Abstract
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.
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© 1984 Plenum Press, New York
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Maéda, Y. (1984). On the Intensity Reversal of the “Tropomyosin Reflexions” in X-ray Diffraction Patterns from Crab Striated Muscle. In: Pollack, G.H., Sugi, H. (eds) Contractile Mechanisms in Muscle. Advances in Experimental Medicine and Biology, vol 37. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4703-3_22
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DOI: https://doi.org/10.1007/978-1-4684-4703-3_22
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