J. Anim Sci. 2007. 85:2005-2011. doi:10.2527/jas.2006-398
© 2007 American Society of Animal Science
Consequence of muscle hypertrophy on characteristics of Pectoralis major muscle and breast meat quality of broiler chickens1
C. Berri*,2,
E. Le Bihan-Duval*,
M. Debut*,
V. Santé-Lhoutellier
,
E. Baéza,
V. Gigaud
,
Y. Jégo
and
M. J. Duclos*
* Institut National de la Recherche Agronomique (INRA), UR83 Recherches Avicoles, F-37380 Nouzilly, France;
and
INRA, Unité Qualité des Produits Animaux, 63122 Saint-Genès-Champanelle, France;
and
Institut Technique Avicole, 28 Rue du Rocher, 75008 Paris, France; and and
Hubbard, 35220 Châteaubourg, France
 |
Abstract
|
|---|
The structural and metabolic characteristics of the pectoralis major (P. major) muscle (i.e., breast muscle) and the quality of the resulting meat were studied in relation to breast muscle fiber development in broiler chickens. Six hundred birds originating from a commercial, grand parental, male heavy line (Hubbard-Europe, Châteaubourg, France) were kept under conventional breeding methods until their usual marketing age of 6 wk. For all birds, the plasma creatine kinase activity and the P. major muscle fiber cross-sectional area (CSA), glycolytic potential, lactate content, pH at 15 min postmortem, as well as the ultimate pH, CIELAB color parameters [lightness (L*), redness (a*), and yellowness (b*)], and drip loss of breast meat, were measured. Increased breast weight and yield were associated with increased fiber CSA, reduced muscle glycolytic potential, and reduced lactate content at 15 min postmortem. Therefore, P. major muscle exhibiting larger fiber CSA exhibited greater pH at 15 min postmortem and ultimate pH, produced breast meat with lower L* and reduced drip loss, and was potentially better adapted to further processing than muscle exhibiting small fiber CSA.
Key Words: chicken • breast meat quality • muscle fiber • glycogen • pH
|
INTRODUCTION
|
|---|
Since the modern poultry industry began more than 50 yr ago, global production of poultry meat has continued to expand, and significant changes have occurred in the marketplace. Thus, the demand for oven-ready carcasses has been superseded in developed countries by a market in which an increasing diversity of further processed products has become the predominant form (Mead, 2004
). As a consequence, poultry companies are now involved in food technology and product development, and the improvement of meat processing ability has become a more prevalent concern. The change in the poultry market toward processing has been strongly related to the improvement in poultry growth and carcass yield, with a significant increase in breast muscle proportion (Barton, 1994; Nicholson, 1998).
Only a few studies focused on the consequences of such improvements in carcass composition on the sensory and functional properties of the meat for further processing. A Canadian study reported differences in sensory attributes of dark meat from light, experimental strains, and heavy commercial broilers (Chambers et al., 1989). Among broilers of similar age, it appears that dark meat from larger broilers had a more intense flavor, was more tender, and exhibited a greater overall acceptability score than that from smaller birds, which suggests that broiler size (i.e., growth rate) can affect the sensory attributes of meat. More recently, other traits of broiler breast meat have been considered in relation to muscle development. Experimental selection for increased breast meat yield and reduced carcass fatness was associated with breast meat that was lighter in color and exhibited a lower drip loss (Le Bihan-Duval et al., 1999). By comparison with unselected birds, the breast meat also showed a lower rate of postmortem acidification and a greater ultimate pH, which was consistent with the lower reserves of muscle glycogen in these birds (Berri et al., 2001).
In broilers, selection for increased growth rate and breast yield does not markedly affect the type of muscle fiber present but coincides with an increase in fiber diameter and length (Aberle and Stewart, 1983; Rémignon et al., 1994, 1995; Guernec et al., 2003). However, the consequences of muscle fiber hypertrophy on the sensory and processing quality of poultry meat products have not yet received much attention.
