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A total of 383 barrows and gilts from a French Large White experimental herd were slaughtered at 100 kg BW. Samples of longissimus muscle were taken to categorize myofibers according to their contractile (I, IIA, and IIB) and metabolic (oxidative and nonoxidative) properties. Myofiber percentages, cross-sectional areas (CSA), and relative areas were measured. Growth rate, carcass composition, muscle chemical composition, metabolic enzyme activities, and meat quality traits were also measured to estimate phenotypic and genetic correlations between these traits and myofiber characteristics. Genetic parameters were estimated using a REML procedure applied to an individual animal model. Heritabilities of fiber traits were moderate to high (h2 = .20 to .59). Highest heritabilities were found for type I fiber percentage (h2 = .46 +/- .11), type IIBw fiber percentage (h2 = .58 +/- .11), and type I fiber cross-sectional area (h2 = .59 +/- .10). For a given fiber type, the relative area was phenotypically and genetically more closely related to the percentage than to the CSA. Phenotypic correlations between fiber type composition and other traits were low. Genetically, growth rate, carcass leanness, and loin eye area were positively related to fiber CSA. Intramuscular fat content was not related to fiber type composition (r(g) = -.05 to .06), whereas it was positively related to fiber CSA (r(g) = .68). Type IIBw fiber percentage was related to pH at 30 min (r(g) = -.46), pH at 24 h (r(g) = -.62), glycolytic potential (r(g) = .31), and lightness of color (r(g) = .55) of longissimus muscle.

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Two-dimensional electrophoresis was used to investigate sarcoplasmic protein expression in pig Semimembranosus muscles sampled 20 min after slaughter. Two groups (light and dark) of 12 animals were selected from 1000 pigs, based on meat L values measured 36 h postmortem. Twenty-two proteins or fragments (p < 0.05) were differentially expressed. Muscles leading to darker meat had a more oxidative metabolism, indicated by more abundant mitochondrial enzymes of the respiratory chain, hemoglobin, and chaperone or regulator proteins (HSP27, alphaB-crystallin, and glucose-regulated protein 58 kDa). Conversely, enzymes of glycolysis were overexpressed in the lighter group. Such samples were also characterized by higher levels of glutathione S-transferase omega, which can activate the RyR calcium channels, and higher levels of cyclophilin D. This protein pattern is likely to have severe implications on postmortem metabolism, namely, acceleration of ATP depletion and pH fall and subsequent enhanced protein denaturation, well-known to induce discoloration.