FN Archimer Export Format
PT J
TI In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain
BT 
AF VERREZ-BAGNIS, Veronique
   DELBARRE LADRAT, Christine
   NOEL, Joelle
   FLEURENCE, Joel
AS 1:;2:;3:;4:;
FF 1:PDG-DRV-VP-BPQ;2:PDG-RBE-BRM-BMM;3:PDG-DRV-VP-BPQ;4:PDG-DRV-VP-BPQ;
C1 IFREMER, Lab Prot Biochem & Qual, F-44311 Nantes 3, France.
C2 IFREMER, FRANCE
SI NANTES
SE PDG-DRV-VP-BPQ
   PDG-RBE-BRM-BMM
IN WOS Ifremer jusqu'en 2018
IF 1.41
TC 33
UR https://archimer.ifremer.fr/doc/2002/publication-1108.pdf
LA English
DT Article
DE ;Dicentrarchus labrax L;Proteolysis;Sarcoplasmic protein;Calpain;Myofibrillar protein
AB 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.
PY 2002
PD SEP
SO Journal of the science of food and agriculture
SN 0022-5142
PU Wiley inter-science
VL 82
IS 11
UT 000177577200002
BP 1256
EP 1262
DI 10.1002/jsfa.1172
ID 1108
ER

EF