The purpose of this study was to determine the effect of breast muscle hypertrophy on the characteristics of Pectoralis major (P. major) breast muscle, including fiber size, glycogen content, and functional properties of the meat for further processing.
|
MATERIALS AND METHODS
|
|---|
Birds and Slaughter Conditions
All animal procedures and care were performed in accordance with the French Ministry of Agriculture and Fisherie.
A total of 609 male and female broilers originating from a grand-parental, male line (Hubbard, Châteaubourg, France) were used for this trial. Birds were reared in 2 successive batches 2 wk apart under similar conditions in a conventional poultry house at the INRA Avian Research Center (Nouzilly, France). They were given ad libitum access to a standard diet (from 0 to 2 wk: 21.5% CP, 7.8% crude fat, 1.13% lysine, and 3,010 Mcal of ME/kg, and from 3 to 6 wk: 19.3% CP, 6.8% crude fat, 0.88% lysine, and 3,066 Mcal of ME/kg; as-fed basis) throughout the growth period. At 6 wk of age, the birds were individually weighed on the day before slaughter. After a 7 h of feed withdrawal, all of the birds were slaughtered at the experimental processing plant of the INRA Avian Research Center. Before killing by ventral neck cutting, the birds were stunned in bath of water (125 Hz AC, 80 mA/bird, 5 s). After evisceration, whole carcasses were air chilled (airflow of 7 m3/s) and stored at 2°C until the next day. The carcasses were deboned 1 d after slaughter.
Blood and Pectoralis Major Muscle Traits
Individual blood samples were collected into heparinized tubes and temporarily stored on ice. Plasmas were separated after centrifugation at 2,000 x g for 15 min at 4°C and were stored at –20°C until assayed. Plasma creatine kinase activity (IU/L) was measured by spectrophotometry, using CK-NAC reagent and normal human serum as the control (Advanced Diagnostics, Plainfield, NJ). Creatine kinase activity was measured twice or more if differences were found between the first 2 measurements. The P. major muscle glycogen, glucose-6-phosphate, free glucose, and lactate were measured by enzymatic procedures, according to Dalrymple and Hamm (1973), from 1 g of fresh tissue, which was homogenized in 10 mL of 0.55 M perchloric acid at 15 min postmortem. The results were expressed as micromoles per gram of fresh tissue. Glycolytic potential takes into account the main intermediates of glycogen degradation in live and postmortem muscle and therefore represents an estimation of the resting glycogen level (Monin and Sellier, 1985); it was calculated as follows:
 |
and was expressed as micromoles of lactate equivalent per gram of fresh tissue.
At 15 min postmortem, P. major muscle samples collected for histology were rapidly frozen in isopentane, cooled with liquid nitrogen, and then stored at –80°C until analysis. The mean cross-sectional area (CSA) of muscle fibers was determined, as described by Rémignon et al. (1995), on 12-µm-thick cross-sections stained with red azorubin.
At 15 min postmortem, the P. major muscle pH (pH15) was measured as described by Jeacocke (1977). Two grams of fresh muscle were immediately homogenized in 18 mL of 5 mM iodoacetate/0.15 M KCl solution. The pH of the homogenate was measured with a portable pH meter (Model 506, Crison Instruments, SA, 08328 Alella, Barcelona, Spain) equipped with a combined glass electrode.
Breast Meat Quality Traits
At 24 h postmortem, the P. major ultimate pH (pHu) was measured by direct insertion of an electrode (pH meter Model 506, Crison Instruments, Barcelona, Spain) into the muscle. At the same time, breast color was measured on the cranial, ventral side of the P. major muscle by using a Miniscan Spectrocolorimeter (Hunterlab, Reston, VA). Color was measured by the CIELAB trichromatic system as lightness (L*), redness (a*), and yellowness (b*) values. The water holding capacity of meat was estimated by measuring drip loss of the raw meat after storage. The breast P. major muscles was weighed 24 h postmortem and immediately placed in a plastic bag, hung from a hook, and stored at 2°C for 48 h. After hanging, the sample was wiped with absorbent paper and weighed again. The difference in weight corresponded to the drip loss and was expressed as the percentage of the initial muscle weight.
