鹅肉ROS形成对宰后caspase介导细胞骨架蛋白降解的影响
摘要
本文试验原料是浙东白鹅，它是高蛋白质、低脂肪、低胆固醇的优质禽肉，具有很高的营养价值，作为鹅品种中主要的一大类，研究浙东白鹅肌肉成熟品质变化及其肌肉的成熟机理具有极其重要的现实意义，主要研究结果如下：
1、为了研究鹅宰杀后肌肉在自然成熟状态下肌原纤维蛋白的降解情况，快速取下胸肉约10g为0d样品,其余肉样在4℃分别成熟4h、12h、1d、2d、4d、7d后取样快速冷冻。ROS含量的测定采用定量荧光探针(DHE)分析法，细胞凋亡量的检测采用Hoechst染色法测定。研究发现，肌肉自然成熟2d荧光值显著高于对照组（P<0.05），并且在2d时出现了明显的凋亡细胞。通过SDS-PAGE法测定了骨骼肌中和肉嫩度高度相关的伴肌动蛋白(nebulin)、伴肌球蛋白(titin)以及肌钙蛋白-T(troponin-T)的降解变化，通过免疫印迹法分析肌间线蛋白(desmin)和caspase-3，9活化片段表达水平的变化，研究发现这些蛋白在成熟过程中均发生显著降解（P<0.05）。并分析不同成熟时期caspase3，9酶活力的变化，发现caspase-3酶活性在1d时最高，而caspase-9酶活性在1d时活性相对较低。
2、探讨经不同成熟时期不同部位鹅肉品质以及肌肉内Na+K+ATPase和Ca~(2+)ATPase活性的变化，并且研究酶活性与品质间的相关性。结果显示：在胸肉中，Ca~(2+)ATPase活性与pH值，蒸煮损失率以及色泽（L*、a*和b*）均具有显著相关性（P<0.05），其中仅与b*呈正相关。而Na+K+ATPase活性与滴水损失率和剪切力有显著负相关性（P<0.05）；在腿肉中，Ca~(2+)ATPase活性仅与pH值，以及色泽（L*）呈显著正相关性（P<0.05），与其他各指标相关性较低，而Na+K+ATPase活性仍与滴水损失率和剪切力有显著负相关性（P<0.05）。鹅宰后肉在4℃下成熟4d到5d时品质最佳，ATPase与肌肉品质指标密切相关。并且分析了MFI和MDA的含量变化，结果显示，胸肉中MFI含量在1d最高，而腿肉的MFI含量在整个成熟过程中变化不显著（P>0.05）。胸肉中MDA的含量整个变化不显著（P>0.05），腿肉中含量在1d时最低。
3、采用不同的诱导方式（10mmol/L的H_2O_2和NAC）处理样品，再次探究鹅肉其宰后肌肉的成熟机理。ROS含量的测定采用定量荧光探针(DCFH-DA)分析法。试验研究发现，H_2O_2处理样品1d的荧光强度值显著高于对照组（P<0.05）。通过SDS-PAGE法和免疫印迹法测定了肌钙蛋白-T(troponin-T)和肌间线蛋白(desmin)和降解变化。和对照组相比，desmin和troponin-T在处理1d时条带均发生降解（P<0.05）。两种处理组，MFI的含量均在1d时达到最高，而后随着处理时间的延长而下降。
The samples of this study was Zhejiang white goose, which is a kind of nutrition and healthfood with its high protein, low-fat and low cholesterol. As in a large class in the geese family,research about the changes of muscle quality and mature mechanism of muscles has extremelyimportant practical significance. The main results were as follows:
1. In order to investigate the mechanism underlying postmortem proeolysis of goose muscleproteins during meat aging,after goose were slaughtered,take the breast muscles about10g quicklyas the at death sample,the other muscles were stored at4℃for4h,12h,1d,4d,7d,and then quicklyfreezing. A method of quantitative fluorescence probe was used for the determination of ROS(DHE), apoptosis detection using Hoechst dye assay.The results found that fluorescence values at2d are higher than control groups(P<0.05), and Apoptotic cells were showed. The changes ofmyofibril proteins (titin, nebulin, desmin, and troponin-T) and the main activated proteins(caspase-3and caspase-9) expression levels which were highly associated with the meat tendernesswere examined by SDS-PAGE and western blotting, all of these proteins occurred apparentchange(P<0.05). The change of Enzymes activities were showed that caspase-3activity highest at1d and caspase-9activity the lowest.
