Skip to main content
NCBI home page
The Journal of General Physiology logoLink to The Journal of General Physiology
. 1977 Jan 1;69(1):37–55. doi: 10.1085/jgp.69.1.37

Tension generation by threads of contractile proteins

PMCID: PMC2215041  PMID: 137958

Abstract

Threads of contractile proteins were formed via extrusion and their isometric tensions and isotonic contraction velocities were measured. We obtained reproducible data by using a new and sensitive tensiometer. The force-velocity curves of actomyosin threads were similar to those of muscle, with isometric tensions of the order of 10g/cm2 and maximum contraction velocites of the order of 10(-2) lengths/s. The data could be fitted by Hill's equation. Addition of tropomyosin and troponin to the threads increased isometric tension and maximum contraction velocity. Threads which contained troponin and tropomyosin required Ca++ for contraction and the dependence of their isometric tension on the level of free Ca++ was like that of muscle. The dependence of tension or of contraction velocity upon temperature or upon ionic strength is similar for actomyosin threads and muscle fibers. In contrast, the dependence of most parameters which are characteristic of the actomyosin interaction in solution (or suspension) upon these variables is not similar to the dependence of the muscle fiber parameters. The conclusion we have drawn from these results is that the mechanism of tension generation in the threads is similar to the mechanism that exists in muscle. Because the protein composition of the thread system can be manipulated readily and because the tensions and velocities of the threads can be related directly to the physiological parameters of muscle fibers, the threads provide a powerful method for studying contractile proteins.

Full Text

The Full Text of this article is available as a PDF (1.5 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burke M., Reisler E., Himmelfarb S., Harrington W. F. Myosin adenosine triphosphatase. Convergence of activation by actin and by SH1 modification at physiological ionic strength. J Biol Chem. 1974 Oct 10;249(19):6361–6363. [PubMed] [Google Scholar]
  2. Bárány M. ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol. 1967 Jul;50(6 Suppl):197–218. doi: 10.1085/jgp.50.6.197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Close R. The relation between intrinsic speed of shortening and duration of the active state of muscle. J Physiol. 1965 Oct;180(3):542–559. doi: 10.1113/jphysiol.1965.sp007716. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cooke R. A new method for producing myosin subfragment-1. Biochem Biophys Res Commun. 1972 Nov 15;49(4):1021–1028. doi: 10.1016/0006-291x(72)90314-2. [DOI] [PubMed] [Google Scholar]
  5. Eisenberg E., Kielley W. W. Native tropomyosin: effect on the interaction of actin with heavy meromyosin and subfragment-1. Biochem Biophys Res Commun. 1970 Jul 13;40(1):50–56. doi: 10.1016/0006-291x(70)91044-2. [DOI] [PubMed] [Google Scholar]
  6. Gordon A. M., Godt R. E., Donaldson S. K., Harris C. E. Tension in skinned frog muscle fibers in solutions of varying ionic strength and neutral salt composition. J Gen Physiol. 1973 Nov;62(5):550–574. doi: 10.1085/jgp.62.5.550. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gordon A. M., Godt R. E. Some effects of hypertonic solutions on contraction and excitation-contraction coupling in frog skeletal muscles. J Gen Physiol. 1970 Feb;55(2):254–275. doi: 10.1085/jgp.55.2.254. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Greaser M. L., Gergely J. Purification and properties of the components from troponin. J Biol Chem. 1973 Mar 25;248(6):2125–2133. [PubMed] [Google Scholar]
  9. Greaser M. L., Gergely J. Reconstitution of troponin activity from three protein components. J Biol Chem. 1971 Jul 10;246(13):4226–4233. [PubMed] [Google Scholar]
  10. Hellam D. C., Podolsky R. J. Force measurements in skinned muscle fibres. J Physiol. 1969 Feb;200(3):807–819. doi: 10.1113/jphysiol.1969.sp008723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. IKEHARA M., OHTSUKA E., UNO H., IMAMURA K., TONOMURA Y. 3. INTERACTION BETWEEN SYNTHETIC ADENOSINE TRIPHOSPHATE ANALOGUES AND ACTOMYOSIN SYSTEMS. Biochim Biophys Acta. 1965 May 4;100:471–478. doi: 10.1016/0304-4165(65)90017-6. [DOI] [PubMed] [Google Scholar]
  12. JOHNSON P., ROWE A. J. The spontaneous transformation reactions of myosin. Biochim Biophys Acta. 1961 Oct 28;53:343–360. doi: 10.1016/0006-3002(61)90446-2. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Lännergren J., Noth J. Tension in isolated frog muscle fibers induced by hypertonic solutions. J Gen Physiol. 1973 Feb;61(2):158–175. doi: 10.1085/jgp.61.2.158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Mommaerts W. F. Energetics of muscular contraction. Physiol Rev. 1969 Jul;49(3):427–508. doi: 10.1152/physrev.1969.49.3.427. [DOI] [PubMed] [Google Scholar]
  16. Murphy R. A., Beardsley A. C. Mechanical properties of the cat soleus muscle in situ. Am J Physiol. 1974 Nov;227(5):1008–1013. doi: 10.1152/ajplegacy.1974.227.5.1008. [DOI] [PubMed] [Google Scholar]
  17. PORTZEHL H., CALDWELL P. C., RUEEGG J. C. THE DEPENDENCE OF CONTRACTION AND RELAXATION OF MUSCLE FIBRES FROM THE CRAB MAIA SQUINADO ON THE INTERNAL CONCENTRATION OF FREE CALCIUM IONS. Biochim Biophys Acta. 1964 May 25;79:581–591. doi: 10.1016/0926-6577(64)90224-4. [DOI] [PubMed] [Google Scholar]
  18. Reed K. C., Bygrave F. L. Methodology for in vitro studies of Ca-2+ transport. Anal Biochem. 1975 Jul;67(1):44–54. doi: 10.1016/0003-2697(75)90270-5. [DOI] [PubMed] [Google Scholar]
  19. Rizzino A. A., Barouch W. W., Eisenberg E., Moos C. Actin-heavy meromyosin biding. Determination of binding stoichiometry from adenosine triphosphatase kinetic measurements. Biochemistry. 1970 Jun 9;9(12):2402–2408. doi: 10.1021/bi00814a003. [DOI] [PubMed] [Google Scholar]
  20. Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
  21. Tada M. Adenosine triphosphatase activity and superprecipitation of canine cardiac myosin B. J Biochem. 1967 Dec;62(6):658–672. doi: 10.1093/oxfordjournals.jbchem.a128722. [DOI] [PubMed] [Google Scholar]
  22. Thames M. D., Teichholz L. E., Podolsky R. J. Ionic strength and the contraction kinetics of skinned muscle fibers. J Gen Physiol. 1974 Apr;63(4):509–530. doi: 10.1085/jgp.63.4.509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Tonomura Y., Appel P., Morales M. On the molecular weight of myosin. II. Biochemistry. 1966 Feb;5(2):515–521. doi: 10.1021/bi00866a017. [DOI] [PubMed] [Google Scholar]
  24. Tregear R. T., Squire J. M. Myosin content and filament structure in smooth and striated muscle. J Mol Biol. 1973 Jun 25;77(2):279–290. doi: 10.1016/0022-2836(73)90336-7. [DOI] [PubMed] [Google Scholar]
  25. Weber A., Murray J. M. Molecular control mechanisms in muscle contraction. Physiol Rev. 1973 Jul;53(3):612–673. doi: 10.1152/physrev.1973.53.3.612. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of General Physiology are provided here courtesy of The Rockefeller University Press

RESOURCES