肌肉纤维类型组成对猪肉品质的影响及其机理研究
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摘要
通过改变肌肉纤维类型组成提高猪肉品质已经成为肉品科学和养猪生产领域的研究热点。本论文首先研究猪背最长肌肌球蛋白重链(MyHC)表达的生长发育规律,确定用于分析纤维类型组成的科学指标,进一步研究肌肉纤维类型组成的品种差异及其与肉质性状的相关性,并揭示其分子机理,最后在育肥后期进行营养调控研究,为肌肉纤维类型组成在提高猪肉品质中发挥作用提供科学依据。
     猪背最长肌MyHC表达的生长发育规律:选取7、40、60、120和175日龄杜长大公猪各5头,测定背最长肌MyHC蛋白表达、MyHC mRNA转录以及氧化代谢酶活性。结果显示,猪出生后生长过程中MyHC mRNA比例与相应蛋白亚基比例呈显著正相关(P<0.05),MyHC I mRNA比例与琥珀酸脱氢酶及苹果酸脱氢酶活性呈显著正相关(P<0.05)。以MyHC I、IIa、IIx和IIb mRNA比例分别表示慢速氧化型、快速氧化型、中间型和快速酵解型纤维比例,分析表明:慢速氧化型纤维比例随日龄增加呈下降趋势,其它类型纤维比例呈升上升趋势;在7-60日龄,所有类型纤维比例变化明显;在120-175日龄,快速氧化型、中间型和快速酵解型纤维比例无显著变化(P<0.05),慢速氧化型纤维比例仍显著降低(P<0.05)。结果提示,MyHC mRNA组成比例可作为分析肌肉纤维类型组成的科学指标,纤维类型转化在生长早期最为明显,在育肥后期仍存在调控可能性。
     猪肌肉纤维类型组成的品种差异及其与肉质性状的相关性:选择上市体重金华猪、浙江中白猪、杜浙猪和杜大长猪阉公猪各8头,分别含有100%、12.5%、6.25%和0%的金华猪血缘,以MyHC mRNA比例为指标分析背最长肌纤维类型组成,并测定肉质性状。结果显示,慢速氧化型、快速氧化型和中间型纤维比例均在金华猪表现最高(P<0.05),快速酵解型纤维比例在金华猪表现最低(P<0.05);慢速氧化型纤维比例按照金华猪>浙江中白猪>杜浙猪>杜大长猪的顺序显著降低(P<0.05),快速氧化型纤维比例也表现相似趋势,但在浙江中白猪和杜浙猪之间无显著差异(P>0.05);中间型和快速酵解型纤维比例在浙江中白猪、杜浙猪和杜大长猪之间无显著差异(P>0.05);氧化型纤维比例与肉色a*值、剪切力、肌内脂肪(IMF)含量及蛋白质溶解度呈显著正相关(P<0.05),与ΔpH呈显著负相关(P<0.05)。结果证实了肌肉纤维类型组成的品种差异,解释了不同猪群的肉质特性,并提示在商品猪生产过程中引入一定比例优质地方血缘,有利于提高肌肉氧化型纤维比例,进而改善肉质性状。
     猪肌肉纤维类型组成差异相关的能量代谢分析:以纤维类型组成明显差异的金华猪和杜大长猪背最长肌为研究对象,测定磷酸原转化指标(肌酸激酶活性与磷酸化合物含量)和糖酵解指标(糖代谢物含量和糖酵解潜力)。结果显示,高比例氧化型纤维(金华猪)肌肉具有较高的肌酸激酶(CK)活性、Cr:(Cr+CP)和肌酸(Cr)含量(P<0.05),较低的磷酸肌酸(CP)、糖原、葡萄糖、葡萄糖-6-磷酸及乳酸含量与糖酵解潜力(P<0.05);CK活性、Cr:(Cr+CP)与均pH显著负相关(P<0.05),与慢速氧化型、快速氧化型及中间型纤维比例呈显著正相关(P<0.01),与快速酵解型纤维比例呈显著负相关(P<0.01),葡萄糖-6-磷酸含量、糖酵解潜力均与pH、纤维类型组成的相关性表现刚好相反。结果提示:高比例氧化型纤维肌肉具有较高的磷酸原转化能力和较低的糖酵解能力,是肌肉纤维类型组成影响猪肉品质的能量代谢机理。
     猪肌肉纤维类型组成差异相关的蛋白质组与基因表达谱分析:以纤维类型组成明显差异的金华猪和杜大长猪背最长肌为研究对象,利用2-DE-MS和表达谱芯片分别对肌浆蛋白和基因表达谱进行差异比较。结果显示,高比例氧化型纤维(金华猪)肌肉表现较高含量的nesprin-2-like、热休克蛋白HSP90\70\60、转铁蛋白、Gc蛋白、线粒体ATP合成酶和环腺苷蛋白激酶(PKA)(P<0.05),较低含量的糖原磷酸化酶和葡萄糖磷酸变位酶(P<0.05);高比例氧化型纤维(金华猪)肌肉中上调倍数大于3的基因分布在免疫反应、信号转导、结构成分形成、代谢调节、抗氧化、离子转运、脂类代谢、核酸代谢及氧化磷酸化等相关生物学过程,信号转导基因主要参与Jak-STAT、cAMP、TGF-β、MAPK和Wnt通路。结果提示,高比例氧化型纤维肌肉表现较强的氧化代谢、细胞骨架与结缔组织形成、线粒体ATP生成、抗氧化应激等能力,较弱的糖酵解能力,是肌肉纤维类型组成影响猪肉品质的重要分子机理;其中Wnt信号通路在氧化型纤维分化中的作用值得关注与入研究。
     育肥后期猪肌肉纤维类型组成的营养调控研究:选取育肥后期(70kg体重)杜浙猪45头,平均分成3组,分别饲喂基础日粮、基础日粮+1.2%共轭亚油酸(CLA)和基础日粮+0.5%一水肌酸(CMH)。试验30天后测定生长性能、胴体性状、背最长肌纤维类型组成及肉质性状。结果显示,CLA和CMH表现促进肌肉生长、降低脂肪沉积、提高pH与肉色a*的趋势(P>0.05);CLA还显著提高慢速氧化型纤维比例、剪切力和蛋白质溶解度,显著降低滴水损失和压榨损失(P<0.05); CMH对pH的提高趋势比CLA明显,对其它肉质性状的改善程度低于CLA。在生产实际中印证了育肥后期猪肌肉纤维类型组成的可调控性,并为CLA改善肉质性状提供新的机理解释。
     本论文确定了MyHC表达用于分析猪肌肉纤维类型组成的科学指标—MyHCmRNA比例,提出育肥后期猪肌肉纤维类型组成存在调控可能性,并在生产实际中得到印证。首次利用遗传基础梯度变化猪群,以MyHC mRNA比例为指标研究肌肉纤维类型组成与肉质性状的相关性,从能量代谢、肌浆蛋白质组与基因表达谱三个层次综合阐明分子机理。本文结论为优质猪肉生产、地方猪种资源利用、肉质性状营养调控提供了科学依据。
Improving pork quality through changing the muscle fibre types is a focus in the fields ofmeat science and pig production. Firstly the law of MyHC expression in porcine longissimudoris (LD) was studied during the different growth stages after birth. Then taking differentpercentage of native bloodline pigs as objects, the breed difference of muscle fibre types andits association with pork quality traits were analyzed, and the underlying molecularmechanisms were further studied. Lastly dietary modification on muscle fibre types and porkquality in late finishing pigs was conducted.
     Study on postnatal growth law of MyHC expression in porcine LD. Five DLY(Duroc×Landrace×Yorshire) crossbred pigs were selected at the age of7,40,60,120and175days, respectively. MyHC isoforms, MyHC mRNA and activities of succinate dehydrogenase(SDH) and malate dehydrogenase (MDH) were measured, and the associations among themwere analyzed. The results showed that MyHC mRNA was more likely to be changed thanMyHC isoform, and MyHC mRNA proportion was positively related to the correspondingisoform proportion (P<0.05), simultaneously MyHC I mRNA proportion was positivelyrelated to the activities of SDH and MDH (P<0.05). The analysis of muscle fibre typesaccording to MyHC mRNA composition showed that slow-oxidative fibre was obviouslydecreased with the days of age increasing during postnatal period (P<0.05), and other fibretypes was opposite. From7to60days of age, all fibre types exhibited obviously undulatechanges. From120to175days of age, fast-oxidative, fast-glycolytic and intermediate-typefibre exhibited no significant changes (P>0.05), while slow-oxidative fibre decreasedsignificantly (P<0.05). The above results indicated that MyHC mRNA proportion wassuitably used to analyze muscle fibre types; the conversion among different myofibre typesmainly occured at the early growth stage, and also could be changed during the late finishingperiod.
     Study on genetic diversity of muscle fibre types and its association with porkquality traits. Jinhua pigs (JHP), Zhejiang Zhongbai pigs (ZBP), Duroc×ZB crossbred pigs(DZP) and Duroc×Yorshire×Landrace (DYL) pigs, which contains100%,12.5%,6.25%and0%of JHP bloodline repectively, were selected, eight pigs per genotype. Muscle fibre types(MyHC mRNA proportions) and pork quality traits in LD were measured. The results showedthat JHP had more slow-oxidative, fast-oxidative and intermediate-type fibre, lessfast-glycolytic firbe in than other genotypes (P<0.05); slow-oxidative fibre decreasedsignificantly in the order of JHP>ZBP>DZP>DYL (P<0.05), fast-oxidative fibre exhibitedthe similar tendency but no significant difference between ZBP and DZP (P>0.05);fast-oxidative and intermediate-type fibre exhibited no significant difference among ZBP,DZP and DYL (P>0.05); slow-and fast-oxidative type fibre were positively related to huantera*, intramuscularly fat (IMF) content and protein solubility, negatively to ΔpH (P<0.05).The above results confirmed the genotypic difference of muscle fibre types, explained pork quality charastics in LD of different genotypes, and indicated that it is beneficial for porkquality by increasing oxidative-type fibre to introduce a certain percentage of native pig breedinto commercial crossbred pigs.