2. The experiment was conducted to study the variation of the active of Na~+K~+ATPase andCa~(2+)ATPase and meat quality in different aging time and position. Relationship between enzymeand meat quality was studied. Results indicated: the active of Ca~(2+)ATPase had significantcorrelations with pH value, water boiling loss (WBL) and meat color(L*、a*and b*) in breast meat（P<0.05）, and it had negative correlations with b*.the active of Na~+K~+ATPase had significantnegative correlations with water dripping loss (WDL) and tenderness（P<0.05）; the active ofCa~(2+)ATPase only had significant positive correlations with pH value and meat color(L*) in legmeat（P<0.05）, and lower correlations with other characteris of meat quality. But Na~+K~+ATPasealso had significant negative correlations with water dripping loss(WDL) and tenderness（P<0.05）.It was concluded that The best quality of goose after slaughter was from4d to5d at4℃andit hadrelationship between ATPase and meat quality. And analyzed the variation of the content of MEIand MDA, Results indicated: the content of MFI was highest at1d in the breast muscle, and whichhad no significant variation during the aging time(P>0.05) in the leg muscle. The content of MDAwas lowest at1d in the leg muscle, and had no significant variation in the breast muscle (P>0.05)
3. Investigate the mechanism underlying postmortem after induced the samples by differentmeans (10mmol/L H_2O_2and NAC). A method of quantitative fluorescence probe was used for the determination of ROS (DCFH-DA), The results found that fluorescence values at treated samplesfor1d with H_2O_2are significant higher than control groups (P<0.05). The changes of myofibrilproteins (desmin and troponin-T) were examined by SDS-PAGE and western blotting. Comparedwith the control group, it had significant degradation of desmin and troponin-T in treated samplesat1d (P<0.05). The content of MFI was highest at1d, and grew lower and lower during the agingtime.
1、为了研究鹅宰杀后肌肉在自然成熟状态下肌原纤维蛋白的降解情况，快速取下胸肉约10g为0d样品,其余肉样在4℃分别成熟4h、12h、1d、2d、4d、7d后取样快速冷冻。ROS含量的测定采用定量荧光探针(DHE)分析法，细胞凋亡量的检测采用Hoechst染色法测定。研究发现，肌肉自然成熟2d荧光值显著高于对照组（P<0.05），并且在2d时出现了明显的凋亡细胞。通过SDS-PAGE法测定了骨骼肌中和肉嫩度高度相关的伴肌动蛋白(nebulin)、伴肌球蛋白(titin)以及肌钙蛋白-T(troponin-T)的降解变化，通过免疫印迹法分析肌间线蛋白(desmin)和caspase-3，9活化片段表达水平的变化，研究发现这些蛋白在成熟过程中均发生显著降解（P<0.05）。并分析不同成熟时期caspase3，9酶活力的变化，发现caspase-3酶活性在1d时最高，而caspase-9酶活性在1d时活性相对较低。
2、探讨经不同成熟时期不同部位鹅肉品质以及肌肉内Na+K+ATPase和Ca~(2+)ATPase活性的变化，并且研究酶活性与品质间的相关性。结果显示：在胸肉中，Ca~(2+)ATPase活性与pH值，蒸煮损失率以及色泽（L*、a*和b*）均具有显著相关性（P<0.05），其中仅与b*呈正相关。而Na+K+ATPase活性与滴水损失率和剪切力有显著负相关性（P<0.05）；在腿肉中，Ca~(2+)ATPase活性仅与pH值，以及色泽（L*）呈显著正相关性（P<0.05），与其他各指标相关性较低，而Na+K+ATPase活性仍与滴水损失率和剪切力有显著负相关性（P<0.05）。鹅宰后肉在4℃下成熟4d到5d时品质最佳，ATPase与肌肉品质指标密切相关。并且分析了MFI和MDA的含量变化，结果显示，胸肉中MFI含量在1d最高，而腿肉的MFI含量在整个成熟过程中变化不显著（P>0.05）。胸肉中MDA的含量整个变化不显著（P>0.05），腿肉中含量在1d时最低。
3、采用不同的诱导方式（10mmol/L的H_2O_2和NAC）处理样品，再次探究鹅肉其宰后肌肉的成熟机理。ROS含量的测定采用定量荧光探针(DCFH-DA)分析法。试验研究发现，H_2O_2处理样品1d的荧光强度值显著高于对照组（P<0.05）。通过SDS-PAGE法和免疫印迹法测定了肌钙蛋白-T(troponin-T)和肌间线蛋白(desmin)和降解变化。和对照组相比，desmin和troponin-T在处理1d时条带均发生降解（P<0.05）。两种处理组，MFI的含量均在1d时达到最高，而后随着处理时间的延长而下降。
The samples of this study was Zhejiang white goose, which is a kind of nutrition and healthfood with its high protein, low-fat and low cholesterol. As in a large class in the geese family,research about the changes of muscle quality and mature mechanism of muscles has extremelyimportant practical significance. The main results were as follows:
1. In order to investigate the mechanism underlying postmortem proeolysis of goose muscleproteins during meat aging,after goose were slaughtered,take the breast muscles about10g quicklyas the at death sample,the other muscles were stored at4℃for4h,12h,1d,4d,7d,and then quicklyfreezing. A method of quantitative fluorescence probe was used for the determination of ROS(DHE), apoptosis detection using Hoechst dye assay.The results found that fluorescence values at2d are higher than control groups(P<0.05), and Apoptotic cells were showed. The changes ofmyofibril proteins (titin, nebulin, desmin, and troponin-T) and the main activated proteins(caspase-3and caspase-9) expression levels which were highly associated with the meat tendernesswere examined by SDS-PAGE and western blotting, all of these proteins occurred apparentchange(P<0.05). The change of Enzymes activities were showed that caspase-3activity highest at1d and caspase-9activity the lowest.
2. The experiment was conducted to study the variation of the active of Na~+K~+ATPase andCa~(2+)ATPase and meat quality in different aging time and position. Relationship between enzymeand meat quality was studied. Results indicated: the active of Ca~(2+)ATPase had significantcorrelations with pH value, water boiling loss (WBL) and meat color(L*、a*and b*) in breast meat（P<0.05）, and it had negative correlations with b*.the active of Na~+K~+ATPase had significantnegative correlations with water dripping loss (WDL) and tenderness（P<0.05）; the active ofCa~(2+)ATPase only had significant positive correlations with pH value and meat color(L*) in legmeat（P<0.05）, and lower correlations with other characteris of meat quality. But Na~+K~+ATPasealso had significant negative correlations with water dripping loss(WDL) and tenderness（P<0.05）.It was concluded that The best quality of goose after slaughter was from4d to5d at4℃andit hadrelationship between ATPase and meat quality. And analyzed the variation of the content of MEIand MDA, Results indicated: the content of MFI was highest at1d in the breast muscle, and whichhad no significant variation during the aging time(P>0.05) in the leg muscle. The content of MDAwas lowest at1d in the leg muscle, and had no significant variation in the breast muscle (P>0.05)
3. Investigate the mechanism underlying postmortem after induced the samples by differentmeans (10mmol/L H_2O_2and NAC). A method of quantitative fluorescence probe was used for the determination of ROS (DCFH-DA), The results found that fluorescence values at treated samplesfor1d with H_2O_2are significant higher than control groups (P<0.05). The changes of myofibrilproteins (desmin and troponin-T) were examined by SDS-PAGE and western blotting. Comparedwith the control group, it had significant degradation of desmin and troponin-T in treated samplesat1d (P<0.05). The content of MFI was highest at1d, and grew lower and lower during the agingtime.
引文
[1]张响英,唐现文.我国种鹅的育种现状及展望[J].安徽农业科学,2009,37(22):10511-10513.
[2]倪东衍.我国养鹅业前景广阔[J].农民科技培训,2008,(10):40-40.
[3]丁美中.我国鹅业发展状况及消费市场发展趋势[J].水禽世界,2008,(1):7-8.
[4]闵育娜,高玉鹏,侯水生,等.我国养鹅业现状及前景展望[J].中国畜牧杂志,2005,41(5):57-59.
[5]吴军,赵志军.我国养鹅业存在的问题及对策[J].当代畜牧,2010,(1):1-3.
[6]何大乾,侯水生.我国鹅业育种现状与未来发展方向[J].中国禽业导刊,2009,26(9):10-12.
[7]建龙.鹅肉[J].中老年:健身科学,2009,(7):46-47.
[8]尹兆正.养鹅手册[M].北京:中国农业大学出版社,2005.
