Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1976 Mar 1;68(3):497–511. doi: 10.1083/jcb.68.3.497

Quantitative studies on the polarization optical properties of striated muscle. I. Birefringence changes of rabbit psoas muscle in the transition from rigor to relaxed state

PMCID: PMC2109640  PMID: 16016

Abstract

The changes in birefringence in the rigor to relax transition of single triton-extracted rabbit psoas muscle fibers have been investigated with quantitative polarized light techniques. The total birefringence of rest lenght fibers in rigor was (1.46 +/- 0.08) x 10(-3) and increased to (1.67 +/- 0.05) x 10(-3) after Mg-ATP relaxation. Pyrophosphate relaxation increased the total birefringence only slightly, whereas subsequent Mg-ATP relaxation elicited the maximum increase in birefringence. Changes in lattice spacing did not account for the total increase in birefrigence during relaxation. Moreover, the increase in total birefringence was attributable to increases in intrinsic birefringence as well as form birefringence. No change in birefringence was exhibited upon exposure to a relaxation solution after myosin extraction. Synthetic myosin filaments were prepared and treated with relaxation and rigor solutions. The negatively stained filaments treated with a rigor solution had gross irregular projections at either end, while the filaments treated with a relaxing solution were more spindle shaped. The results are compatible with the view that the subfragment-2 moieties of myosin angle away from the myosin aggregates (light meromyosin) to permit the attachment of the subfragment-1 moieties to actin.

Full Text

The Full Text of this article is available as a PDF (2.0 MB).