Statistical Analyses
Phenotypic data were analyzed using SAS (SAS Inst. Inc., Cary, NC). The accepted type I error was 5%. The effects of batch of breeding and sex on animal and muscle measurements were analyzed by a 2-way ANOVA using the GLM procedure. Pairwise comparisons of means for each significant effect were performed by Scheffe test using the LSMEANS statement of the GLM procedure. Individuals were also classified in 5 classes of 120 birds according to their mean P. major muscle fiber CSA (RANK procedure), and a 1-way ANOVA was performed to test the effects of fiber CSA classes on other animal and muscle traits (GLM procedure). Comparisons of means for each significant effect were performed by Student Newman Keul’s test using the SNK statement of the GLM procedure. To assess the relationships among animal, muscle, and meat traits, Pearson’s correlation coefficient (rp) were analyzed with the CORR procedure. A multiple regression test was performed (REG procedure) to estimate the relative involvement of fiber CSA, muscle pH15, and pHu in determining the color and drip loss of breast meat.
The genetic correlation coefficients (rg) between muscle fiber CSA and other animal and muscle traits were obtained by the REML methodology with the VCE (version 4.2.5) software (Neumaier and Groeneveld, 1998). To increase the accuracy of the genetic parameter estimation, pedigree information of the parents of the animals used for the study was also considered; this was composed of a total of 15 males and 64 females.
|
RESULTS
|
|---|
Effect of Batch of Breeding and Sex on Body, Muscle, and Meat Characteristics
There were significant effects of the batch on most characters under study, but there was no significant batch of breeding x sex interaction (data not shown). The birds from the second batch of breeding exhibited slightly greater breast yield (P 
0.001) and lower abdominal fatness (P 0.01) despite a similar BW. Their P. major muscle exhibited a lower glycolytic potential (P 0.001) and lower lactate content at 15 min postmortem (P 0.001). Also, their breast meat was characterized by greater pH15 and lower L*, a*, b* values (P 0.001 for all traits).
There were significant effects of sex on most traits under study (Table 1). The females exhibited greater breast (P 0.001) and abdominal fat yields (P 0.001) despite a similar BW (Table 1). The CSA of P. major muscle fiber was much greater (P 0.001) in females than in males as well as their plasma creatine kinase activity (P 0.001). The P. major muscles of males and females exhibited similar glycolytic potential and pHu, but female muscles exhibited lower lactate content (P 0.001) and greater pH at 15 min postmortem (P 0.001) than those of males. Compared with males, breast meat from female chickens exhibited lower lightness (L*) and drip loss (P 0.001 for all traits).
Relationship Between Muscle Fiber Cross-Sectional Area and Growth and Meat Traits
Increased fiber CSA was associated with increased P. major muscle weight (Table 2). Besides, the weight of P. major muscle was highly positively correlated to BW (rp = 0.88, P 0.001) and to breast (rp = 0.53, P 0.001) and abdominal fat (rp = 0.51, P 0.001) yields. Consequently, the P. major muscle fiber mean CSA increased as BW and breast and abdominal fat yields of broilers increased (Table 2). Increased fiber CSA coincided with increased plasma creatine kinase activity and with changes in muscle metabolites (Table 2). Indeed, the glycolytic potential and the lactate content at 15 min postmortem of the P. major muscle decreased as fiber CSA increased. The lactate and glycolytic potential were negatively correlated to pH15 and pHu values, respectively (Table 3); therefore as muscle fiber CSA increased, muscle pH15 and pHu increased (Table 2). In the same way, because of the negative correlations between muscle pH15 or pHu and meat quality traits (Table 3), increased muscle fiber CSA was associated with decreased lightness and lower drip loss (Table 2).
