In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain

Type Article
Date 2002-09
Language English
Author(s) Verrez-Bagnis VeroniqueORCID, Delbarre Ladrat ChristineORCID, Noel Joelle, Fleurence Joel
Affiliation(s) IFREMER, Lab Prot Biochem & Qual, F-44311 Nantes 3, France.
Source Journal of the science of food and agriculture (0022-5142) (Wiley inter-science), 2002-09 , Vol. 82 , N. 11 , P. 1256-1262
DOI 10.1002/jsfa.1172
WOS© Times Cited 31
Keyword(s) Dicentrarchus labrax L, Proteolysis, Sarcoplasmic protein, Calpain, Myofibrillar protein
Abstract 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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Verrez-Bagnis Veronique, Delbarre Ladrat Christine, Noel Joelle, Fleurence Joel (2002). In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain. Journal of the science of food and agriculture, 82(11), 1256-1262. Publisher's official version : https://doi.org/10.1002/jsfa.1172 , Open Access version : https://archimer.ifremer.fr/doc/00000/1108/