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Postmortem degradation of dystrophin from bass (Dicentrarchus labrax) white muscle.

Author(s) : PAPA I., VENTRE F., LEBART M. C., ROUSTAN C., BENYAMIN Y.

Summary

The authors studied Z-disk disintegration by means of alpha-actinin follow during storage of fish muscle. This protein, a major component of the Z-disk, is released and degraded very rapidly during fish white muscle storage at 4 deg C. In order to better understand the mechanisms involved in muscle degradation, the authors studied costamere (dystrophin) behaviour after fish death. Dystrophin is the main protein of costameres, structure which binds myofibrils to sarcolemma. Here the authors report that: 1) dystrophin is degraded very rapidly during bass (D. labrax) white muscle storage at 4 deg C; 2) the total degradation of this protein occurs within 48 h in freshly slaughtered bass, but only some hours (8 h) in muscle that have been frozen for two or six months; 3) the antibody utilized to follow dystrophin degradation is not species-specific. That means that it can be used for the study of dystrophin in other fish.

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Details

  • Original title: Postmortem degradation of dystrophin from bass (Dicentrarchus labrax) white muscle.
  • Record ID : 1997-0960
  • Languages: English
  • Source: Refrigeration and Aquaculture.
  • Publication date: 1996/03/20
  • Document available for consultation in the library of the IIR headquarters only.

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