Analysis of phenotypic and genetic correlations between muscle fiber CSA and the biochemical and meat quality traits on the overall population (Table 4) confirmed the results of the ANOVA analysis. Positive correlations between fiber CSA and plasma creatine kinase were observed. In the P. major muscle, fiber CSA was negatively related to lactate content and positively to pH15. Fiber CSA was also negatively related to muscle glycolytic potential and positively to meat pHu. Concerning breast meat quality traits, fiber CSA was negatively related to lightness and drip loss of fresh meat. There was a genetic negative correlation between fiber CSA and meat yellowness that was not observed at the phenotypic level. Phenotypic correlations between fiber CSA and other traits were similar when evaluated within sex (data not shown).
View this table:
[in this window]
[in a new window]
|
Table 4. Phenotypic and genetic correlations between Pectoralis major muscle fiber cross-sectional area and biochemical and breast meat quality traits
|
|
According to the multiple regression test (Table 5), fiber CSA was not directly involved in variations of breast meat drip loss and lightness. For these 2 characters, the main factor of variation was the pHu and to a lesser extent the pH15. Fiber CSA was only slightly implicated in determining redness and yellowness.
View this table:
[in this window]
[in a new window]
|
Table 5. Partial correlations between Pectoralis major muscle fiber cross-sectional area (CSA), pH15, and pHu and the resulting breast meat quality1
|
|
|
DISCUSSION
|
|---|
Fiber Hypertrophy and Muscle Growth
In the current study, chickens varied for growth and body composition and generally breast and abdominal fat yields increased with animal BW at slaughter. Our results supported previous findings that the increase of chicken breast muscle weight and yield largely involved the increase in muscle fiber diameter, but did not exclude the possible implication of an increase in number or in length of fibers. In chickens, selection for overall growth has been shown to induce greater muscle weight at the same age by increasing the fiber size and number (Rémignon et al., 1995; Burke and Henry, 1997; Scheuermann et al., 2004). However, according to Prentis et al. (1984), fiber size was of greater importance than fiber number in determining muscle size. Moreover, it seems that broiler selection focused on improved breast yield led to wider and thicker P. major muscles essentially by increasing the diameter and length of fiber without significantly altering their number (Guernec et al., 2003). Nevertheless, a recent study of Scheuermann et al. (2004) suggested that increased muscle fiber number may also participate to improve breast yield even though it confirmed that fiber hypertrophy is an essential factor for an increase in muscle volume.
Interestingly, males exhibited muscle fiber CSA about 16% smaller than females, whereas their P. major muscle weight was less then 4% lower. This suggests a greater muscle fiber number in males as already reported in different species such as broiler chickens (Rehfeldt et al., 1997; Henry and Burke, 1998; Scheuermann et al., 2003), ducks (Baéza et al., 1999), and pigs (Petersen et al., 1998). Therefore, comparing male and female chickens could allow assessing the impact of increased muscle fiber diameter on muscle and meat properties between muscles with similar weights. The greater muscle fiber diameter in females was associated with an increased plasma creatine kinase activity. The positive relationship between muscle fiber area and plasma creatine kinase activity was confirmed through the phenotypic and genetic correlation coefficients. Although the increase in plasma creatine kinase activity may be indicative of stress-associated tissue dysfunction (Mitchell et al., 1992; Mitchell and Sandercock, 1995), the histological observations of the 600 muscle samples did not reveal any particular damage related to fiber cross-sectional area or sex. Therefore, it can be suggested that plasma creatine kinase activity may also reflect the protein turn-over, which is closely related to muscle growth rate.
