| Type |
Article |
| Date |
2002-09 |
| Language |
English |
| Author(s) |
Verrez-Bagnis Veronique , Delbarre Ladrat Christine, 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 |
33 |
| 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. |
| Full Text |
| File |
Pages |
Size |
Access |
| publication-1108.pdf |
14 |
375 KB |
Open access |
|