     Study on energy metabolism related to muscle fibre types. Glycometabolite,phosphate compounds and creatine kinase (CK) activity in LD from JHP (high slow-oxidativefibre proportion, HSO) and DYL (low slow-oxidative fibre proportion, LSO) were measured.The results showed that HSO muscle had the higher CK activity and Cr:(creatinephosphate(CP)+Cr), the more inosine monophosphate (IMP) and creatine (Cr), the lowerglycolysis potential (GP), and the less CP, glycogen, glucose, and glucose-6-phosphate thanLSO muscle (P<0.05); CK activity and Cr:(CP+Cr) were positively related to pH and thepercentages of slow-oxidative, fast-oxidative and intermediate-type fribre, negatively to thepercentage of fast-glycolytic type (P<0.05), the relationships between glucose-6-phosphatecontent, GP and muscle fibre types, pH were opposite; The above results revealed theenergy metabolism mechanism of muscle fibre types influencing pork quality that HSOmuscle had a relatively strong phosphate conversion capacity and a relatively weak glycolyticcapacity.
     Differential analyses of proteome and gene expression profiling related to musclefibre types. Differential analyses of sarcoplasmic proteome and gene expression profilingwere performed between HSO (JHP) and LSO (DYL) muscle. The results showed that HSOmuscle had the higher contents of nesprin-2-like protein, heat shock protein (HSP)60\70\90,transferring, Gc protein, ATP synthase in mitochondrion and cAMP protein kinase (PKA)(P<0.05), and the lower the contents of glycogen phosphorylase and glucose phosphomutasethan LSO muscle (P<0.05); the up-expressed genes with more than three folds in HSOmuscle were classified into ten categories including immunological reaction, signal transduction,formation of cystoskeleton and connective tissue, metabolic regulation, oxidation resistance,ionic transport, lipid metabolism, nucleic acid metabolism and oxidative phosphorylation, andthe genes in signal transduction were related to the signal pathways of Jak-STAT、cAMP、TGF-β、MAPK and Wnt. The above results revealed the molecular mechanism of muscle fibretypes influencing pork quality that HSO muscle had the relatively strong capacities ofoxidative metabolism, cystoskeleton and connective tissue synthesis, ATP synthesis inmitochondrion, oxidative stress resistance. And the role of Wnt pathway on the differentiationof oxidative-type fibre in porcine muscle was worthy to be concerned and further studied.
     Nutritional regulation of muscle fibre types in the late finishing pigs.45DZcrossbred pigs (about70kg bodyweight) were divided into three groups (five replicates/group, three pigs/replicate), which were fed with control diet, control+1.2%CLA, control+0.5%CMH, respectively. The feeding experiment lasted for30days, and growth performance,carcass traits, muscle fibre types (MyHC mRNA proportions) and pork quality traits in LDwere measured. The results showed that there was a tendency of promoting granulation,reducing fat deposition, raising pH and hunter a*in the groups of CLA and CMH (P>0.05); slow-oxidative fibre proportion, shear force and protein solubility were significantly increased,and drip loss and milling loss were significantly decreased in CLA group (P<0.05); except forpH, the changing degrees of other pork quality traits was lower in CMH than those in CLAgroup. The above results confirmed the former hypothesis that muscle fibre types could bechanged during the late finishing period, and supplied a new explaination for the mechanismof CLA improving pork quality.
     This study determined MyHC mRNA proportion as the scientific index for analyzingmuscle fibre types in pigs, and suggested that the porcine muscle fibre types could be changedduring the late finishing period, which was confirmed through feeding experiment. Therelationship between muscle fibre types and pork quality was firstly studied according toMyHC mRNA proportions through the pig populations with different percentage of native pigbreed, and the underlying mechanism was investigated through energy metabolism,sarcoplasmic proteome and gene expression profiling. The conclusion would provide theevidences for high quality pork production, utilization of native pig breed and nutritionalregulation of pork quality.
引文
[1] Depreux F F S, Grant A L, Gerrard D E. Influence of halothane genotype and body-weight on myosinheavy chain composition in pig muscle as related to meat quality [J]. Livestock Production Science,2002,73:265-273
    [2] Ryu Y C, Choi Y M, KimB C. Variations in metabolite contents and protein denaturation of thelongissimus dorsi muscle in various porcine quality classifications and metabolic rates [J]. MeatScience,2005,71:522-529
    [3] Gil M, Oliver M à, Gispert M, et al. The relationship between pig genetics, myosin heavy chain I,biochemical traits and quality of M. longissimus thoracis [J]. Meat Science,2003,65:1063-1070
    [4] Kim N K, Lim J H, Song M J, et al. Comparisons of longissimus muscle metabolic enzymes and musclefiber types in.Korean and western pig breeds [J]. Meat Science,2008,78:455-460
    [5] Wigmore P M C and Stickland N C. Muscle development in large and small pig fetuses [J]. Journal ofAnatomy,1983,2:235-245.
    [6] Goldring K, Partridge T and Watt D. Muscle stem cells [J]. Journal of Pathology,2002,197:457-467.
    [7] Glass D J. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy [J]. Nature CellBiology,2003,5:87-90.
    [8] Padykula H A, Herman E. Factors affecting the activity of adenosine triphosphatase and otherphosphatases as measured by histochemical techniques [J]. Histochem Cytochem,1955,3:161-169.
    [9] Ogilvie R W, Feeback D L. A metachromatic dye-ATPase method for the simultaneous identification ofskeletal muscle fiber types I, IIA, IIB and IIC [J]. Stain Technology,1990,65:231-241.
    [10] Sweeney L J, Brodfuehrer P D, Raughley B L. An introductory biology lab that uses enzymehistochemisty to teach student about skeletal muscle fiber types [J]. Advances in PhysiologyEducation,2004,28:23-28.
    [11] Larzul C, Lefaucheur L, Ecolan P, et al. Phenotypic and genetic parameters for longissimus musclefiber characteristics in relation to growth, carcass, and meat quality traits in Large White pigs [J].Journal of Animal Science,1997,75:3126-3137.
    [12]贲长恩,李叔庚.组织化学[M].北京:人民卫生出版社,2001.383-385.
    [13] Jouffroy K, Medina M F, Renous S, et al. Immunocyto chemical characteristics of elbow, knee andankle muscles of the five to edjerboa (Allactaga elater)[J]. Journal of Anatomy,2003,202:373-386.
    [14] B r A, Pette D. Three fast myosin heavy chains in adult rat skeletal muscle [J]. FEBS Letters,1988,235:153-155.
    [15] Schiaffino S, Gorza L, Sartore S, et al. Three myosin heavy chain isoforms in type2skeletal musclefibres [J]. Journal of Muscle Research and Cell Motility,1989,10:197-205.
    [16] Schiaffino S,&Reggiani C. Molecular diversity of myofibrillar proteins: Gene regulation andfunctional significance [J]. Physiological Reviews,1996,76:371-423.
    [17] Lefaucheur L, Hoffman R K, Gerrard D E, et al. Evidence for three adult fast myosin heavy chainisoforms in type II skeletal muscle fibers in pigs [J]. Journal of Animal Science,1998,76:1584-1593.
    [18] Carol E T and Mathew P D. Regulation of Myosin Heavy Chain Expression during Rat SkeletalMuscle Development In Vitro [J]. Molecular Biology of the Cell,2001,12:1499-1508.
    [19] Eggert J M, Depreux F F S, Schinckel A P, et al. Myosin heavy chain isoforms account for variation inpork quality [J]. Meat Science,2002,61:117-126
    [20] Sanchez H, Chapot R, Banzet S, et al. Quantification by real-time PCR of developmental and adultmyosin mRNA in rat muscles [J]. Biochemical and Biophysical Research Communications,2006,340:165-174
    [21] Short K R, Vittone J L, Bigelow M L, et al. Changes in myosin heavy chain mRNA and proteinexpression in human skeletal muscle with age and endurance exercise training [J]. Journal of Appliedphysiology,2005,99:95-102.
    [22]Gunawan A M, Park S K, Pleitner J M, et al. Contractile protein content reflects myosin heavy-chainisoform gene expression [J]. Journal of Animal Science,2007,85:1247-1256.
    [23] Haddad F, Qin A X, Bodell P W, et al. Intergenic transcription and developmental regulation of cardiacmyosin heavy chain genes [J]. American Journal of Physiology (Heart and Circulatory Physiology),2008,294: H29-H40.
    [24] Ruusunen M,&Puolanne E. Histochemical properties of fibre types in muscles of wild and domesticpigs and the effect of growth rate on muscle fibre properties [J]. Meat Science,2004,67:533-539.
    [25] Bonneau M, Mourot J, Noblet J, et al. Tissue development in Meishan pigs: Muscle and fatdevelopment and metabolism and growth regulation by somatotropic hormone [C]. Chinese pigsymposium. Jouy-en-Josas in France: INRA,1990.203-213.
    [26] Lefaucheur L, Le Roy P, Lebret B, et al. Divergent selection on contractile properties of longissimusmuscle fibres in the pig [J]. In Proceedings of the46th international congress of meat science andtechnology,2000,94-95
    [27] Wimmers K, Ngu N T, Jennen D G J, et al. Relationship between myosin heavy chain isoformexpression and muscling in several diverse pig breeds [J]. Journal of Animal Science,2008,86:795-803.
    [28] Henckel P, Oksbjerg N, Erlandsen E, et al. Histo-and biochemical characteristics of the longissimusdorsi muscle in pigs and their relationships to performance and meat quality [J]. Meat Science,1997,47:311-32
    [29] Tribout T, Caritez J C, Cogué J, et al. Estimation, par utilisation de semence congelée, du progrèsgénétique réalisé en France entre1977et1998dans la race porcine Large White: Résultats pourquelques caractères de production et de qualité des tissus gras et maigres. Journées de la RecherchePorcine en France,2004,36,275-282.
    [30] Ryu Y C, Rhee M S,&Kim B C. Estimation of correlation coefficients between histologicalparameters and carcass traits of pig longissimus dorsi muscle [J]. Asian-Australasian Journal ofAnimal Sciences,2004,17:428-433.
    [31] Bowker B C, Grant A, Swartz D R, et al. Myosin heavy chain isoforms influence myofibrillar ATPaseactivity under simulated postmortem pH, calcium, and temperature conditions [J]. Meat Science,2004,67:139-147.
    [32] Ryu Y C,&Kim B C. The relationship between muscle fiber characteristics,postmortem metabolicrate, and meat quality of pig longissimus dorsi muscle [J]. Meat Science,2005,71:351-357.
