Journal of Muscle Research & Cell Motility

, Volume 4, Issue 2, pp 223–232 | Cite as

Myosin polymorphism in muscles of the toadfish,Opsanus tau

  • F. Huriaux
  • F. Lefebvre
  • B. Focant


The superfast swimbladder muscle ofOpsanus tau differs from the corresponding fast skeletal muscle not only by its greater sarcoplasmic reticulum and parvalbumin content but also by a genuine myosin LC2. The study of light chains has been extended here to other striated muscles. Myosins from fast (trunk muscle), superfast (swimbladder muscle), slow (lateral-line muscle) and cardiac (ventricle muscle) were compared, using one- and two-dimensional polyacrylamide gel electrophoresis. The results showed that the light chains all appear distinct in isoelectric point and molecular weight, except for the two LC1 and two LC3 from fast and superfast muscles. Striated muscles from the toadfishOpsanus tau exhibited at least four isoenzymic forms of the myosin, related to the light chains and corresponding to different physiological properties.


Striate Muscle Polyacrylamide Light Chain Sarcoplasmic Reticulum Isoelectric Point 
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.


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Copyright information

© Chapman and Hall Ltd 1983

Authors and Affiliations

  • F. Huriaux
    • 1
  • F. Lefebvre
    • 1
  • B. Focant
    • 1
  1. 1.Laboratoire de Biochimie MusculaireInstitut de Chimie B6, Université de Liège, Sart TilmanLiègeBelgium

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