, Volume 60, Issue 1, pp 21–41 | Cite as

Supercontraction in crayfish muscle: Correlation with a peculiar actin localization

  • G. Benzonana
  • Ch. Campanella
  • G. Gabbiani


Crayfish muscle, like muscles from some other invertebrates, can supercontract. This muscle shortening is characterized by an overlap of thin filaments with crossing of thick filaments through the Z discs. In intact muscle cells, supercontraction does not seem to induce irreversible structural modifications in the tissue.

Isolated crayfish myofibrils in the relaxed state cannot be distinguished from vertebrate myofibrils under light microscope, either by phase contrast or by immunofluorescence, with antiactin antibodies, actin being localized in the I bands. However, when isolated crayfish myofibrils are supercontracted, irreversible dammage occurs, most thin filaments being lost. Actin becomes then hardly detectable, being visible, by immunofluorescence, either in the Z discs or evenly distributed in the whole myofibril.

During myofibril supercontraction, high amounts of denatured actin, become soluble as shown by SDS-PAGE, by double immunodiffusion, and by DNAse inhibition.


Public Health Muscle Cell Light Microscope Phase Contrast Structural Modification 
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.

Abbreviations used in the text


ethyleneglycol-bis (β-aminoethyl ether)-N, N′-tetraacetic acid


sodium dodecylsulfate


polyacrylamide gel electrophoresis


N, N, N′, N′-tetramethylenediamine


Tris (hydroxymethyl) aminomethane


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Copyright information

© Springer-Verlag 1979

Authors and Affiliations

  • G. Benzonana
    • 1
  • Ch. Campanella
    • 2
  • G. Gabbiani
    • 2
  1. 1.Department of BiochemistryUniversity of GenevaGeneva 4Switzerland
  2. 2.Department of PathologyUniversity of GenevaGeneva 4Switzerland

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