    [33] Ryu Y C,&Kim B C. Comparison of histochemical characteristics in various pork groups categorizedby postmortem metabolic rate and pork quality [J]. Journal of Animal Science,2006,84:894-901.
    [34] Choi Y M, Ryu Y C,&Kim B C. Influence of myosin heavy-and light chain isoforms on earlypostmortem glycolytic rate and pork quality [J]. Meat Science,2007,76:281-288.
    [35] Choe J H, Choi Y M, Lee S H, et al. The relation between glycogen, lactate content and muscle fibertype composition, and their influence on postmortem glycolytic rate and pork quality [J]. MeatScience,2008,80:355-362.
    [36] Golding-Myers J D, Showers C D, Shand P J, et al. Muscle fibre type and the occurrence of pale, soft,exudative pork [J]. Journal of Muscle Foods,2010,21:484-498
    [37] Essén-Gustavsson B, Henriksson J. Enzyme levels in pools of microdissected human muscle fibres ofidentified type [J]. Acta Physiologica Scandinavica,1984,120:505-515.
    [38] Monin G, Mejenes-Quijano A, Talmant A, et al. Influence of breed and muscle metabolic type onmuscle glycolytic potential and meat pH in pigs [J]. Meat Science,1987,20:149-158.
    [39] Wallimann T, Wyss M, Brdiczka D, et al. Intracellular compartmentation, structure and function of thecreatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine’circuit for cellular energy homeostasis [J]. The Biochemical Journal,1992,281:21-40.
    [40] Bottinelli R, Reggiani C. Human skeletal muscle fibers: molecular and functional diversity [J].Progress in Biophysics and Molecular Biology,2000,73:195-262.
    [41] Olivǎn M, Martinez A, Osoro K, et al. Effect of muscular hypertrophy on physico-chemical,biochemical and texture traits of meat from yearling bulls [J]. Meat Science,2004,68:567-575
    [42] Ramirez J A, Oliver M à, Pla M, et al. Effect of selection for growth rate on biochemical, quality andtexture characteristics of meat from rabbits [J]. Meat Science,2004,67:617-624
    [43] Sazili A Q, Parr T, Sensky P L, et al. The relationship between slow and fast myosin heavy chaincontent, calpastatin and meat tenderness in different ovine skeletal muscles [J]. Meat Science,2005,69(1):17-25
    [44] Li X, Yang X, Shan B, et al. Meat quality is associated with muscle metabolic status but not contractilemyofiber type composition in premature pigs [J]. Meat Science,2009,81:218-223
    [45] Stadtman E R. Oxidation of free amino acids and amino acids residues in proteins by radiolysis and bymetal-catalyzed reactions [J]. Annual Review of Biochemistry,1993,62:797-821.
    [46] Rowe L J, Maddock K R, Lonergan S M, Huff-Lonergan E. Influence of early postmortem proteinoxidation on beef quality [J]. Journal of Animal Science,2004,82:785-793.
    [47] Joo S T, Kauffman R G, Kim B C, et al. The relationship of sarcoplasmic and myofibrillar proteinsolubility to color and water-holding capacity in porcine longissimus muscle [J]. Meat Science,1999,52:291-297.
    [48]孔保华.畜产品加工储藏新技术[M].北京:科学出版社,2007.40.
    [49] Sensky P L, Parr T, Scothern G P, et al. Differences in the calpain enzyme system in tough and tendersamples of porcine longissimus dorsi muscle [J]. Proceedings of the British Society of Animal Science,1998,14
    [50] Choi Y M, Lee S H, Choe J H, et al. Protein solubility is related to myosin isoforms, muscle fibertypes, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle [J].Livestock Science,2010,127:183-191.
    [51] Karlsson A H, Klont R E,&Fernandez X. Skeletal muscle fibres as factors for pork quality [J].Livestock Production Science,1999,60:255-269.
    [52] De Feyter H M, Schaart G, Hesselink M K, et al. Regional variations in intramyocellular lipidconcentration correlate with muscle fiber type distribution in rat tibialis anterior muscle [J]. MagneticResonance in Medicine,2006,56:19-25
    [53] Park B Y, Kim N K, Lee C S, et al. Effect of fiber type on postmortem proteolysis in longissimusmuscle of Landrace and Korean native black pigs [J]. Meat Science,2007,77:482-491
    [54] Hu H M, Wang J Y, Zhu R S, et al. Effect of myosin heavy chain composition of muscles on meatquality in Laiwu pigs and Duroc [J]. Science in China Series C: Life Sciences,2008,51:127-132
    [55] Gondret F, Mourot J, Bonneau M. Comparison of intramuscular adipose tissue cellularity in musclesdiffering in their lipid content and fibre type composition during rabbit growth [J]. LivestockProduction Science,1998,54:1-10
    [56] Letaucheur L, Milan D, Ecolan P, et al. Myosin heavy chain composition of different skeletal musclesin Large White and Meishan pigs [J]. Journal of Animal Science,2004,82:1931-1941.
    [57] Guo J, Shan T, Wu T, et al. Comparisons of different muscle metabolic enzymes and muscle fibertypes in Jinhua and Landrace pigs [J]. Journal of Animal Science,2011,89:185-191
    [58]杨飞云,陈代文,黄金秀,等.猪背最长肌肌纤维类型的发育性变化及品种与营养影响特点[J].畜牧兽医学报,2008,39(12):1701-1708.
    [59]杨晓静.猪骨骼肌生长及肌纤维类型分布的分子机理研究[D].南京:南京农业大学,2004.
    [60] Chang K C, Costa N D, Blackley R, et al. Relationships of myosin heavy chain fiber types to meatquality traits in traditional and modern pigs [J]. Meat Science,2003,64:93-103
    [61] Buckingham M, Vincent S D. Distinct and dynamic myogenic populations in the vertebrate embryo [J].Current Opinion in Genetics&Development,2009,19:444-453
    [62] Lefaucheur L,Vigneronn P. Post-natal changes in some histochemical and enzymatic characteristics ofthree pig muscle [J]. Meat Science,1986,16:199-216.
    [63] Picard B, Lefaucheur L, Berri C, et al. Muscle fibre ontogenesis in farm animal species [J].Reproduction Nutrition Development,2002,42:415-431
    [64] Suzuki A, Kojima N, Ikeuchi Y, et al. Carcass composition and meat quality of Chinese purebred andEuropean×Chinese crossbred pigs [J]. Meat Science,1991,29:31-38
    [65] Harrison A P, Rowlerson A M and Dauncey M J. Selective regulation of myofiber differentiation byenergy status during postnatal development [J]. American Journal of Physiology,1996,270:667-674
    [66] White P, Cattaneo D&Dauncey M J. Postnatal regulation of myosin heavy chain isoform expressionand metabolic enzyme activity by nutrition [J]. British Journal of Nutrition,2000,84:185-194.
    [67] Lefaucheur L, Ecolan P, Barzic Y M, et al. Early postnatal food intake alters myofiber maturation inpig skeletal muscle [J]. Journal of Nutrition,2003,133:140-147.
    [68] Bee G. Effectof earlygestation feeding, birthweight, and gender of progeny on muscle fibercharacteristics of pigs at slaughter [J]. Journal of Animal Science,2004,82:826-836.
    [69] Emérita A, Eugenio Q R, Ana-Isabel M, et al. Myosin heavy chain fibre types and fibre sizes innuliparous and primiparous ovariectomized Iberian sows: Interaction with two alternative rearingsystems during the fattening period [J]. Meat Science,2006,74:359-372.
    [70] Zhu M J, Ford S P, Means W J, et al. Maternal nutrient restriction affects properties of skeletal musclein offspring [J]. The Journal of Physiology,2006,575:241-250.
    [71] Wang J Q, Li X, Yang X J, et al. Maternal dietary protein induces opposite myofiber type transition inmeishan pigs at weaning and finishing stages [J]. Meat Science,2011,89:221-227.
    [72] Migdal M, Wojtysiak D, Pa ciak, et al. The histochemical profile of the muscle fibre infatteners-genetic and non-genetic fators [J]. Biotechnology in Animal Husbandry,2005,21:161-167
    [73]田春庄.鱼油上调断奶仔猪肌纤维类型及相关基因表达促进肌肉生长的研究[D].武汉:华中农业大学硕士学位论文,2008.
    [74]黄金秀,杨飞云,刘作华,等.共轭亚油酸对体外培养的猪骨骼肌肌纤维类型组成的影响[J].畜牧兽医学报,2010,41(3):295-300.
    [75] Buller A J, Eccles J C and Eccles R M.Interactions between motoneurones and muscles in respect ofthe characteristic speeds of their responses [J].Journal of Physiology,1960,150:417-439.
    [76] Wang L C and Kernel D.Recovery of type I fiber regionalization in gast rocnemius medialis of t he ratafter reinnervation along original and foreign paths, with and without muscle rotation [J].NeuroScience,2002,114:629-640.
    [77] Gorza L, Gundersen K, LEmo T, et al. Slow to fast transformation of denervated soleus muscles bychronic high—frequency stimulation in the rat [J]. Journal of Physiology,1988,402:627-649.
    [78] Bacou F, Rouanet P, Barjot C, et al. Expression of myosin isoforms in denervated, cross-reinnervat-ed,and electrically stimulated rabbit muscles [J]. European Journal of Biochemistry,1996,236:539-547.
    [79] Staron R S. Skeletal muscle adaptations during early phase of heavy—resistance training in men andwomen [J]. Journal of Applied Physiology,1994,76:1247-1255.
    [80] Caiozzo V J, Haddad F, Baker M J, et al. Microgravity—induced transformations of myosin isoformsand contractile properties of skeletal muscle [J]. Journal of Applied Physiology,1996,8I:123-132.
    [81] Lefaucheur L, Le Dividich J, Mourot J, et al.Influence of environmental temperature on growth,muscle and adipose tissue metabolism, and meat quality in swine [J]. Journal of Animal Science,1991,69:2844-2854.
    [82] Rinaldo D,&Le Dividich J. Effects of warm exposure on adipose tissue and muscle metabolism ingrowing pigs [J]. Comparative Biochemistry and Physiology Part A,1991,100A:995-1002.
    [83] Staron R S, Hagerman F C, Hikida R S, et al. Fiber type composition of the vastus lateralis muscle ofyoung men and women [J]. Journal of Histochemistry and Cytochemistry,2000,48:623-629.
