of Ca2+ control of dog and rabbit cardiac myofibrils by Mg2+. Comparison with rabbit skeletal myofibrils. Circ Res 39:8–14PubMedGoogle Scholar
  85. Sundaralingam M, Bergstrom R, Strasburg G, Rao ST, Roychowdhury P, Greaser M, Wang BC (1985a) Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution. Science 227:945–948PubMedCrossRefGoogle Scholar
  86. Sundaralingam M, Drendel W, Greaser M (1985b) Stabilization of the long central helix of troponin C by intrahelical salt bridges between charged amino acid side chains. Proc Natl Acad Sci USA 82:7944–7947PubMedCrossRefGoogle Scholar
  87. Szent-Györgyi AG, Szentkiralyi EM, Kendrick-Jones J (1973) The light chains of scallop myosin as regulatory subunits. J Mol Biol 74:179–203PubMedCrossRefGoogle Scholar
  88. Takagi T, Konishi K (1983) Amino acid sequence of troponin C obtained from ascidian (Halocynthia roretzi) body wall muscle. J Biochem (Tokyo) 94:1753–1760Google Scholar
  89. Taylor EW (1979) Mechanisms of actomyosin ATPase and the problem of muscle contraction. CRC Crit Rev Biochem 6:103–164PubMedCrossRefGoogle Scholar
  90. Trybus KM, Taylor EW (1980) Kinetic studies of the cooperative binding of subfragment 1 to regulated actin. Proc Natl Acad Sci USA 77:7209–7213PubMedCrossRefGoogle Scholar
  91. Tsuchiya T, Head JF, Lehman (1982) The isolation and characterization of a troponin C-like protein from the mantle muscle of the squid Loligo pealei. Comp Biochem Physiol 71B:507–509Google Scholar
  92. Van Eerd JP, Takahashi K (1976) Determination of the complete amino acid sequence of bovine cardiac troponin C. Biochemistry 15:1171–1180PubMedCrossRefGoogle Scholar
  93. Van Eerd JP, Capony JP, Ferraz C, Pechère JF (1978) The amino-acid sequence of troponin C from frog skeletal muscle. Eur J Biochem 91:231–242PubMedCrossRefGoogle Scholar
  94. Wagner P, Stone DB (1983) Calcium-sensitive binding of heavy meromyosin to regulated actin requires light chain 2 and the head-tail junction. Biochemistry 22:1334–1342PubMedCrossRefGoogle Scholar
  95. Wakabayashi T, Huxley HE, Amos LA, Klug A (1975) Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin I complex. J Mol Biol 93:477–497PubMedCrossRefGoogle Scholar
  96. Wang CK, Cheung HC (1985) Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle. Biophys J 48:727–739PubMedCrossRefGoogle Scholar
  97. Watanabe K, Kitaura T, Yamaguchi M (1982) Crayfish myosin has no Ca2+-dependent regulation in actomyosin. J Biochem (Tokyo) 92:1635–1641Google Scholar
  98. Watterson DM, Sharief F, Vanaman TC (1980) The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain. J Biol Chem 255:962–975PubMedGoogle Scholar
  99. Weber A, Murray JM (1973) Molecular control mechanisms in muscle contraction. Physiol Rev 53:612–673PubMedGoogle Scholar
  100. Weeds AG, McLachlan AD (1974) Structural homology of myosin alkali light chains, troponin C and carp calcium binding protein. Nature (Lond) 252:646–649CrossRefGoogle Scholar
  101. Wegner Y, Walsh TP (1981) Interaction of tropomyosin-troponin with actin filaments. Biochemistry 20:5633–5642PubMedCrossRefGoogle Scholar
  102. Wilkinson JM (1976) The amino acid sequence of troponin C from chicken skeletal muscle. FEBS Lett 70:254–256PubMedCrossRefGoogle Scholar
  103. Wilkinson JM (1980) Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene. Eur J Biochem 103:179–188PubMedCrossRefGoogle Scholar
  104. Wilkinson JM, Grand RJA (1975) The amino acid sequence of troponin I from rabbit skeletal muscle. Biochem J 149:493–496PubMedGoogle Scholar
  105. Wilkinson JM, Grand RJA (1978) Comparison of amino acid sequence of troponin I from different striated muscles. Nature (Lond) 271:31–35CrossRefGoogle Scholar
  106. Wnuk W, Stein EA (1978) Evolution of the Ca-binding properties of troponin C. Experientia 34:920Google Scholar
  107. Wnuk W, Stein EA (1980) Does the cooperative response of myofibrils to Ca2+ result from multiple Ca2+-sites on troponin C? In: Siegel FL, Carafoli E, Kretsinger RH, MacLennan DH, Wasserman RH (eds) Calcium binding proteins: structure and function. Elsevier North-Holland, New York, pp 343–344Google Scholar
  108. Wnuk W, Cox JA, Stein EA (1982) Parvalbumins and other soluble high-affinity calcium-binding proteins from muscle. In: Cheung WY (ed) Calcium and cell function. Vol II. Academic Press, New York London, pp 243–278Google Scholar
  109. Wnuk W, Schoechlin M, Stein EA (1984) Regulation of actomyosin ATPase by a single calcium-binding site on troponin C from crayfish. J Biol Chem 259:9017–9023PubMedGoogle Scholar
  110. Wnuk W, Schoechlin M, Kobayashi T, Takagi T, Konishi K, Hoar PE, Kerrick WGL (1986) Two isoforms of troponin C from crayfish. Their characterization and a comparison of their primary structure with the tertiary structure of skeletal troponin C. J Muscle Res Cell Motil 7:67Google Scholar
  111. Zot HG, Potter JD (1982) A structural role for the Ca2+-Mg2+ sites on troponin C in the regulation of muscle contraction. Preparation and properties of troponin C depleted myofibrils. J Biol Chem 257:7678–7683PubMedGoogle Scholar
  112. Zot HG, Potter JD (1984) The role of calcium in the regulation of the skeletal muscle contraction-relaxation cycle. In: Siegel H (ed) Metal Ions in biological systems. Vol XVII. Decker, New York Basel, pp 381–410Google Scholar
  113. Zot HG, Iida S, Potter JD (1983) Thin filament interactions and Ca2+ binding to Tn. Chem Scr 21:135–138Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1988

Authors and Affiliations

  • W. Wnuk
    • 1
  1. 1.Division de Gastroentérologie et NutritionHôpital Cantonal UniversitaireGenevaSwitzerland

Personalised recommendations