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Fish Physiol Biochem. 2014 Feb;40(1):311-22. doi: 10.1007/s10695-013-9855-x. Epub 2013 Sep 21.

Proteomic profiling of sea bass muscle by two-dimensional gel electrophoresis and tandem mass spectrometry.

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  • 1Department of Biotechnology and Life Sciences (DBSV), University of Insubria, Via J. H. Dunant, 3, 21100, Varese, Italy, genciana.terova@uninsubria.it.

Abstract

In this study, the proteome profile of European sea bass (Dicentrarchus labrax) muscle was analyzed using two-dimensional electrophoresis (2-DE) and tandem mass spectrometry with the aim of providing a more detailed characterization of its specific protein expression profile. A highly populated and well-resolved 2-DE map of the sea bass muscle tissue was generated, and the corresponding protein identity was provided for a total of 49 abundant protein spots. Upon Ingenuity Pathway Analysis, the proteins mapped in the sea bass muscle profile were mostly related to glycolysis and to the muscle myofibril structure, together with other biological activities crucial to fish muscle metabolism and contraction, and therefore to fish locomotor performance. The data presented in this work provide important and novel information on the sea bass muscle tissue-specific protein expression, which can be useful for future studies aimed to improve seafood traceability, food safety/risk management and authentication analysis. This work is also important for understanding the proteome map of the sea bass toward establishing the animal as a potential model for muscular studies.

PMID:
24057758
DOI:
10.1007/s10695-013-9855-x
[PubMed - indexed for MEDLINE]
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