    [84] Canepari M, Cappelli V, Pellegrino M A, et al.Thyroid hormone regulation of MHC isoformcomposition and myofibrillar ATPase activity in rat skeletal muscles [J]. Archives of Physiology andBiochemistry,1998,106:308-3l5.
    [85] Adams G R, Haddad F, McCue S A, et al. Effects of spaceflight and thyroid deficiency on rat hindlimbdevelopment.II. Expression of MHC isoforms [J]. Journal of Appllied Physiology,2000,88:904-916
    [86] Rehfeldt C, Kuhn G, Vanselow J, et al. Maternal treatment with somatotropin during early gestationaffects basic events of myogenesis in pigs [J]. Cell and Tissue Research,2001,306:429-440.
    [87] Denley A, Cosgrove L J, Booker G W, et al. Molecular interactions of the IGF system [J]. Cytokine&Growth Factor Reviews,2005,16:421-439.
    [88] Glass D J. Molecular mechanisms modulating muscle mass [J]. Trends in Molecular Medicine,2003,9:344-350.
    [89] Glass D J. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy [J]. Nature CellBiology,2003,5:87-90.
    [90] Haddad F and Adams G R. Inhibition of MAP/ERK kinase prevents IGF-I induced hypertrophy in ratmuscles [J]. Journal of Applied Physiology,2004,96:203-210.
    [91] Cabane C, Englaro W, Yeow K, et al. Regulation of C2C12myogenic terminal differentiation byMKK3/p38a pathway [J]. American Journal of Physiology-Cell Physiology,2003,284: C658-C666.
    [92] Lee J, Hong F, Kwon S, et al. Activation of p38MAPK induces cell cycle arrest via inhibition of Raf/ERK pathway during muscle differentiation [J]. Biochemical and Biophysical ResearchCommunications,2002,298:765-771.
    [93] Kocamis H and Killefer J. Myostatin expression and possible functions in animal muscle growth [J].Domestic Animal Endocrinology,2002,23:447-454.
    [94] Marchitelli C, Savarese M C, Crisa A, et al. Double muscling in Marchigiana beef breed is caused by astop codon in the third exon of myostatin gene [J]. Mammalian Genome,2003,14:392-395.
    [95] Thomas M, Langley B, Berry C, et al. Myostatin, a negative regulator of muscle growth, functions byinhibiting myoblast proliferation [J]. Journal of Biological Chemistry,2000,275:40235-40243.
    [96] Philip B, Lu Z and Gao Y. Regulation of GDF-8signaling by the p38MAPK [J]. Cellular Signalling,2005,17:365-375.
    [97] Langley B, Thomas M, Bishop A, et al. Myostatin inhibits myoblast differentiation by down-regulat-ing MyoD expression [J]. Journal of Biological Chemistry,2000,277:49831-49840.
    [98] Kamanga-Sollo E, Pampusch MS, White ME, et al Role of insulin-like growth factor binding protein(IGFBP)-3in TGF-b and GDF-8(myostatin)-induced suppression of proliferation in porcineembryonic myogenic cell cultures [J]. Journal of Cellular Physiology,2003,197:225-231.
    [99] Costelli P, Carbo N, Busquets S, et al. Reduced protein degradation rates and low expression ofproteolytic systems support skeletal muscle hypertrophy in transgenic mice overexpressing the c-skioncogene [J]. Cancer Letters,2003,200:153-160.
    [100] Sutrave P, Kelly A M and Hughes S H. Ski can cause selective growth of skeletal muscle intransgenic mice [J]. Genes and Development,1990,4:1462-1472.
    [101] d’Albis A, Butler-Browne G S. The hormonal control of myosin isoform expression in skeletalmuscles of mammals [J]. Basic and Applied Myology,1993,3:7-17.
    [102] Semsarian C, Wu M J, Ju Y K, et al. Skeletal muscle hypertrophy is mediated by a Ca2+-dependentcalcineurin signalling pathway [J]. Nature,1999,400:576-581.
    [103] MusaròA, McCullagh K, Paul A, et al. Localized Igf-1transgene expression sustains hypertrophy andregeneration in senescent skeletal muscle [J]. Nature Genetics,2001,27:195-200.
    [104] Lynch G S, Cuffe S A, Plant D R, et al. IGF-I treatment improves the functional properties of fast-and slow-twitch skeletal muscles from dystrophic mice [J]. Neuromuscular Disorders,2001,11:260-268.
    [105] Liu Y W, Shen T S, Randall W R, et al. Signaling pathway in activity-dependent fiber type plasticityin adult skeletal muscle [J] Journal of Muscle Research and Cell Motility,2005,26:13-21.
    [106] Fraysse B, Desaphy J F, Pierno S, et al Decrease in resting calcium and calcium entry associated withslow-to-fast transition in unloaded rat soleus muscle [J]. FASEB Journal,2003,17:1916-1918.
    [107] Schulz R A and Yutzey K E. Calcineurin signaling and NFAT activation in cardiovascular andskeletal muscle development [J]. Developmental Biology,2004,266:1-16.
    [108] Naya F J and Olson E. MEF2: a transcriptional target for signaling pathways controlling skeletalmuscle growth and differentiation [J]. Current Opinion in Cell Biology,1999,11:683-688.
    [109] Wu H, Rothermel B, Kanatous S, et al. Activation of MEF2by muscle activity is mediated through acalcineurin-dependent pathway[J]. EMBO Journal,2001,20:6414-6423.
    [110] Lin J, Wu H, Tarr P T, et al. Transcriptional co-activator PGC-1a drives the formation of slow-twitchmuscle fibres [J]. Nature,2002,418:797-801.
    [111] Swoap S J, Hunter R B, Stevenson E J, et al. The calcineurin-NFAT pathway and muscle fibertypegene expression [J]. American Journal of Physiology-Cell Physiology,2000,279: C915-C924.
    [112] Naya F J, Mercer B, Shelton J, et al.Stimulation of slow skeletal muscle fiber gene expression bycalcineurin in vivo [J]. Journal of Biological Chemistry,2000,275:4545-4548.
    [113] Koh E H, Kim M S, Park J T, et al. Peroxisome proliferator-activated receptor (PPAR)-α activationprevents diabetes in OLETF rats: comparison with PPAR-γactivation [J]. Diabetes,2003,52:2331-2337.
    [114] Yu Y H, Liu B H, Mersmann H J, et al. Porcine peroxisome proliferator-activated receptor γinduces transdifferentiation of myocytes into adipocytes [J]. Journal of Animal Science,2006,84:2655-2665.
    [115] Wang Y X, Lee C H, Tiep S, et al. Peroxisome-proliferator-activated receptorδactivates fatmetabolism to prevent obesity [J]. Cell,2003,113:159-170.
    [116] Oberkofler H, Esterbauer H, Linnemayr V, et al. Peroxisome proliferator-activated receptor (PPAR)γcoactivator-1αrecruitment regulates PPAR subtype specificity [J]. Journal of Biological Chemistry,2002,277:16750-16757.
    [117] Handschin C, Rhee J, Lin J, et al An autoregulatory loop controls peroxisome proliferator-activatedreceptor g coactivator1αexpression in muscle [J]. Proceedings of the National Academy of SciencesUSA,2003,100:7111-7116.
    [118] Miura S, Kai Y, Ono M, et al. Overexpression of peroxisome proliferator-activated receptorγcoactivator-1αdown-regulates GLUT4mRNA in skeletal muscles [J]. Journal of BiologicalChemistry,2003,278:31385-31390.
    [119] Zoltan A, Nathan L, Carl M, et al. The transcriptional coactivator PGC-1βdrives the formation ofoxidative type IIX fibers in skeletal muscle [J]. Cell metabolism,2007,5:35-46
    [120] Vihang A N, Michael D, Ruth T. Y, et al. AMPK and PPARδAgonists Are Exercise Mimetics [J].Cell,2008,134:405-415
    [121] Shi H, Scheffler J M, Pleitner J M, et al. Modulation of skeletal muscle fiber type by mitogenacti-vated protein kinase signaling [J]. The FASEB Journal,2008,22:2990-3000
    [122]杨秋梅. Wnt/β-catenin信号通路调控猪骨骼肌纤维类型变化的初步研究[D].陕西杨凌:西北农林大学硕士学位论文,2011.
    [123] Chang K C. Key signalling factors and pathways in the molecular determination of skeletal musclephenotype [J]. Animal,2007,1:681-698.
    [1] Te Pas M F, De Wit A A, Priem J, et al. Transcriptome expression profiles in prenatal pigs in relation tomyogenesis [J]. Journal of Muscle Research and Cell Motility,2005,26:157-165
    [2] Tang Z, Li Y, Wan P, et al. Long SAGE analysis of skeletal muscle at three prenatal stages inTongcheng and Landrace pigs [J]. Genome Biology,2007,8: R115
    [3] Buckingham M, Vincent S D. Distinct and dynamic myogenic populations in the vertebrate embryo [J].Current Opinion in Genetics&Development,2009,19:444-453
    [4] Lefaucheur L. A second look into fibre typing–relation to meat quality [J]. Meat Science,2010,84:257-270.
    [5] Schiaffino S, Gorza L, Sartore S, et al. Three myosin heavy chain isoforms in type2skeletal musclefibers [J]. Journal of Muscle Research and Cell Motility,1989,10:197-205
    [6] Schiaffino S, Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functionalsignificance [J]. Physiological Reviews,1996,76:371-423.
    [7] Cox R D, Buckingham M E. Actin and myosin genes are transcriptionally regulated during mouseskeletal muscle development [J]. Developmental Biology,1992,149:228-234
    [8] Short K R, Vittone J L, A Bigelow M L, et al. Changes in myosin heavy chain mRNA and proteinexpression in human skeletal muscle with age and endurance exercise training [J]. Journal of AppliedPhysiology,2005,99:95-102
    [9] Eggert J M, Depreuxf F S, Schinkel A P, et al. Myosin heavy chain isoforms account for variation inpork quality [J]. Meat Science,2002,61:117-126
    [10] Depreuxf F S, Grant A L, Derrard D E. Influence of halothane genotype and body-weight on myosinheavy chain composition in pig muscle as related to meat quality [J]. Livestock Production Science,2002,73:265-273.