Selected References

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

  1. ALLEN R. D., BRAULT J., MOORE R. D. A NEW METHOD OF POLARIZATION MICROSCOPIC ANALYSIS. I. SCANNING WITH A BIREFRINGENCE DETECTION SYSTEM. J Cell Biol. 1963 Aug;18:223–235. doi: 10.1083/jcb.18.2.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cassim J. Y., Tobias P. S., Taylor E. W. Birefringence of muscle proteins and the problem of structural birefringence. Biochim Biophys Acta. 1968 Dec 3;168(3):463–471. doi: 10.1016/0005-2795(68)90180-3. [DOI] [PubMed] [Google Scholar]
  3. Colby R. H. Intrinsic birefringence of glycerinated myofibrils. J Cell Biol. 1971 Dec;51(3):763–771. doi: 10.1083/jcb.51.3.763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. 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]
  5. HUXLEY A. F. Muscle structure and theories of contraction. Prog Biophys Biophys Chem. 1957;7:255–318. [PubMed] [Google Scholar]
  6. HUXLEY H. E., HANSON J. Quantitative studies on the structure of cross-striated myofibrils. I. Investigations by interference microscopy. Biochim Biophys Acta. 1957 Feb;23(2):229–249. doi: 10.1016/0006-3002(57)90325-6. [DOI] [PubMed] [Google Scholar]
  7. Haselgrove J. C. X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J Mol Biol. 1975 Feb 15;92(1):113–143. doi: 10.1016/0022-2836(75)90094-7. [DOI] [PubMed] [Google Scholar]
  8. Huxley A. F., Simmons R. M. Proposed mechanism of force generation in striated muscle. Nature. 1971 Oct 22;233(5321):533–538. doi: 10.1038/233533a0. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Huxley H. E. The mechanism of muscular contraction. Science. 1969 Jun 20;164(3886):1356–1365. doi: 10.1126/science.164.3886.1356. [DOI] [PubMed] [Google Scholar]
  11. KIELLEY W. W., HARRINGTON W. F. A model for the myosin molecule. Biochim Biophys Acta. 1960 Jul 15;41:401–421. doi: 10.1016/0006-3002(60)90037-8. [DOI] [PubMed] [Google Scholar]
  12. Kaminer B., Bell A. L. Myosin filamentogenesis: effects of pH and ionic concentration. J Mol Biol. 1966 Sep;20(2):391–401. doi: 10.1016/0022-2836(66)90070-2. [DOI] [PubMed] [Google Scholar]
  13. Lowey S., Goldstein L., Cohen C., Luck S. M. Proteolytic degradation of myosin and the meromyosins by a water-insoluble polyanionic derivative of trypsin: properties of a helical subunit isolated from heavy meromyosin. J Mol Biol. 1967 Feb 14;23(3):287–304. doi: 10.1016/s0022-2836(67)80106-2. [DOI] [PubMed] [Google Scholar]
  14. Lowey S., Slayter H. S., Weeds A. G., Baker H. Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J Mol Biol. 1969 May 28;42(1):1–29. doi: 10.1016/0022-2836(69)90483-5. [DOI] [PubMed] [Google Scholar]
  15. Mendelson R. A., Morales M. F., Botts J. Segmental flexibility of the S-1 moiety of myosin. Biochemistry. 1973 Jun 5;12(12):2250–2255. doi: 10.1021/bi00736a011. [DOI] [PubMed] [Google Scholar]
  16. Moore P. L., Condeelis J. S., Taylor D. L., Allen R. D. A method for the morphological identification of contractile filaments in single cells. Exp Cell Res. 1973 Aug;80(2):493–495. doi: 10.1016/0014-4827(73)90332-7. [DOI] [PubMed] [Google Scholar]
  17. Nihei T., Mendelson R. A., Botts J. Use of fluorescence polarization to observe changes in attitude of S-1 moieties in muscle fibers. Biophys J. 1974 Mar;14(3):236–242. doi: 10.1016/S0006-3495(74)85911-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Rome E. Light and X-ray diffraction studies of the filament lattice of glycerol-extracted rabbit psoas muscle. J Mol Biol. 1967 Aug 14;27(3):591–602. doi: 10.1016/0022-2836(67)90061-7. [DOI] [PubMed] [Google Scholar]
  19. Rome E. Relaxation of glycerinated muscle: low-angle x-ray diffraction studies. J Mol Biol. 1972 Mar 28;65(2):331–345. doi: 10.1016/0022-2836(72)90285-9. [DOI] [PubMed] [Google Scholar]
  20. Rome E. X-ray diffraction studies of the filament lattice of striated muscle in various bathing media. J Mol Biol. 1968 Oct 28;37(2):331–344. doi: 10.1016/0022-2836(68)90272-6. [DOI] [PubMed] [Google Scholar]
  21. Sato H., Ellis G. W., Inoué S. Microtubular origin of mitotic spindle form birefringence. Demonstration of the applicability of Wiener's equation. J Cell Biol. 1975 Dec;67(3):501–517. doi: 10.1083/jcb.67.3.501. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Solaro R. J., Pang D. C., Briggs F. N. The purification of cardiac myofibrils with Triton X-100. Biochim Biophys Acta. 1971 Aug 6;245(1):259–262. doi: 10.1016/0005-2728(71)90033-8. [DOI] [PubMed] [Google Scholar]
  23. Spudich J. A., Huxley H. E., Finch J. T. Regulation of skeletal muscle contraction. II. Structural studies of the interaction of the tropomyosin-troponin complex with actin. J Mol Biol. 1972 Dec 30;72(3):619–632. doi: 10.1016/0022-2836(72)90180-5. [DOI] [PubMed] [Google Scholar]
  24. Taylor D. L., Allen R. D., Benditt E. P. Determination of the polarization optical properties of the amyloid-Congo red complex by phase modulation microspectrophotometry. J Histochem Cytochem. 1974 Dec;22(12):1105–1112. doi: 10.1177/22.12.1105. [DOI] [PubMed] [Google Scholar]
  25. Taylor D. L. Birefringence changes in vertebrate striated muscle. J Supramol Struct. 1975;3(2):181–191. doi: 10.1002/jss.400030212. [DOI] [PubMed] [Google Scholar]
  26. 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]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES