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| Clop, A.; Marcq, F.; Takeda, H.; Pirottin, D.; Tordoir, X.; Bibé, B.; Bouix, J.; Caimen, F.; Elsen, J.M.; Eychenne, F.; Larzul, C.; Laville, E.; Meish, F.; Milenkovic, D.; Tobin, J.; Charlier, C.; Georges, M.. |
| Tipo: Journal Article |
Palavras-chave: TEXEL SHEEP; MYOSTATIN GENE; MUSCULARITY; HYPERTROPHY; GDF8; SNP. |
| Ano: 2006 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20087ed0d44b&uri=/notices/prodinra1/2008/09/ |
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| Laville, E.; Sayd, T.; Sante-Lhoutellier, V.; Morzel, M.; Labas, R.; Franck, M.; Chambon, C.; Monin, G.. |
| Pig semimembranosus muscles, sampled from normal hams or from PSE-zones of defective hams, were analysed by histochemistry and electrophoretic techniques. PSE zones were characterised by a disorganisation of fibre alignment and a significant increase of inter fibre spacing (26.2% vs. 16.9%, p < 0.05). Protein solubility was significantly lower in defective muscle (55.4 vs. 91.5 mg/g, p < 0.001). SDS-PAGE evidenced in such samples a lower abundance of the 97, 40 and 26 kDa bands in the sarcoplasmic fraction and a higher abundance of the 97, 58, 34, 31, 15 and 11 kDa bands in the myofibrillar fraction. Intensity of the MHC band (200 kDa) was lower in PSE zone samples. By 2-D electrophoresis, it was shown that troponin T, MLC 1 and alpha-crystallin were... |
| Tipo: Journal Article |
Palavras-chave: VIANDE PORCINE; JAMBON; VIANDE EXSUDATIVE; SOLUBILITE DES PROTEINES; HISTOCHIMIE; CHUTE DE PH; FIBRE MUSCULAIRE PIG; PSE-ZONES; PROTEINE SOLUBILITY. |
| Ano: 2005 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007d9efa252&uri=/notices/prodinra1/2007/07/ |
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| Laville, E.; Sayd, T.; Morzel, M.; Blinet, S.; Chambon, C.; Lepetit, J.; Renand, G.; Hocquette, J.F.. |
| Within a population of Charolais young bulls, two extreme groups of longissimus thoracis muscle samples, classified according to Warner−Bratzler shear force (WBSF) of 55 °C grilled meat, were analyzed by 2D-electrophoresis. Muscle analyses were performed on 4 bulls of the “tender” group (WBSF = 27.7 ± 4.8 N) and 4 bulls of the “tough” group (WBSF = 41.2 ± 6.1 N), at 3 post-mortem times: D0, samples taken within 10 min post-mortem; D5 and D21, samples kept at 4 °C under vacuum during 5 and 21 days. Proteins of muscle samples were separated in two fractions based on protein solubility in Tris buffer: “soluble” and “insoluble”. Proteins of both fractions were separated by 2D-electrophoresis. Evolution of spots during the 3 post-mortem times was analyzed by... |
| Tipo: Journal Article |
Palavras-chave: TENDRETE PROTEOME ANALYSIS; BEEF MUSCLE; TENDERNESS; HIERACHICAL CLUSTERING ANLYSIS; PROTEIN SOLUBILITY; PROTEOLYSIS; HSP27; GLYCOLYTIC ENZYMES; MITOCHONDRIAL MEMBRANE. |
| Ano: 2009 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010c73be391&uri=/notices/prodinra1/2010/06/ |
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