    [11] Park B Y, Kim N K, Lee C S, et al. Effect of fiber type on postmortem proteolysis in longissimusmuscle of Landrace and Korean native black pigs [J]. Meat Science,2007,77:482-491
    [12] Kim N K, Lim J H, Song M J, et al. Comparisons of longissimus muscle metabolic enzymes andmuscle fiber types in.Korean and western pig breeds [J]. Meat Science,2008,78:455-460
    [13]呼红梅,朱荣生,张印,等.莱芜猪和杜洛克猪背最长肌肌球蛋白重链组成[J].中国农业科学,2008,41:3754-3759
    [14] Savolainen J, Vornanen M. Myosin heavy chains in skeletal muscles of the common shrew (Sorexaraneus): absence of a slow isoform and transitions of fast isoforms with ageing [J]. Acta physiologicaScandinavica,1995,155:233-239.
    [15] Tanabe R, Muroya S, Chikuni K. Expression of myosin heavy chain isoforms in porcine muscledetermined by multiplex PCR [J]. Journal of Food Science,1999,64:222-225.
    [16] Wydro R M, Nguyen H T, Gubits R M, Nadal-Ginard B. Characterization of sarcomeric myosin heavychain genes [J]. Journal of Biological Chemistry,1983,258:670-678.
    [17] Mahdavi V, Izumo S, Nadal-Ginard B. Developmental and hormonal regulation of sarcomeric myosinheavy chain gene family [J]. Circulation research,1987,60:804-814.
    [18] Staron, R.S., Johnson, P. Myosin polymorphism and differential expression in adult human skeletalmuscle [J]. Comparative Biochemistry and Physiology B,1993,106:463-475.
    [19] Pette D, Staron R S. Myosin isoforms, muscle fiber types, and transitions [J]. Microscopy ResearchAnd Technique,2000,50:500-509.
    [20] Wieczorek D F, Periasamy M, Butler-Browne G S, et al. Coexpression of multiple myosin heavy chaingenes, in addition to a tissue-specific one, in extraocular musculature [J]. Journal of Cell Biology,1985,101:618-629.
    [21] Périé S, Agbulut O, St Guily J L, et al. Myosin heavy chain expression in human laryngeal musclefibers [J]. Ann Otol Rhinol Laryngol,2000,109:216-220.
    [22] Haddad F, Qin A X, et al. Effects of isometric training on skeletal myosin heavy chain expression [J].Journal of Applied Physiology,1998,84:2036-2041.
    [23] da Costa N, Blackley R, Alzuherri H, et al.Quantifying the temporo-spatial expression of porcinepostnatal skeletal myosin heavy chain genes [J]. Journal of histochemistry and cytochemistry,2002,50:353-364.
    [24] Zhao R Q, Yang X J, Xu Q F, et al. Expression of GHR and PGC-1alpha in association with changesof MyHC isoform types in longissimus muscle of Erhualian and Large White pigs (Sus scrofa) duringpostnatal growth [J]. Animal Science,2004,79:203-211.
    [25]杨飞云,陈代文,黄金秀,等.猪背最长肌肌纤维类型的发育性变化及品种与营养影响特点[J].畜牧兽医学报,2008,39:1701-1708.
    [26]杨晓静.猪骨骼肌生长及肌纤维类型分布的分子机理研究[D].南京:南京农业大学,2004.
    [27] Hamalainen N, Pette D. Coordinated fast-to-slow transitions ofmyosin and SERCA isoforms inchronically stimulated muscles of euthyroid and hyperthyroid rabbits [J]. Journal of Muscle Researchand Cell Motility,1997,18:545-554.
    [28] Reggiani C, Bottinelli R, Stienen G J. Sarcomeric myosin isoforms: fine tuning of a molecular motor[J]. News in Physiological Sciences,2000,15:26-33.
    [29] Baldwin K M, Haddad F. Effects of different activity and inactivity paradigms on myosin heavy chaingene expression in striated muscle [J]. Journal of Applied Physiology,2001,90:345-357
    [30] DelGaudio J M&Sciote J J. Changes in myosin expression in denervated laryngeal muscle [J]. AnnOtol Rhinol Laryngol,1997,106:1076-108
    [31] Shiotani A,&Flint P W. Myosin heavy chain composition in rat laryngeal muscles after denervation[J]. Laryngoscope,1998,108:1225-1229.
    [32] Caiozzo V J, Wu Y Z, Baker M J, et al. Effects of denervation on cell cycle control in laryngeal muscle[J]. Archives of Otolaryngology—Head&Neck Surgery,2004,130:1056-1068.
    [33] Rhee H S, Lucas C A&Hoh J F. Fiber types in rat laryngeal muscles and their transformations afterdenervation and reinnervation [J]. Journal of Histochemistry and Cytochemistry,2004,52:581-590.
    [34] Li Z B, Lehar M, Samlan R, et al. Proteomic analysis of rat laryngeal muscle following denervation [J].Proteomics,2005,5:4764-4776.
    [35] Diffee G M., Haddad F, Herrick R E, et al. Control of myosin heavy chain expression: interaction ofhypothyroidism and hindlimb suspension [J]. American Journal of Physiology,1991,261:C1099-C1106.
    [36] Caiozzo V J, Haddad F, Baker M J, et al. Influence of mechanical loading on myosin heavy-chainprotein and mRNA isoform expression [J]. Journal of Applied Physiology,1996,80:1503-1512.
    [37] Reilly M E, McKoy G, Mantle D, et al. Protein and mRNA levels of the myosin heavy chain isoformsIbeta, IIa, IIx and IIb in type I and type II fibre-predominant rat skeletal muscles in response tochronic alcohol feeding [J]. Journal of Muscle Research and Cell Motility,2000,21:763-773.
    [38] Serrano A L, Murgia M, Pallafacchina G, et al. Calcineurin controls nerve activity-dependentspecification of slow skeletal muscle fibers but not muscle growth [J]. Proceedings of the NationalAcademy of Sciences of USA,2001,98:13108-13113.
    [39] Sanchez H, Chapot R, Banzet S, et al. Quantification by real-time PCR of developmental and adultmyosin mRNA in rat muscles [J]. Biochemical and Biophysical Research Communications,2006,340:165-174
    [40] McKoy G., Leger M E, Bacou F, et al. Differential expression of myosin heavy chain mRNA andprotein isoforms in four functionally diverse rabbit skeletal muscles during pre-and postnataldevelopment [J]. Developmental Dynamics,1998,211:193-203.
    [41] Haddad F, Qin A X, Bodell P W, et al. Intergenic transcription and developmental regulation of cardiacmyosin heavy chain genes [J]. American Journal of Physiology (Heart and Circulatory Physiology),2008,294: H29-H40.
    [42] Wang J Q, Li X, Yang X J, et al. Maternal dietary protein induces opposite myofiber type transition inMeishan pigs at weaning and finishing stages [J]. Meat Science,2011,89:221-227
    [43] Lefaucheur L,Vigneronn P. Post-natal changes in some histochemical and enzymatic characteristics ofthree pig muscle [J]. Meat Science,1986,16:199-216.
    [44] Lefaucheur L. Myofiber typing and pig meat production [J]. Slovenian Veterinary Research,2001,38:5-33
    [45] Picard B, Lefaucheur L, Berri C, et al. Muscle fibre ontogenesis in farm animal species [J].Reproduction Nutrition Development,2002,42:415-431
    [46] Suzuki A, Kojima N, Ikeuchi Y, et al. Carcass composition and meat quality of Chinese purebred andEuropean×Chinese crossbred pigs [J]. Meat Science,1991,29:31-38
    [47] Chang K C. Key signaling factors and pathways in the molecular determination of skeletal musclephenotype [J]. Animal,2007,1:681-698.
    [1]薛尚军,杨晓奋,刘宏,等.中国地方猪种的肉质特性[J].国外畜牧学-猪与禽,2011,31(2):92-94.
    [2]沈元新,徐继初.金华猪及其杂种肌肉组织学特性与肉质的关系[J].浙江大学学报(农业与生命科学版),1984,10:265-272.
    [3] Huan Y J, Zhou G H, Zhao G M, et al. Changes in flavor compounds of dry-cured Chinese Jinhua hamduring processing [J]. Meat Science,2005,71:291-299
    [4] Zhou G H, Zhao G M. Biochemical changes during processing of traditional Jinhua ham [J]. MeatScience,2007,77:114-120
    [5] Larzul C, Lefaucheur L, Ecolan P, et al. Phenotypic and genetic parameters for longissimus muscle fibrecharacteristics in relations to growth, carcass, and meat quality traits in large white pigs[J]. Journal ofAnimal Science,1997,75:3126-3137.
    [6] Lefaucheur L. A second look into fiber typing-relation to meat quality [J]. Meat Science,2010,84:257-270.
    [7] Choi Y M, Ryu Y C, Kim B C. Influence of myosin heavy-and light chain isoforms on earlypostmortem glycolytic rate and pork quality [J]. Meat Science,2007,76:281-288.
    [8] Essen-Gustavsson B, Fjelkner-Modig S. Skeletal muscle characteristics in muscles of pigs in relation tosensory properties of meat [J]. Meat Science,1985,13:33-45
    [9] Lefaucheur L, Milan D, Ecolan P, et al. Myosin heavy chain composition of different skeletal musclesin Large White and Meishan pigs [J]. Journal of Animal Science,2004,82:1931-1941.
    [10] Guo J, Shan T, Wu T, et al. Comparisons of different muscle metabolic enzymes and muscle fibertypes in Jinhua and Landrace pigs [J]. Journal of Animal Science,2011,89:185-191
    [11] Larzul C, Lefaucheur L, Ecolan P, et al. Phenotypic and genetic parameters for longissimus musclefibre characteristics in relations to growth, carcass, and meat quality traits in large white pigs [J].Journal of Animal Science,1997,75:3126-3137.
    [12] Karlsson A H, Klont R E&Fernandez X. Skeletal muscle fibres as factors for pork quality [J].Livestock Production Science,1999,60:255-269.
    [13] Chang K C, Costa N D, Blackley R, et al. Relationships of myosin heavy chain fiber types to meatquality traits in traditional and modern pigs [J]. Meat Science,2003,64:93-103
    [14] Joo S T, Kauffman R G, Kim B C, et al. The relationship of sarcoplasmic and myofibrillar proteinsolubility to color and water-holding capacity in porcine longissimus muscle [J]. Meat Science,1999,52:291-297.
    [15] Scheffler T L, Park S, Gerrard D E. Lessons to learn about postmortem metabolism using theAMPKγ3R200Q mutation in the pig [J]. Meat Science,2011,89:244-250
    [16]陈伯祥.肉与肉制品工艺学[M].南京:江苏科学技术出版社,1993.
