||Verrez-Bagnis Veronique, Delbarre Ladrat Christine, Noel Joelle, Fleurence Joel
||IFREMER, Lab Prot Biochem & Qual, F-44311 Nantes 3, France.
||Journal of the science of food and agriculture (0022-5142) (Wiley inter-science), 2002-09 , Vol. 82 , N. 11 , P. 1256-1262
|WOS© Times Cited
||Dicentrarchus labrax L, Proteolysis, Sarcoplasmic protein, Calpain, Myofibrillar protein
||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.