Muscle Fiber Cross-Sectional Area and Meat Quality Traits
To investigate the influence of fiber size on meat quality in mammals is rather difficult because of the strong relationship between muscle fiber size and muscle metabolism (Rehfeldt et al., 2000). The chicken breast P. major muscle is entirely composed of fast glycolytic fibers, predominantly expressing the adult form of rapid myosin heavy chain (Tidyman et al., 1997), so that fiber type diversity should only play a minor role in breast meat quality (Sams and Janky, 1990). This muscle is therefore relevant to evaluate the influence of fiber size on meat quality. According to the current study, increasing muscle fiber CSA and thus muscle weight in chicken was linked to a number of changes in muscle and meat characteristics. Indeed, as the fiber CSA increased, the muscle postmortem pH fall slowed down and its glycolytic potential decreased, whereas breast meat ultimate pH increased. Regarding meat quality, an increase in fiber CSA corresponded to meat with a darker color (lower L*) and a lower drip loss. In the same way, muscles of female chickens, which contain larger fibers than those of males, are also characterized by slower postmortem pH fall, darker color, and lower drip loss. However, no difference in muscle glycolytic potential or pHu was observed between males and females, whereas significant negative correlations between fiber CSA and these 2 parameters were reported on the whole population. This suggests that muscle glycogen content would be related to the overall muscle growth rather than to fiber diameter. This observation would support Henckel’s statement (1996) according to which a concentrated growth period of broilers may imply in muscle a constant state of hypoxia, obliging the use of the glycolytic pathway with degradation of glycogen to lactate to supply energy to muscle cells, even for light activity. Moreover, in chicken, an unfavorable relationship between the percentage of breast muscle and the density of capillaries has already been demonstrated, which implies a risk for the oxygen supply to the muscle and might affect perimortem processes determining meat quality (Hoving-Bolink et al., 2000). In the current study, we reported a negative genetic correlation between in vivo glycogen level and breast development. Recent results also highlighted a negative relationship between chicken breast muscle glycolytic potential and carcass leanness (Berri et al., 2005). Therefore, in chickens, selection for growth and leanness would lead to lower muscle glycogen content, whereas in pigs, increasing lean meat content led to greater muscle glycogen content (Larzul et al., 1999). Furthermore, the negative relationships found in chickens between the growth and leanness and the muscle glycogen content could explain the lack of difference in muscle glycogen between chicken males and females because females exhibited greater breast yield and greater fatness than males. Finally, our results showed that the decrease in meat lightness, and drip loss brought by muscle hypertrophy mainly result from changes in the rate and the extent of postmortem pH fall. Involvement of postmortem pH fall rate in determining further breast meat traits also appeared through the comparison between male and female because the latter exhibited at the same time greater pH15, lower lightness, and lower drip loss.
The current study allowed characterizing the physico-chemical properties of chicken breast muscles within a pedigree population of commercial broilers showing large variations in muscle weight and fiber size. Breast muscle weight and yield were positively correlated with muscle fiber diameter and negatively with glycogen levels. These changes resulted in breast meat with greater pH and consequently darker color and greater water holding capacity. Several studies have reported the occurrence of PSE-like syndrome in current commercial broilers (Wilkins et al., 2000; Woelfel et al., 2002), and some authors suggested that this could be associated with high growth rate (Dransfield and Sosnicki, 1999). This was not observed in the current study. At present, our data do not provide a mechanism supporting a true cause-and-effect relationship between fiber size and quality traits. Further research is needed to determine if glycogen synthesis, degradation, or both are altered and which enzymes are involved. This relationship would also deserve to be verified in other strains of broilers.
|
Footnotes
|
|---|
1 We acknowledge Hubbard breeders, Châteaubourg, France, for providing the 1-d-old broilers used in the trial. The authors wish to thank Nadim Haj Hattab, Thierry Bordeau, Estelle Godet, Nadine Sellier, and the technical staff of the experimental unit for their technical assistance. This work was financially supported by OFI-VAL (France). 
2 Corresponding author: berri{at}tours.inra.fr
Received for publication June 22, 2006.
Accepted for publication April 10, 2007.
|
LITERATURE CITED
|
|---|
Aberle, E. D., and T. S. Stewart. 1983. Growth of fiber types and apparent fiber number in skeletal muscle of broiler- and layer-type chickens. Growth 47:135–144.[Medline]
Baéza, E., G. Marché, and N. Wacrenier. 1999. Effect of sex on muscular development of Muscovy ducks. Reprod. Nutr. Dev. 39:675–682.[Medline]
Barton, N. F. 1994. Breeding meat type poultry for the future targets for selection, limits to performance and market requirements for chicken. Pages 33–38 in Proc. 9th Eur. Poult. Conf., Glasgow, UK.