    [17]孔保华.畜产品加工储藏新技术[M].北京:科学出版社,2007.
    [18] Bowker B C, Grandt A L, Swartz D R, et al. Myosin heavy chain isoforms influence myofibrillarATPase activity under simulated postmortem pH, calcium, and temperature conditions [J]. MeatScience,2004,67:139-147
    [19] Ryu Y C, Choi Y M, Kim B C. The relationship between muscle fiber characteristics, postmortemmetabolic rate, and meat quality of pig longissimus dorsi muscle [J]. Meat Science,2005,71:351-357
    [20] Ryu Y C, Choi Y M, Kim B C. Variations in metabolite contents and protein denaturation of thelongissimus dorsi muscle in various porcine quality classifications and metabolic rates [J]. MeatScience,2005,71:522-529
    [21] Depreux F F S, Grant A L, Gerrard D E. Influence of halothane genotype and body-weight on myosinheavy chain composition in pig muscle as related to meat quality [J]. Livestock Production Science,2002,73:265-273
    [22] Kovanen V, Suominen H, Heikkinen E. Mechanical properties of fast and slow skeletal muscle withspecial reference to collagen and endurance training [J]. Journal of Biomechanics,1984,17:725-727,729-735
    [23] Budohoski L, Gorski J, Nazar K, et al. Triacylglycerol synthesis in the different skeletal muscle fibersections of the rat [J]. American Journal of Physiology,1996,271: E574-581.
    [24] Gondret F, Mourot J, Bonneau M. Comparison of intramuscular adipose tissue cellularity in musclesdiffering in their lipid content and fibre type composition during rabbit growth Livestock ProductionScience,1998,54(1):1-10
    [25] Karlsson A H, Klont R E&Fernandez X. Skeletal muscle fibres as factors for pork quality [J].Livestock Production Science,1999,60:255-269.
    [26] De Feyter H M, Schaart G, Hesselink M K, et al. Regional variations in intramyocellular lipidconcentration correlate with muscle fiber type distribution in rat tibialis anterior muscle [J]. MagneticResonance in Medicine,2006,56:19-25
    [27] Park B Y, Kim N K, Lee C S, et al. Effect of fiber type on postmortem proteolysis in longissimusmuscle of Landrace and Korean native black pigs [J]. Meat Science,2007,77:482-491
    [28] Hu H M, Wang J Y, Zhu R S, et al. Effect of myosin heavy chain composition of muscles on meatquality in Laiwu pigs and Duroc [J]. Science in China Series C: Life Sciences,2008,51:127-132
    [29] Costa P, Roseiro L C, Bessa R J B, et al. Muscle fiber and fatty acid profiles of Mertolenga-PDO meat[J]. Meat Science,2008,78:502-512.
    [30] Leseigneur-Meynier A&Gandemer G. Lipid composition of pork muscle in relation to the metabolictype of the fibres [J]. Meat Science,1991,29:229-241.
    [31] Stadtman E R. Oxidation of free amino acids and amino acids residues in proteins by radiolysis and bymetal-catalyzed reactions [J]. Annual Review of Biochemistry,1993,62:797-821.
    [32] Rowe L J, Maddock K R, Lonergan S M, et al. Influence of early postmortem protein oxidation onbeef quality [J]. Journal of Animal Science,2004,82:785-793.
    [33] Choi Y M, Lee S H, Choe J H, et al. Protein solubility is related to myosin isoforms, muscle fibertypes, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle [J].Livestock Science,2010,127:183-191.
    [34]周光宏.肉品学[M].北京:中国农业科技出版社,1999.
    [35] Gil M, Oliver M à, Gispert M, Dierstre A, et al. The relationship between pig genetics, myosin heavychain I, biochemical traits and quality of M. longissimus thoracis [J]. Meat Science,2003,65:1063-1070
    [36] Olivan M, Martinez A, Osoro K, et al. Effect of muscular hypertrophy on physico-chemical,biochemical and texture traits of meat from yearling bulls [J]. Meat Science,2004,68:567-575
    [37] Ramirez J A, Oliver M à, Pla M, et al. Effect of selection for growth rate on biochemical, quality andtexture characteristics of meat from rabbits [J]. Meat Science,2004,67:617-624
    [1] Henckel P, Karlsson A, Jensen M T, et al. Metabolic conditions in porcine Longissimus muscleimmediately pre-slaughter and its influence on peri-and post mortem energy metabolism [J]. MeatScience,2002,62:145-155.
    [2] Gaitanos G C, Williams C, Boobis L H, et al. Human muscle metabolism during intermittent maximalexercise [J]. Journal of Applied Physiology,1993,75:712-911.
    [3] Brooks G A. Mammalian fuel utilization during sustained exercise [J]. Comparative Biochemistry andPhysiology,1998,120:89-107.
    [4] Brooks G A, But Z C E. Role of mitochondrial lactate dehydrogenase and lactate oxidation in theintracellular lactate shuttle [J]. Proceedings of the National Academy of Sciences,1999,96:1129-1134
    [5] Bendall J R. The shortening of rabbit muscles during rigor mortis: Its relation to the breakdown ofadenosine triphosphate and creatine phosphate and to muscular contraction [J]. The Journal ofPhysiology,1951,114:71-88.
    [6] Hambrecht E, Eissen J J, Newman D J, et al. Preslaughter handling effects on pork quality andglycolytic potential in two muscles differing in fiber type composition [J]. Journal of Animal Science,2005,83:900-907.
    [7] Ryu Y C&Kim B C. The relationship between muscle fiber characteristics, postmortem metabolic rate,and meat quality of pig longissimus dorsi muscle [J]. Meat Science,2005,71:351-357.
    [8] Gil M, Oliver M à, Gispert M, et al. The relationship between pig genetics, myosin heavy chain I,biochemical traits and quality of M. longissimus thoracis [J]. Meat Science,2003,65:1063-1070
    [9] Olivǎn M, Martinez A, Osoro K, et al. Effect of muscular hypertrophy on physico-chemical,biochemical and texture traits of meat from yearling bulls [J]. Meat Science,2004,68:567-575
    [10] Ramirez J A, Oliver M à, Pla M, et al. Effect of selection for growth rate on biochemical, quality andtexture characteristics of meat from rabbits [J]. Meat Science,2004,67:617-624
    [11] Sazili A Q, Parr T, Sensky P L, et al. The relationship between slow and fast myosin heavy chaincontent, calpastatin and meat tenderness in different ovine skeletal muscles [J]. Meat Science,2005,69:17-25
    [12] Bowker B C, Grant A L, Swartz D R, et al. Myosin heavy chain isoforms influence myofibrillarATPase activity under simulated postmortem pH, calcium, and temperature conditions [J]. MeatScience,2004,67:139-147
    [13] Li X, Yang X, Shan B, et al. Meat quality is associated with muscle metabolic status but not contractilemyofiber type composition in premature pigs [J]. Meat Science,2009,81:218-223
    [14]洪平,刘虎威,靳光华,黎燕,杨奎生.高效液相色谱法测定骨骼肌ATP、ADP、AMP、NAD+、NADH含量[J].中国运动医学杂志,2002,21(1):57-60
    [15]于文兵.核能补充剂对大鼠骨骼肌高能磷酸化合物变化的影响[J].南京体育学院学报(自然科学版),2004,3(2):6-8,70
    [16] Berg E P, Allee G L. Creatine monohydrate supplemented in swine finishing diets and fresh pork quality:I. A controlled laboratory experiment [J]. Journal of Animal Science,2001,79:3075-3080.
    [17] Young J F, Bertram H C, Rosenvold K, et al. Dietary creatine monohydrate(CMH) affects qualityattributes of Duroc but not Landrace pork [J]. Meat Science,2005,70:717-725.
    [18] Bee G, Biolley C, Guex G, et al. Effects of available dietary carbohydrate and preslaughter treatmenton glycolytic potential, protein degradation, and quality traits of pig muscles. Journal of AnimalScience,2006,84:191-203.
    [19] Hamilton D N, Ellis M, Hemann M D, et al The impact of longissimus glycolytic potential andshort-term feeding of magnesium sulfate heptahydrate prior to slaughter on carcass characteristics andpork quality [J]. Journal of Animal Science,2002,80:1586-1592.
    [20] Rosenvold K, Paterson J S, Lwerke H N, et al. Muscle glycogen stores and meat quality as affectedby strategic finishing feeding of slaughter pigs [J]. Journal of Animal Science,2001,79:382-391.
    [21] O’Quinn P R, Andrews B S, Goodband R D, et al. Effects of modified tall oil and creatinemonohydrate on growth performance, carcass characteristics, and meat quality of growing-finishingpigs [J]. Journal of Animal Science,2000,78:2376-2382.
    [22] Maddock R J, Bindner B S, Carr S N, et al. Creatine monohydrate supplementation and the quality offresh pork in normal and halothane carrier pigs [J]. Journal of Animal Science,2002,80:997-1004.
    [23] Han J Z, Gu Z Y, Wu J S, et al. Effects and mechanism: creatine monohydrate on carcasscharacteristics and meat quality of finishing swine [J]. Journal of the Chinese Cereals and OilsAssociation,2007,22:101-106
    [24] Hou M D, Zeng S Y. Biochemical methods to appraise meat quality [J]. Food Science,2000,21:121-123
    [25] Li L A, Xia D, Bao E D, et al. Erhualian and Pertrain pigs exhibit distinct behavioral, endocrine andbiochemical responses during transport [J]. Livestock Science,2008,113:169-177.
    [26]Briskey E J. Etiological status and associated studies of pale, soft, exudative porcine musculature [J].Advances in Food Research,1964,13:89-178.
    [27] Honikel K O, Kim C J. Causes of the development of PSE pork [J]. Fleischwirtsch,1986,66:349-353
    [28] Offer G, Knight P K, Jeacocke R, et al. The structural basis of the water-holding, appearance andtoughness of meat and meat products [J]. Food Microstructure,1989,8:151-170.
    [29] Joo S T, Kauffman R G, Kim B C, et al. The relationship of sarcoplasmic and myofibrillar proteinsolubility to colour and water-holding capacity in porcine longissimus muscle [J]. Meat Science,1999,52:291-297
    [30] Miller K D,Ellis M,Bidner B,et al. Porcine longissimus glycolytic potential level effects on growthperformance, carcass, and meat quality characteristic [J]. Journal of Muscle Foods,2000,11:169-181.
