| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain
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| Autores: |
Verrez-bagnis, Veronique
Delbarre Ladrat, Christine
Noel, Joelle
Fleurence, Joel
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| Data: |
2002-09
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| Ano: |
2002
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| Palavras-chave: |
Dicentrarchus labrax L
Proteolysis
Sarcoplasmic protein
Calpain
Myofibrillar protein
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| Resumo: |
The effects of m-calpain isolated from the skeletal muscle of sea bass on sarcoplasmic and myofibrillar proteins isolated from the same tissue were examined in vitro. Incubation of sarcoplasmic proteins with m-calpain resulted in only a slight decrease (0.7 kDa) in the molecular weight (MW) of a 26.5 kDa protein. Degradation of myofibrils, monitored by quantification of TCA-soluble peptides generated, resulted in the maximum amount of peptides being generated after 1 h of incubation at 25degreesC. Noticeable modifications in the SDS-PAGE profile of digested myofibrils were observed, including partial denaturation of myosin heavy chain and the release of tropomyosin, similar to69 and similar to27 kDa doublet bands and a few polypeptides of MW lower than 20 kDa in the soluble fraction. Examination of the degradation patterns of myofibrillar proteins using Western blotting showed that alpha-actinin was partially degraded, with release of native alpha-actinin and its fragments from myofibrils, whereas desmin was highly degraded after 2h of digestion. (C) 2002 Society of Chemical Industry.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
http://archimer.ifremer.fr/doc/2002/publication-1108.pdf
DOI:10.1002/jsfa.1172
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| Editor: |
Wiley inter-science
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| Relação: |
http://archimer.ifremer.fr/doc/00000/1108/
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| Formato: |
application/pdf
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| Fonte: |
Journal of the science of food and agriculture (0022-5142) (Wiley inter-science), 2002-09 , Vol. 82 , N. 11 , P. 1256-1262
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| Direitos: |
2002 Society of Chemical Industry
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