Data/hora: 27/07/2024 02:51:49

Provedor de dados: 	5	
País: 	France	
Título: 	In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain	
Autores: 	Verrez-bagnis, Veronique; Delbarre Ladrat, Christine; Noel, Joelle; Fleurence, Joel.	
Data: 	2002-09	
Ano: 	2002	
Palavras-chave: 	Dicentrarchus labrax L; Proteolysis; Sarcoplasmic protein; Calpain; Myofibrillar protein.	
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.	
Tipo: 	Text	
Idioma: 	Inglês	
Identificador: 	http://archimer.ifremer.fr/doc/2002/publication-1108.pdf

DOI:10.1002/jsfa.1172	
Editor: 	Wiley inter-science	
Relação: 	http://archimer.ifremer.fr/doc/00000/1108/	
Formato: 	application/pdf	
Fonte: 	Journal of the science of food and agriculture (0022-5142) (Wiley inter-science), 2002-09 , Vol. 82 , N. 11 , P. 1256-1262	
Fonte: 	2002 Society of Chemical Industry