    [31] Scheffler T L, Park S, Gerrard D E. Lessons to learn about postmortem metabolism using theAMPKγ3R200Q mutation in the pig [J]. Meat Science,2011,89:244-250
    [32] Essén-Gustavsson B, Henriksson J. Enzyme levels in pools of microdissected human muscle fibres ofidentified type [J]. Acta Physiologica Scandinavica,1984,120:505-515.
    [33] Monin G, Mejenes-Quijano A, Talmant A, et al. Influence of breed and muscle metabolic type onmuscle glycolytic potential and meat pH in pigs [J]. Meat Science,1987,20:149-158.
    [34] Choi Y M, Ryu Y C, Kim B C. Influence of myosin heavy-and light-chain isoforms on earlypostmortem glycolytic rate and pork quality [J]. Meat Science,2007,76:281-288.
    [35] Choe J H, Choi Y M, Lee S H, et al. The relation between glycogen, lactate content and muscle fibertype composition, and their influence on postmortem glycolytic rate and pork quality [J]. MeatScience,2008,80:355-362.
    [36] Wallimann T, Wyss M, Brdiczka D, et al. Intracellular compartmentation, structure and function of thecreatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine’circuit for cellular energy homeostasis [J]. The Biochemical Journal,1992,281:21-40.
    [37] Vaarmann A, Fortin D, Veksler V, et al. Mitochondrial biogenesis in fast skeletal muscle of CKdeficient mice [J]. Biochimica et Biophysica Acta,2008,1777:39-47.
    [38] Bottinelli R, Reggiani C. Human skeletal muscle fibers: molecular and functional diversity [J].Progress in Biophysics and Molecular Biology,2000,73:195-262.
    [1] Zhao X, Mo D, Li A, et al. Comparative analyses by sequencing of transcriptomes during skeletalmuscle development between pig breeds differing in muscle growth rate and fatness [J]. PLoS One,2011,6: e19774.
    [2] Hollung K, Veiseth E, Jia X H, et al. Application of proteomics to understand the molecularmechanisms behind meat quality [J]. Meat Science,2007,77:97-104.
    [3] Mullen A M, Stapleton P C, Corcoran D, et al. Understanding meat quality through the application ofgenomic and proteomic approaches [J]. Meat Science,2006,74:3-16.
    [4] Tang Z, Li Y, Wan P, et al. Long SAGE analysis of skeletal muscle at three prenatal stages inTongcheng and Landrace pigs [J]. Genome Biology,2007,8: R115.
    [5] Kim N K, Lim J H, Song M J, et al. Developmental proteomic profiling of porcine skeletal muscleduring postnatal development [J]. Asian Australas Journal of Animal Science,2007,20:1612-1617
    [6] Li Y, Xu Z, Li H, et al. Differential transcriptional analysis between red and white skeletal muscle ofChinese Meishan pigs [J]. International Journal Biological Science,2010,6:350-360.
    [7]冯宪超,徐幸莲,周光宏.蛋白质组学在肉品学中的应用[J].食品科学,2009,30:277-281
    [8]张凯.猪不同肌纤维类型骨骼肌的基因组表达谱差异[D].四川雅安:四川农业大学博士学位论文,2010.
    [9] Tian Q, Stepaniants S B, Mao M, et al. Integrated genomic and proteomic analyses of gene expressionin mammalian cells [J]. Molecular Cell Proteomics,2004,3:960-969.
    [10] Chen G, Gharib T G, Huang C C, et al. Discordant protein and mRNA expression in lungadenocarcinomas [J]. Molecular Cell Proteomics,2002,1:304-313.
    [11] Yi Z P, Bowen B P, Hwang H, et al. Global relationship between the proteome and transcriptome ofhuman skeletal muscle [J]. Journal of Proteome Research,2008,7:3230-3241.
    [12] Hansson O, Donsmark M, Ling C, et al. Transcriptome and proteome analysis of soleus muscle ofhormone-sensitive lipase-null mice [J]. Journal of Lipid Research,2005,46:2614-2623.
    [13] Chelh I, Meunier B, Picard B, et al. Molecular profiles of Quadriceps muscle in myostatin-null micereveal PI3K and apoptotic pathways as myostatin targets [J]. BMC Genomics,2009,10:196.
    [14] Xu Y J, Qian H, Feng X T, et al. Differential proteome and transcriptome analysis of porcine skeletalmuscle during development [J]. Journal of Proteomics,2012, online16January
    [15]钱小红,贺福初.蛋白质组成:理论与方法[M].北京:科学出版社,2003.
    [16] Locke M, Atkinson B G, Tanguay R M. Shifts in type I fiber proportion in rat hind limb muscle areaccompanied by changes in HSP72content [J]. American Journal of Physiology-Cell Physiology,1994,35: C1240-C1246
    [17] Mattson J P, Ross C R, Kilgore J L, et al. Induction of mitochondrial stress proteins followingtreadmill running [J]. Medicine and Science in Sports and Exercise,2000,32:365-369
    [18] Dalman F G, Scherrer I C, Taylor I P, et al. Localization of the90-kDa heat shock protein-binding sitewithin the hormone-binding domain of the glucocorticoid receptor by peptide competition [J]. Journalof Biology and Chemistry,1991,266:3482-3490
    [19]王海涛,刘玉倩,刘建国,等.骨骼肌细胞铁代谢的研究进展[J].体育学刊,2009,16:96-100
    [20]邝永玲,袁伟杰. Gc球蛋白生物学特性及与肝脏疾病的关系[J].中国实用内科杂志,2010,30(增刊1):85-87
    [21]李爽,艾英伟,阿拉木斯,等.黄芪总苷对力竭运动大鼠骨骼肌中ATP酶活性的影响[J].体育科技文献通报,2010,18(3):110-111.
    [22] Holm C, Osterlund T, Laurell H, et al. Molecular mechanisms regulating hormone-sensive lipase asand lipolysis [J]. Annu Rev Nutr,2000,20:365-393.
    [23] Fujii J, Otsu K, Zorzato F, et al. Identification of a mutation in porcine ryanodine receptor associatedwith malignant hyperthermia [J]. Science,253(5018):448-451
    [24]蒋岸岸,李明洲,官久,等.2个猪品种的背最长肌组织中兰尼定受体(RYR1)基因表达的发育性变化[J].基因组学与应用生物学,2010,29(3):485-489
    [25] Camps M, Nichols A and Arkinstall S. Dual specificity phosphatases: a gene family for control ofMAP kinase function [J]. FASEB J.,2000,14:6-16
    [26] Wu J J, Roth R J, Anderson E J, et al. Mice lacking MAP kinase phosphatase-1have enhanced MAPkinase activity and resistance to dietinduced obesity [J]. Cell Metabolism,2006,4:61-73
    [27] Murgia M, Serrano A L, Calabria E, et al. Ras is involved in nerveactivity-dependent regulation ofmuscle genes [J]. Nature Cell Biology,2000,2:142-147
    [28] Higginson J, Wackerhage H, Woods N, et al. Blockades of mitogen-activated protein kinase andcalcineurin both change fibre-type markers in skeletal muscle culture [J]. Pflugers Archiv-europeanjournal of physiology,2002,445:437-443
    [29] Roth R J, Le A M, Zhang L, et al. MAPK phosphatase-1facilitates the loss of oxidative myofibersassociated with obesity in mice [J]. Journal of Clinical Investigation,2009,119:3817-3829
    [30] Shi H, Zeng C, Ricome A., et al. Extracellular signal-regulated kinase pathway is differentiallyinvolved in beta agonist-induced hypertrophy in slow and fast muscles [J]. America Journal of Physiol.2007,292: C1681-C1689
    [31] Shi H, Scheffler J M, Pleitner J M, et al. Modulation of skeletal muscle fiber type by mitogenactivatedprotein kinase signaling [J]. The FASEB Journal,2008,22:2990-3000.
    [32] Meissner J D, Chang K C, Kubis H P, et al. The p38alpha/beta MAP kinases mediate recruitment ofCBP to preserve fast myosin heavy chain IId/x gene activity in myotubes [J]. Journal of BiologicalChemistry,2007,282:7265-7275.
    [33] Foahay K, Rodriguez G, Hoel B, et al. JAK2/STAT3directs cardiomyogenesis within murineembryonic stem cells in vitro [J]. Stem Cells,2005,23:530-543.
    [34] Bromberg J A, and Darnell Jr J E. The role of STATs in transcriptional control and their impact oncellular function [J]. Oncogene,2000,19:2468-2473.
    [35] Xiong H, Zhang Z G, Tian X Q, et al. Inhibition of JAK1,2/STAT3signaling induces apoptosis, cellcycle arrest, and reduces tumor cell invasion in colorectal cancer cells [J]. Neoplasia,2008,10:287-297
    [36]马佩云,孙超,张忠品,等. JAK2/STAT3信号通路对小鼠骨骼肌发育和能量代谢相关基因mRNA表达的影响[J].农业生物技术学报,2010,18:951-955.
    [37] Klover Peter, Chen W P, Zhu B M, et al. Skeletal muscle growth and fiber composition in mice areregulated through the transcription factors STAT5a/b: linking growth hormone to the androgen [J].The FASEB Journal,2009,23:3140-3148
    [38] Chang K C. Key signaling factors and pathways in the molecular determination of skeletal musclephenotype [J]. Animal,2007,1:682-698
    [39] Delling U, Tureckova J, Lim H W, et al. A calcineurin-NFATc3-dependent pathway regulates skeletalmuscle differentiation and slow myosin heavy-chain expression [J]. Molecular and Cellular Biology,2000,20:6600-6611.
    [40] Tee J M, Carina van Rooijen, Rick Boonen, et al. Regulation of Slow and Fast MuscleMyofibrillogenesis by Wnt/b-Catenin and Myostatin Signaling [J]. PLoS ONE,2009,4(6), e5880:1-12.
    [41]杨秋梅. Wnt/β-catenin信号通路调控猪骨骼肌纤维类型变化的初步研究[D].陕西杨凌:西北农林大学硕士学位论文,2011
    [42] Kinoshita N, Iioka H, Miyakoshi A. PKC delta is essential for Dishevelled function in a noncanonicalWnt pathway that regulates Xenopus convergent extension movements [J]. Genes and Development,2003,17:1663-1676.
