Data/hora: 27/07/2024 02:07:48

Provedor de dados: 	5	
País: 	France	
Título: 	AMP-deaminase in elasmobranch fish: A comparative histochemical and enzymatic study	
Autores: 	Thebault, Marie-t; Izem, Lahoucine; Leroy, Jean Paul; Gobin, Eric; Charrier, Gregory; Raffin, Jean-paul.	
Data: 	2005-08	
Ano: 	2005	
Palavras-chave: 	White fibres; Red fibres; Muscle; Histology; Fish; Evolution; Elasmobranch; AMP deaminase.	
Resumo: 	AMP-deaminase activity was measured in white muscle from a wide range of fish, including one cyclostome, 13 chondrosteans, and one teleost to elucidate the pattern of the AMP-deaminase activity in white muscle of fish. Compared to a mammalian (rat) muscle extract, low enzyme activities are found in the cyclostome and two elasmobranchs from two families (Scyliorhinidae, Hexanchidae). In contrast, higher AMP-deaminase activities, similar to mammals, are expressed in Squalidae, all families of skates, Chimaeridae and in the teleostean fish. We then compared AMP-deaminase activities in red and white muscles from two representative elasmobranch fish, the dogfish (Scyliorhinus canicula) and the thornback ray (Raja clavata). The fibre type composition and distribution of the locomotory musculature were determined in these two elasmobranchs to establish a relationship between the morphology, the type of fibres of the locomotion-implicated muscles and the AMP-deaminase activity. Experimental data are discussed with respect to the layout of fibres in the myotome. In both species, three fibre types were identified. In the two fish myotomes, most of the axial muscles are white fibres while red fibres constitute a thin sheet. Some differences were observed between the two species in the distribution of intermediate fibres: in dogfish, these are located between the red and white fibres; in thornback ray, some are dispersed within the white fibre region, while others form an intermediary layer like in dogfish. These results suggest that in the course of evolution, an amplification of the AMP-deaminase activity in muscle was coupled with increase of complexity of the muscular structure.	
Tipo: 	Text	
Idioma: 	Inglês	
Identificador: 	http://archimer.ifremer.fr/doc/2005/publication-635.pdf

DOI:10.1016/j.cbpc.2005.05.009	
Editor: 	Elsevier	
Relação: 	http://archimer.ifremer.fr/doc/00000/635/	
Formato: 	application/pdf	
Fonte: 	Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology (1096-4959) (Elsevier), 2005-08 , Vol. 141 , N. 4 , P. 472-479	
Fonte: 	2005 Elsevier Inc. All rights reserved