[9]杨勇,王存堂,任健.鹅肉嫩度的评定方法[J].黑龙江畜牧兽医,2010,(6):32-33.
[10]谢广富.鹅肉营养成分分析及营养价值评定[J].肉品卫生,1999,(4):2-3.
[11]冯小鹿.鹅全身是宝养殖效益高[J].农业知识,2009,(16):4-5.
[12]韩陆奇.鹅肉生产大有可为[J].肉类研究,1995,(4):7-7.
[13]鹅肉及其副产物的深加工[J].技术与市场,2001,(05):17-18.
[14]李良玉,曹荣安,何香伟,等.香辣鹅肉干加工工艺的研究[J].肉类究,2008,(11):35-39.
[15]徐明生.鹅肉肉质分析[J].中国禽产与食品,1997,(05):87-88.
[16]曹宏,蒋云升,包建忠,等.鹅肉食用前景和消费市场初探[J].安徽农业科学,2005,33(12):2480-2480.
[17]唐修君,陈宽维,高玉时,等.影响鹅肉品质的主要因素[J].水禽世界,2008,(4):38-40.
[18]胡献国.益气补虚说鹅肉[J].东方食疗与保健,2004,(1):26-26.
[19]杨勇,任健,王存堂,王文侠,等.鹅肉酶嫩化技术的研究.食品研究与开发，2010,31(10),25-29.
[20]高海燕，潘润淑，马汉军.超高压技术对鹅肉嫩度的影响.食品科学，2011,32(8),107-110.
[21] Armstrong J S, and Whiteman M. Measurement of reactive oxygen species in cell andmitochondria[M]. Methods Cell Biol,2007,80:355-377.
[22] Gomes A, Fernandes E, and Lima J L. Fluorescence probes used for detection of reactiveoxygen species[J]. J. Biochem. Biophys. Methods,2005,65(2-3):45-80.
[23] Bass D A, Parce J W, Dechatelet L R, et al. Flow cytometric studies of oxidative productformation by neutrophils: a graded response to membrane stimulation. The Journal ofImmunology,1983,130:1910–1917.
[24] Wardman P. Fluorescent and luminescent probes for measurement of oxidative and nitrosativespecies in cells and tissues：Progress，pitfalls，and prospects[J]. Free Radic. Biol. Med,2007,43(7):995－1022.
[25]卫惠杰,张徽,刘莹,唐熹.抗坏血酸与乳腺癌MDA-MB-231细胞增殖和凋亡的相关性[J].中国生物制品学杂志,2011,24(1):48-51.
[26] Heath-Engel H M, and Shore G C. Mitochondrial membrane dynamics, cristae remodellingand apoptosis [J]. Biochim Biophys Acta,2006,1763(5-6):549-560.
[27] Adams J M. Ways of dying: Multiple pathways to apoptosis. Genes and Development,2003,17:2481-2495.
[28] Kerr J F, Wyllie A H, and Currie A R. Apoptosis: a basic biological phenomenon withwide-ranging implications in tissue kinetics [J]. British Journal of Cancer,1972,26:239-257.
[29] Fuentes-Prior P, and Salvesen G S. The protein structures that shape caspase-activity,specificity, activation, and inhibition [J]. Biochemical Journal,2004,384:201-232.
[30]李小明,孙志贤.细胞凋亡中的关键蛋白酶-Caspase-3[J].国外医学分子生物学分册,1999,21(1):6-9.
[31] Kim H E, Du F, Fang M, and Wang X. Formation of apoptosome is initiated by cytochromec-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1[J]. Proceedings ofthe National Academy of Sciences of the United States of America,2005,102:17545-17550.
[32] Dayton W R，and Sehollmeyer J V. Isolation from porcine eardiac muscle of a Ca2+-activatedprotease that partially degades myofibrils [J].Joumal of Moleeular And Cellular Cardiology,1980,12(6):533-551.
[33] Huang M, Huang F, Xue M, et al. The effect of active caspase-3on degradation of chickenmyofibrillar proteins and structure of myofibrils[J]. Food Chemistry,2011,128:22–27.
[34] Boyer-Berri C, and Greaser M L. Effect of postmortem storage on the Z-Iine region of titinin bovine muscle[J]. J.Animal Science,1998,76:1034-1044.
[35] Prates J M. Contribution of major structural changes in myofibrils to rabbit meat tenderizationduring aging[J].Meat science,2002,61:103-113.