    [43]袁媛,刘月光,史新娥,等.调控骨骼肌纤维类型转化的信号通路[J].中国生物化学与分子生物学报,2010,26:796-801.
    [1] Harrison A P, Rowlerson A M, Dauncey M J. Selective regulation of myofiber differentiation by energystatus during postnatal development [J]. American Journal of Physiology,1996,39: R667-R674.
    [2] Lefaucheur L, Ecolan P, Barzic Y M et al, Early postnatal food intake alters myofiber maturation in pigskeletal muscle [J]. Journal of Nutrition,2003,133:140-147.
    [3] Bee G. Effect of early gestation feeding,birth weight,and gender of progeny on muscle fibercharacteristics of pigs at slaughter[J]. Journal of Animal Science,2004,82:826-836.
    [4] Nuno da Costa, Christine McGillivray, Qianfan Bai, et al. Restriction of Dietary Energy and ProteinInduces Molecular Changes in Young Porcine Skeletal Muscles [J]. Journal of Nutrition,2004,134:2191-2199.
    [5] Wang J Q, Li X, Yang X J, et al. Maternal dietary protein induces opposite myofiber type transition inMeishan pigs at weaning and finishing stages [J]. Meat Science,2011,89:221-227.
    [6] Young J F, Bertram H C, Rosenvold K, et al. Dietary creatine monohydrate (CMH) affects qualityattributes of Duroc but not Landrace pork.[J]. Meat Science,2005,70:717-725.
    [7] Maddock R J, Bidner B S, Carr S N, et al. Creatine monohydrate supplementation and the quality offresh pork in normal and halothane carrier pigs [J]. Journal of Animal Science,2002,80:997-1004.
    [8] Dugan M E R, Aalhus J L&Kramer J K G. Conjugated linoleic acid pork research [J]. AmericanJournal of Clinical Nutrition,2004,79:1212S-1216S.
    [9] Corino C, Pastorelli G, Douard V, et al. L’acide linole’ ique conjugue’ en nutrition porcine [J]. INRAProductions Animales,2006,19:39-46.
    [10]黄金秀,杨飞云,刘作华,等.共轭亚油酸对体外培养的猪骨骼肌肌纤维类型组成的影响[J].畜牧兽医学报,2010,41:295-300
    [11] Chin S F, Storkson J M, Albright K J, et al. Conjugated linoleic acid is a growth factor for rats asshown by enhanced weight gain and improved feed efficiency [J]. Journal of Nutrition,1991,124:2344-2349.
    [12] Park Y, Albright K J, Liu W, et al. Effect of conjugated linoleic acid on body composition in mice [J].Lipids,1997,32:853-858.
    [13]杨得坡,曾晓晖,林海燕,等.共轭亚油酸钙营养性改善机体肌肉组成的实验研究[J].中国油脂,2006,31:45-47
    [14] Balsom P D, So¨derlund K, Sjo¨ din B. Skeletal muscle metabolism during short durationhigh-intensity exercise: Influence of creatine supplementation [J]. Acta Physiologica Scandinavia,1995,154:303-310.
    [15] Juhn M S. Oral creatine supplementation [J]. The Physician and Sports medicine,1999,27:47–89.
    [16] Kutz M R&Gunter M J. Creatine monohydrate supplementation on body weight and percent body fat[J]. Journal of Strength and Conditioning Research,2003,17:817-821.
    [17] Berg E P&Allee G L. Creatine monohydrate supplemented in swine finishing diets and fresh porkquality. I: a controlled laboratory experiment [J]. Journal of Animal Science,2001,79:3075-3080.
    [18] Stahl C A&Berg E P. Growth parameters and meat quality of finishing hogs supplemented withcreatine monohydrate and a high glycemic carbohydrate for the last30days of production [J]. MeatScience,2003,64:169-174.
    [19] Snow R J, Murphy R M. Factors Influencing Creatine Loading into Human Skeletal Muscle [J].Exercise and Sport Sciences Reviews,2003,31:154-158.
    [20] Young J F, Bertram H C, Theil P K, et al. In vitro and in vivo studies of creatine monohydratesupplementation to Duroc and Landrace pigs [J]. Meat Science,2007,76:342-351.
    [21] Rosenvold K, Bertram H C, Young J F. Dietary creatine monohydrate has no effect on pork quality ofDanish crossbred pigs [J]. Meat Science,2007,76:160-164.
    [22]韩新燕,许梓荣,邵明丽,等.一水肌酸对肥育猪胴体组成及肌肉系水力的影响[J].动物营养学报,2007,19:401-406.
    [23] Corino C, Magni S, Pastorelli G, et al. Effect of conjugated linoleic acid on meat quality, lipidmetabolism, and sensory characteristics of dry-cured hams from heavy pigs [J]. Journal of AnimalScience,2003,81:2219-2229.
    [24] Kennedy A, Martinez K, Schmidt S, et al. Antiobesity mechanisms of action of conjugated linoleicacid [J]. Journal of Nutritional Biochemistry,2010,21:171-179
    [25] Dugan M E R, Aalhus J L, Jeremiah L E, et al. The effects of feeding conjugated linoleic acid onsubsequent pork quality [J].Canadian Journal of Animal Science,1999,79:45-51.
    [26] Wiegand B R, Parrish Jr F C, Swan J E, et al. Conjugated linoleic acid improves feed efficiency,decreases subcutaneous fat and improves certain aspects of meat quality in stress-genotype pigs [J].Journal of Animal Science,2001,79:2187-2195.
    [27] Joo S T, Lee J L, Ha Y L, et al. Effects of dietary conjugated linoleic acid on fatty acid composition,lipid oxidation, color, and water-holding capacity of pork loin [J]. Journal of Animal Science,2002,80:108-112.
    [28] Bee G. Dietary conjugated linoleic acids affect tissue lipid composition but not de novo lipogenesis infinishing pigs [J]. Animal Research,2001,50:383-399.
    [29] Smith S B, Hively T S, Cortese G M, et al. Conjugated linoleic acid depresses the delta-9desaturaseindex and stearoyl coenzyme A desaturase enzyme activity in porcine subcutaneous adipose tissue [J].Journal of Animal Science,2002,80:2110-2115.
    [30] Martín D, Antequera T, González E, et al. Changes in the fatty acid profile of the subcutaneous fat ofswine throughout fattening as affected by dietary conjugated linoleic acid and monounsaturated fattyacids [J]. Journal of Agricultural and Food Chemistry,2007,55:10820-10826.
    [31] Cordero G, Isabel B, Menoyo D, et al. Dietary CLA alters intramuscular fat and fatty acid compositionof pig skeletal muscle and subcutaneous adipose tissue [J]. Meat Science,2010,85:235-239
    [32]杜瑞平,高民,卢德勋. t10,c12-CLA对猪皮下脂肪和背最长肌组织脂类代谢的影响[J].饲料工业,2010,31(19):12-16
    [33] Tischendorf F, Schone F, Kirchheim U, et al. Influence of conjugated linoleic acid mixture on growth,organ weights, carcass traits and meat quality in growing pigs [J]. Journal of Animal Physiology andAnimal Nutrition,2002,86:117-128.
    [34] D’Souza D N D, Pethick D W, Dunshea F R, et al. Nutritional manipulation increases IMF levels inthe Longissimus dorsi muscle of female finisher pigs [J]. Australian Journal of Agricultural Research,2003,54:745-749.
    [35] Migdal W, Pasciak P, Wojtysiak D. The effect of dietary CLA supplementation on meat and eatingquality, and the histochemical profile of the M. Longissimus dorsi from stress susceptible fattenersslaughtered at heavier weights [J]. Meat Science,2004,66:863-870.
    [36] Lauridsen C,&Henckel P. Influence of dietary conjugated linoleic acid (CLA) and age at slaughteringon performance, slaughter and meat quality, lipoproteins, and tissue deposition of CLA in barrows [J].Meat Science,2005,89:393-399.
    [37] Corino C, Musella M, Pastorelli G, et al. Influences of dietary conjugated linoleic acid (CLA) and totallisine content of growth, carcass characteristics and meat quality of heavy pigs [J]. Meat Science,2008,79:307-316.
    [38] Choi Y M, Lee S H, Choe J H, et al. Protein solubility is related to myosin isoforms, muscle fibertypes, meat quality traits, and postmortem protein changes in porcine longissimus dorsi muscle [J].Livestock Science,2010,127:183-191.
    [39] Wang Y X, Lee C H, Tiep S, et al. Peroxiasome-proliferator-activated receptor δ activate fatmetabolism to prevent obesity [J]. Cell,2003,113:139-170
    [40] Miura S, Kai You, Ono M and Ezaki O. Overexpression of peroxisome proliferator-activated receptorγ coactivatro-1down-regulates GLUT4mRNA in skeletal muscles. Journal of Biological Chemistry,2003,278:31385-31390
    [41] Narkar V A, Downes M, Yu R T, et al. AMPK and PPARδ agonists are exercise mimetics [J]. Cell,2008,134:405-415.
    [42]韩剑众,顾振宇,吴劲松,等.一水肌酸对肥育猪胴体组成和肉质的影响及机理研究[J].中国粮油学报,2007,22:101-106
    [43] O’Quinn P R, Andrews B S, Goodband R D, et al. Effects of modified tall oil and creatinemonohydrate on growth performance, carcass characteristics, and meat quality of growing-finishingpigs [J]. Journal of Animal Science,2000,78:2376-2382.
    [44] Berg E P, Maddock K R&Linville M L. Creatine monohydrate supplemented in swine finishing dietsand fresh pork quality: III. Evaluating the cumulative effect of creatine monohydrate and alpha-lipoicacid [J]. Journal of Animal Science,2003,81:2469-2474.
    [45] Ceddia R B&Sweeney G. Creatine supplementation increases glucose oxidation and AMKphosphorylation and reduces lactate production in L6rat skeletal muscle cells [J]. Journal ofPhysiology,2003.555:409-421.
    [46] James B W, Goodband R D, Unruh J A, et al. Effect of creatine monohydrate on finishing pig growthperformance, carcass characteristics and meat quality [J]. Animal Feed Science and Technology,2002,96:135-145.
    [47] Pearce K L, Katja R, Henrik J, et al. Water distribution and mobility in meat during the conversion ofmuscle to meat and ageing and the impacts on fresh meat quality attributes-A review [J]. MeatScience,2011,89:111-124

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