Berri, C., E. Le Bihan-Duval, E. Baéza, P. Chartrin, N. Millet, and T. Bordeau. 2005. Effect of selection for or against abdominal fatness on muscle and meat characteristics of broilers. Pages 266–270 in Proc. 17th Eur. Symp. Qual. Poult. Meat, Doorwerth, the Netherlands. WPSA, Beekbergen, the Netherlands.
Berri, C., N. Wacrenier, N. Millet, and E. Le Bihan-Duval. 2001. Effect of selection for improved body composition on muscle and meat characteristics of broilers from experimental and commercial lines. Poult. Sci. 80:833–838.[Abstract/Free Full Text]
Burke, W. H., and M. H. Henry. 1997. Characteristics of the Pectoralis superficialis and semimembranosus of broiler strain chickens, bantam chickens, and the reciprocal crosses. Poult. Sci. 76:767–773.[Abstract/Free Full Text]
Chambers, J. R., A. Fortin, D. A. Mackie, and E. Larmond. 1989. Comparison of sensory properties of meat from broilers of modern stocks and experimental strains differing in growth and fatness. Can. Inst. Food Sci. Technol. J. 22:353–358.
Dalrymple, R. H., and R. Hamm. 1973. A method for extraction of glycogen and metabolites from a single muscle sample. J. Food Technol. 8:439–444.
Dransfield, E., and A. A. Sosnicki. 1999. Relationship between muscle growth and poultry meat quality. Poult. Sci. 78:743–746.[Abstract/Free Full Text]
Guernec, A., C. Berri, B. Chevalier, N. Wacrenier-Ceré, E. Le Bihan-Duval, and M. J. Duclos. 2003. Muscle development, insulin-like growth factor-I and myostatin mRNA levels in chickens selected for increased breast muscle yield. Growth Horm. IGF Res. 13:8–18.[CrossRef][Medline]
Henckel, P. 1996. Physiology and biochemistry of muscle fibres in poultry. Pages 79–89 in Proc. 2nd Eur. Poult. Breeders Roundtable, Foulum, Denmark. P. Sorensen, ed. Foulum, Denmark.
Henry, M. H., and W. H. Burke. 1998. Sexual dimorphism in broiler chick embryos and embryonic muscle development in late incubation. Poult. Sci. 77:728–736.[Abstract/Free Full Text]
Hoving-Bolink, A. H., R. W. Kranen, R. E. Klont, C. L. M. Gerritsen, and K. H. de Greef. 2000. Fibre area and capillary supply in broiler breast muscle in relation to productivity and ascites. Meat Sci. 66:397–402.
Jeacocke, R. E. 1977. Continuous measurement of the pH of beef muscle in intact beef carcass. J. Food Technol. 12:375–386.
Larzul, C., P. Leroy, L. Lefaucheur, P. Ecolan, P. Sellier, and G. Monin. 1999. Selection for reduced muscle glycolytic potential in Large White pigs. II. Correlated responses in meat quality and muscle compositional traits. Genet. Sel. Evol. 31:61–76.
Le Bihan-Duval, E., N. Millet, and H. Rémignon. 1999. Broiler meat quality: Effect of selection for increased carcass quality and estimates of genetic parameters. Poult. Sci. 78:822–826.[Abstract/Free Full Text]
Mead, G. C. 2004. Meat Quality and consumer requirements. Pages 1–18 in Poultry Meat Processing and Quality. G. C. Mead, ed. CRC Press, Boca Raton, FL; Woodhead Publishing Ltd., Cambridge, UK.
Mitchell, M. A., P. J. Kettlewell, and M. H. Maxwell. 1992. Indicators of physiological stress in broiler chickens during road transportation. Anim. Welf. 1:91–103.
Mitchell, M. A., and D. A. Sandercock. 1995. Creatine kinase isoenzyme profiles in the plasma of the domestic fowl (Gallus domesticus): Effects of acute heat stress. Res. Vet. Sci. 59:30–34.[CrossRef][Medline]
Monin, G., and P. Sellier. 1985. Pork of low technological quality with a normal rate of pH fall in the intermediate post mortem period: The case of the Hampshire breed. Meat Sci. 13:49–63.[CrossRef]
Neumaier, A., and E. Groeneveld. 1998. Restricted maximum likelihood of covariances in sparse linear models. Genet. Sel. Evol. 30:13–26.
