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Evaluation of a European sea bass (Dicentrarchus labrax L.) post-larval tagging method with ultra-small RFID tags ArchiMer
Faggion, Sara; Sanchez, Pierre; Vandeputte, Marc; Clota, Frederic; Vergnet, Alain; Blanc, Marie-odile; Allal, Francois.
Individual tagging is key to a better understanding of early life stages in fish. Very small RFID transponder microchips (500 × 500 × 100 μm, 82 μg) are now available. The aim of this study was to develop a protocol to tag European sea bass (Dicentrarchus labrax L.) larvae from 61 days post-hatching (dph; standard length ~10 mm) to 96 dph (standard length ~28 mm) through intra-coelomic implantation of microchips. The suitability of such a tagging procedure was evaluated, with the purpose of determining the minimal fish age and body size for microchip tagging without adverse effects on survival and growth performance. We produced an experimental population composed by 50:50 normally pigmented larvae and albino larvae through artificial fertilization. Five...
Tipo: Text Palavras-chave: Larvae; RFID transponder; Individual identification; Tagging effects; Dicentrarchus labrax L.
Ano: 2020 URL: https://archimer.ifremer.fr/doc/00601/71331/73084.pdf
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In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m-calpain ArchiMer
Verrez-bagnis, Veronique; Delbarre Ladrat, Christine; Noel, Joelle; Fleurence, Joel.
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...
Tipo: Text Palavras-chave: Dicentrarchus labrax L; Proteolysis; Sarcoplasmic protein; Calpain; Myofibrillar protein.
Ano: 2002 URL: http://archimer.ifremer.fr/doc/2002/publication-1108.pdf
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