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Histochemistry

, 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
Article

Summary

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.

Keywords

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

EGTA

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

SDS

sodium dodecylsulfate

PAGE

polyacrylamide gel electrophoresis

TEMED

N, N, N′, N′-tetramethylenediamine

TRIS

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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