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Proteolytic potential in white muscle of sea bass (Dicentrarchus labrax L.) during post mortem storage on ice: time-dependent changes in the activity of the components of the calpain system ArchiMer
Delbarre Ladrat, Christine; Verrez-bagnis, Veronique; Noel, Joelle; Fleurence, Joel.
The variations in the amounts of milli-calpain and its specific inhibitor in the white muscle of sea bass (Dicentrarchus labrax) during storage at 4 degreesC for up to 7 days were determined after separation by hydrophobic chromatography on a Phenyl Sepharose vel. There was a significant decline in post-slaughter m-calpain activity with an important inter-individual variability in the rate of decrease of the total activity. In contrast with the calpastatin of mammalian post mortem muscles, calpastatin remained constant within fish muscles after death. The initial levels of protease and inhibitor activities, and their behaviour through post mortem storage. are discussed and implications for the mechanism of tenderisation of fish muscle are suggested. (C)...
Tipo: Text Palavras-chave: Proteolysis; Post mortem; Fish muscle; Calpain; Calpastatin; Neutral calcium dependent protease.
Ano: 2004 URL: http://archimer.ifremer.fr/doc/2004/publication-1683.pdf
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Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.) ArchiMer
Delbarre Ladrat, Christine; Verrez-bagnis, Veronique; Noel, Joelle; Fleurence, Joel.
The effects of a milli(m)-calpain isolated from the white muscle of sea bass (Dicentrarchus labrax L) and commercial cathepsins B, D and L, used in combination on the myofibrillar and sarcoplasmic proteins were examined. Protein digestion was first performed by the endogenous m-calpain, (luring 2 h before the addition of a mixture of cathepsins B, D and L and a further incubation up to 22 h. Calpain degraded a 27 kDa sarcoplasmic component as well as myosin heavy chain, a-actinin, desmin and a 32 kDa component from the myofibrillar fraction. A 97 kDa component and the assumed creatine kinase-aldolase doublet were degraded during the incubation of sarcoplasmic proteins with the cathepsin mixture while, among the myofibrillar proteins, myosin, actin,...
Tipo: Text Palavras-chave: Postmortem aging; Fish muscle; Proteolysis; Cathepsins; Neutral calcium dependent protease.
Ano: 2004 URL: http://archimer.ifremer.fr/doc/2004/publication-1682.pdf
Registros recuperados: 2
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