Advertisement

Dynamic Laser Light Scattering of Papain-Treated Thick Filaments from Limulus Striated Muscle in Suspension

  • S-F. Fan
  • M. M. Dewey
  • D. Colflesh
  • P. Brink
  • B. Chu
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 37)

Abstract

Using quasielastic light scattering we have previously shown an increase in high frequency internal motion of isolated thick filament upon activation. This we have attributed to cross-bridge motion.Here we show that after cleavage of the S1 moiety of myosin from isolated filaments with papain, calcium ions no longer activate the isolated filaments to produce high-frequency motions.

Keywords

Thick Filament Myosin ATPase Relaxing Solution Myosin Subfragment Dynamic Laser Light Scattering 
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. Fan, S-F, (1964). Shortening in Congo Red solution of myofibrils isolated from glycerinated muscle fibers. Scientia Sinica. 13: 692–693.PubMedGoogle Scholar
  2. Fan, S-F. and Wen, Y-S. (1979). Concerning the binding sites of myofibril with Congo Red and dichroism change with myofibril length of Congo Red stained glycerinated sartorius muscle fibers. Acta Physiol. Sinica. 31: 227–238.Google Scholar
  3. Goodno, C.C. (1979). Inhibition of myosin ATPase by vanadate ion. Proc. Natl. Acad. Sci. U.S.A. 76: 2629–2634.CrossRefGoogle Scholar
  4. Goodno, C.C. and Taylor, E.W. (1982). Inhibition of actomyosin ATPase by vandate. ibid., 79: 21–25.Google Scholar
  5. Huxley, H.E. (1972). Structural changes in the actin and myosin containing filaments during contraction. Cold Spring Harb. Symp. Quant. Biol. 37: 361–376.CrossRefGoogle Scholar
  6. Koninz, D.P., Mitchell, F.R., Niekei, T. and King, C.M. (1985). The papain digestion of skeletal myosin A. Biochemistry. 4: 2373–2381.CrossRefGoogle Scholar
  7. Kubota, K., Chu, B., Fan, S-F., Dewey, M.M., Brink, P. and Colflesh, D. Quasi-elastic light scattering of suspensions of Lin - Lulus thick myofilaments in relaxed (long), activated and re-relaxed (short) states. Submitted to J. Mol. Biol.Google Scholar
  8. Maeda, T. and Fujirni, S. (1981). Effect of filament flexibility on the dynamic light scattering spectrum with special reference to fd virus and muscle thin filaments. Macromolecules. 14: 809–818.CrossRefGoogle Scholar
  9. Newman, J., Swinney, H.L. and Day, L.A. (1977). Hydrodynamic properties and structure of fd virus. J. Mol. Biol. 116: 593–606.PubMedCrossRefGoogle Scholar
  10. Yamanaotoik, K. and Schiao, T. (1980). Substructure of myosin subfragment (as revealed by digestion with proteolytic enzymes). J. Biochem. ( Tokyo ). 87: 219–226.Google Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • S-F. Fan
    • 1
  • M. M. Dewey
    • 1
  • D. Colflesh
    • 1
  • P. Brink
    • 1
  • B. Chu
    • 2
  1. 1.Department of Anatomical SciencesHealth Sciences CenterStony BrookUSA
  2. 2.Department of ChemistryState University of New York at Stony BrookStony BrookUSA

Personalised recommendations