Skip to main content
PMC home page
The Journal of General Physiology logoLink to The Journal of General Physiology
. 1976 Sep 1;68(3):267–280. doi: 10.1085/jgp.68.3.267

Two rigor states in skinned crayfish single muscle fibers

PMCID: PMC2228434  PMID: 821913

Abstract

We studied the tension and stiffness of crayfish skinned single muscle fibers during and after the induction of rigor by removal of MgATP (substrate). We found that the rigor state is not unique but depends on the condition of the muscle before rigor. Fibers induced into rigor with a minimum of activation (low rigor) develop a small tension and moderate stiffness, while those entering rigor during maximum activation (high rigor) maintain near peak tension (80%) and develop a high stiffness. These rigor states are insensitive to Ca addition or deletion but they are partially interconvertible by length change. Stiffness changes when the rigor muscle length is varied, a condition in which the number of attached cross-rigor muscle length is varied, a condition in which the number of attached cross-bridges cannot change, and high-rigor muscle becomes less stiff than low-rigor muscle when the former is brought to the same tension by length release. The sensitivity of low, high, or length-released high-rigor muscles to trace substrate concentration (less than muM) differs, and rigor at lower strain is more suscepitible to substrate.

Full Text

The Full Text of this article is available as a PDF (906.8 KB).

Selected References

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

  1. April E. W., Brandt P. W., Elliott G. F. The myofilament lattice: studies on isolated fibers. I. The constancy of the unit-cell volume with variation in sarcomere length in a lattice in which the thin-to-thick myofilament ratio is 6:1. J Cell Biol. 1971 Oct;51(1):72–82. doi: 10.1083/jcb.51.1.72. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BOZLER E. The effect of polyphosphates and magnesium on the mechanical properties of extracted muscle fibers. J Gen Physiol. 1956 May 20;39(5):789–800. doi: 10.1085/jgp.39.5.789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brandt P. W., Reuben J. P., Grundfest H. Regulation of tension in the skinned crayfish muscle fiber. II. Role of calcium. J Gen Physiol. 1972 Mar;59(3):305–317. doi: 10.1085/jgp.59.3.305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bremel R. D., Weber A. Cooperation within actin filament in vertebrate skeletal muscle. Nat New Biol. 1972 Jul 26;238(82):97–101. doi: 10.1038/newbio238097a0. [DOI] [PubMed] [Google Scholar]
  5. Dos Remedios C. G., Millikan R. G., Morales M. F. Polarization of tryptophan fluorescence from single striated muscle fibers. A molecular probe of contractile state. J Gen Physiol. 1972 Jan;59(1):103–120. doi: 10.1085/jgp.59.1.103. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ebashi S., Endo M. Calcium ion and muscle contraction. Prog Biophys Mol Biol. 1968;18:123–183. doi: 10.1016/0079-6107(68)90023-0. [DOI] [PubMed] [Google Scholar]
  7. Fabiato A., Fabiato F. Effects of magnesium on contractile activation of skinned cardiac cells. J Physiol. 1975 Aug;249(3):497–517. doi: 10.1113/jphysiol.1975.sp011027. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ford L. E., Huxley A. F., Simmons R. M. Proceedings: Mechanism of early tension recovery after a quick release in tetanized muscle fibres. J Physiol. 1974 Jul;240(2):42P–43P. [PubMed] [Google Scholar]
  9. Gordon A. M., Huxley A. F., Julian F. J. The variation in isometric tension with sarcomere length in vertebrate muscle fibres. J Physiol. 1966 May;184(1):170–192. doi: 10.1113/jphysiol.1966.sp007909. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Heinl P., Kuhn H. J., Rüegg J. C. Tension responses to quick length changes of glycerinated skeletal muscle fibres from the frog and tortoise. J Physiol. 1974 Mar;237(2):243–258. doi: 10.1113/jphysiol.1974.sp010480. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Huxley A. F. Muscular contraction. J Physiol. 1974 Nov;243(1):1–43. [PMC free article] [PubMed] [Google Scholar]
  12. Huxley H. E., Brown W. The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J Mol Biol. 1967 Dec 14;30(2):383–434. doi: 10.1016/s0022-2836(67)80046-9. [DOI] [PubMed] [Google Scholar]
  13. Huxley H. E. Structural difference between resting and rigor muscle; evidence from intensity changes in the lowangle equatorial x-ray diagram. J Mol Biol. 1968 Nov 14;37(3):507–520. doi: 10.1016/0022-2836(68)90118-6. [DOI] [PubMed] [Google Scholar]
  14. Inoue A., Shigekawa M., Tonomura Y. Direct evidence for the two route mechanism of the acto-H-meromyosin-ATPase reaction. J Biochem. 1973 Nov;74(5):923–934. [PubMed] [Google Scholar]
  15. Julian F. J., Sollins K. R., Sollins M. R. A model for the transient and steady-state mechanical behavior of contracting muscle. Biophys J. 1974 Jul;14(7):546–562. doi: 10.1016/S0006-3495(74)85934-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kawai M., Kuntz I. D. Optical diffraction studies of muscle fibers. Biophys J. 1973 Sep;13(9):857–876. doi: 10.1016/S0006-3495(73)86031-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Kuhn H. J., Schröder H., Rüegg J. C. Force generation in glycerinated insect-flight muscles without ATP. Experientia. 1972 May 15;28(5):510–511. doi: 10.1007/BF01931847. [DOI] [PubMed] [Google Scholar]
  18. Lymn R. W., Taylor E. W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 1971 Dec 7;10(25):4617–4624. doi: 10.1021/bi00801a004. [DOI] [PubMed] [Google Scholar]
  19. Lymn R. W., Taylor E. W. Transient state phosphate production in the hydrolysis of nucleoside triphosphates by myosin. Biochemistry. 1970 Jul 21;9(15):2975–2983. doi: 10.1021/bi00817a007. [DOI] [PubMed] [Google Scholar]
  20. Mulvany M. J. Mechanical properties of frog skeletal muscles in iodoacetic acid rigor. J Physiol. 1975 Nov;252(2):319–334. doi: 10.1113/jphysiol.1975.sp011146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Reedy M. K., Holmes K. C., Tregear R. T. Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle. Nature. 1965 Sep 18;207(5003):1276–1280. doi: 10.1038/2071276a0. [DOI] [PubMed] [Google Scholar]
  22. Reedy M. K. Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice. J Mol Biol. 1968 Jan 28;31(2):155–176. doi: 10.1016/0022-2836(68)90437-3. [DOI] [PubMed] [Google Scholar]
  23. Reuben J. P., Brandt P. W., Berman M., Grundfest H. Regulation of tension in the skinned crayfish muscle fiber. I. Contraction and relaxation in the absence of Ca (pCa is greater than 9). J Gen Physiol. 1971 Apr;57(4):385–407. doi: 10.1085/jgp.57.4.385. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Thorson J., White D. C. Distributed representations for actin-myosin interaction in the oscillatory contraction of muscle. Biophys J. 1969 Mar;9(3):360–390. doi: 10.1016/S0006-3495(69)86392-7. [DOI] [PMC free article] [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]
  26. Weber A. Parallel response of myofibrillar contraction and relaxation to four different nucleoside triphophates. J Gen Physiol. 1969 Jun;53(6):781–791. doi: 10.1085/jgp.53.6.781. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. White D. C. Rigor contraction and the effect of various phosphate compounds on glycerinated insect flight and vertebrate muscle. J Physiol. 1970 Jul;208(3):583–605. doi: 10.1113/jphysiol.1970.sp009138. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. White D. C., Thorson J. Phosphate starvation and the nonlinear dynamics of insect fibrillar flight muscle. J Gen Physiol. 1972 Sep;60(3):307–336. doi: 10.1085/jgp.60.3.307. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES