On the Intensity Reversal of the “Tropomyosin Reflexions” in X-ray Diffraction Patterns from Crab Striated Muscle

  • Yuichiro Maéda
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 37)


X-ray diffraction patterns have been recorded from skinned single fibres obtained from crab leg muscle, and the outer parts of layer-lines indexed as orders of 38.5 nm, which have been assigned to tropomyosin and actin, were examined. Fibres at normal length in the presence of ATP (γ-S), and overstretched fibres in rigor solutions, show no intensity reversal of the 2nd and the 3rd layer-lines when the Ca2+ concentration is raised. The results are discussed with reference to the mechanism of Ca2+ regulation.

Fibres in the presence of Mg-ADP and vanadate ion (Vi) and fibres pretreated at low pH, though generating no substantial tension at high Ca2+ concentration, give rise to rigor-like patterns which are dependent on Ca2+ concentration.


Thin Filament Sarcomere Length Adenylate Kinase Myosin Head Thick Filament 
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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Yuichiro Maéda
    • 1
  1. 1.Department of BiophysicsMax-Planck-Institute for Medical ResearchHeidelbergGermany

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