Nicholson, D. 1998. Research, is it the broiler industry’s partner into the new millennium? World’s Poult. Sci. J. 54:271–278.
Petersen, J. S., P. Henckel, N. Oksbjerg, and M. T. Sørensen. 1998. Adaptations in muscle fibre characteristics induced by physical activity in pigs. Anim. Sci. 66:733–740.
Prentis, P. F., R. K. Penney, and G. Goldspink. 1984. Possible use of an indicator muscle in future breeding experiments in domestic fowl. Br. Poult. Sci. 25:33–41.[Medline]
Rehfeldt, C., I. Fiedler, G. Dietl, and K. Ender. 2000. Myogenesis and postnatal skeletal muscle cell growth as influenced by selection. Livest. Prod. Sci. 66:177–188.[CrossRef]
Rehfeldt, C., R. Schadereit, R. Weikard, and K. Reichel. 1997. Effect of clenbuterol on growth, carcase and skeletal muscle characteristics in broiler chickens. Br. Poult. Sci. 38:366–373.[Medline]
Rémignon, H., M. F. Gardahaut, G. Marché, and F. H. Ricard. 1995. Selection for rapid growth increases the number and the size of muscle fibres without changing their typing in chickens. J. Muscle Cell Motil. 16:95–102.[CrossRef]
Rémignon, H., L. Lefaucheur, J.-C. Blum, and F. H. Ricard. 1994. Effects of divergent selection for body weight on three skeletal muscles characteristics in the chicken. Br. Poult. Sci. 35:65–76.[Medline]
Sams, A. R., and D. M. Janky. 1990. Research note: Simultaneous histochemical determination of three fiber types in single sections of broiler skeletal muscles. Poult Sci. 69:1433–1436.[Medline]
Scheuermann, G. N., S. F. Bilgili, J. B. Hess, and D. R. Mulvaney. 2003. Breast muscle development in commercial broiler chickens. Poult. Sci. 82:1648–1658.[Abstract/Free Full Text]
Scheuermann, G. N., S. F. Bilgili, S. Tuzun, and D. R. Mulvaney. 2004. Comparison of chicken genotypes: Myofiber number in Pectoralis muscle and myostatin ontogeny. Poult. Sci. 83:1404–1412.[Abstract/Free Full Text]
Tidyman, W. E., L. A. Moore, and E. Bandman. 1997. Expression of fast myosin heavy chain transcripts in developing and dystrophic chicken skeletal muscle. Dev. Dyn. 208:491–504.[CrossRef][Medline]
Wilkins, L. J., S. N. Brown, A. J. Phillips, and P. D. Warriss. 2000. Variation in the colour of broiler breast fillets in the UK. Br. Poult. Sci. 41:308–312.[CrossRef][Medline]
Woelfel, R. L., C. M. Owens, E. M. Hirschler, R. Martinez-Dawson, and A. R. Sams. 2002. The characterization and incidence of pale, soft, and exudative broiler meat in a commercial processing plant. Poult. Sci. 81:579–584.[Abstract/Free Full Text]
This article has been cited by other articles:
|
|
|
|
 
V. Sibut, E. Le Bihan-Duval, S. Tesseraud, E. Godet, T. Bordeau, E. Cailleau-Audouin, P. Chartrin, M. J. Duclos, and C. Berri
Adenosine monophosphate-activated protein kinase involved in variations of muscle glycogen and breast meat quality between lean and fat chickens
J Anim Sci,
November 1, 2008;
86(11):
2888 - 2896.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. Berri, J. Besnard, and C. Relandeau
Increasing Dietary Lysine Increases Final pH and Decreases Drip Loss of Broiler Breast Meat
Poult. Sci.,
March 1, 2008;
87(3):
480 - 484.
[Abstract]
[Full Text]
[PDF]
|
|
|
Top
Abstract
INTRODUCTION