[36] McElhinny A S, Kazmierski S T, Labeit S, et al. Nebulin: the nebulous, multifunctional giantof striated muscle[J]. Trends in Cardiovascular Medicine,2003,13:195–201.
[37] Negishi H，Yamamoto E, and Kuwata T. The origin of the30kDa component appearingduring Post-mortem ageing of bovine musele [J]. Meat Scienee,1996,42(3):289-303.
[38] Samejima K，and Wolfe F H. Degradation of myofibrillar Protein components duringPost-mortem aging of chicken musele[J]. Joumal of Food Seienee,1976,41(2):250-254.
[39] Koohmaraie M, WhiPPle G, Kretchmar D H, et al. Postmortem Proteolysis in Longissimusmuscle from beef, lamb and pork carcasses[J]. Joumal of Animal Seienee,1991,69:617-624.
[40] WhiPPle G，and Koohmaraie M. Effects of lamb age，muscle type，and24-hour activity ofendogenous proteinases on postmortem proteolysis[J].Journal of Animal Scienee,1992,70:798-804.
[41] Huff-Lonergan E，Mitsuhashi T，BeelQnan D D，et al. Proteolysis of Specific musclestruetural Proteins by u-calpain at low PH and temperature is similar to degradation inPostmortem bovine Musele [J]. Journal of Animal Seience,1996,74(5):993-1008.
[42] Hughes M C，Geary S，Dransfield E，et al.Charaeterization of peptides released from rabbitskeletal muscle troponin-T by u-calpain under conditions of low temperature and high ionicstrength[J]. Meat Seienee,2001,59(1):61-69.
[43] Tsitsilonis O E，Stoeva S，Eehner H，et al. A skeletal muscle troponin-T specific ELISA basedon the use of anantibody against the soluble troponin-T(16-31) fragment [J]. Joumal ofImmunological Methods,2002,268(2):141-145.
[44] Miros L F. Properties of refrigerated ground beef treated with potassium lactate and sodiumdiaeetate [J]. Joumal of The Science Of Food And Agriculture,2008,88(l):91-99.
[45] Kanduc D, Mittelman A, Serpico R, et al. Cell death:apoptosis versus necrosis[J].International Journal of Molecular Medicine,2002,21:165-170.
[46] Eguchi Y, Shimizu S, and Tsujimoto Y. Intracellular ATP Levels Determine Cell Death Fate byApoptosis or Necrosis[J], Cancer Research,1997,57:1835-1840.
[47] Liu X, Kim C N, Yang J, et al. Induction of Apoptotic Program in Cell-Free Extracts:Requirement for dATP and Cytochrome c[J].cell,1996,86:147-157.
[48] Saraster A, and Pulkki K. Morphologic and biochemical hallmarks of apoptosis[J].CardiovascResearch,2000,45:528-537.
[49]吴军,赵志军.我国养鹅业存在的问题及对策[J].当代畜牧,2010,(1):1-3.
[50]翟洪民.介绍八个中型鹅品种[J].当代畜禽养殖业,2008,(3):59-60.
[51] Ji J R, and Takahashi K. Changes in concentration of sarcoplasm ic free calcium duringpost-mortem aging of meat[J]. Meat Science,2006,73:395–403.
[52] Herrera-mendez C H, Becila S, and Boudjellal A. Ouali, A. Meataging: reconsideration of thecurrent concept [J]. Trendsin Food Science and Technology,2006,17:394-405.
[53] Geesink G H, Kuchay S, Chishti A H, et al. μ-Calpain is essential for postmortem proteolysisof muscle proteins[J]. Animal Science,2006,84:834-2840.
[54]张英君,陈有亮.钙激活蛋白酶在肉成熟中的作用机理[J].肉类工业，2000,(8):31-36.
[55]袁长青,丁振华.Caspase的结构与功能[J].国外医学生物学手册，2002,24(3):146-151.
[56]王筱冰,张小翠,夏妙红,等.Caspase的活化机制[J].现代生物医学进展，2006,6(3):53-55.
[57] Menazza S, Blaauw B, Tiepolo T, et al. Oxidative stress by monoamine oxidasesis causallyinvolved in myofiber damage in muscular dystrophy[J]. Human Molecular Genetics,2010,19:4207–4215.
[58] Benov L, Sztejnberg L, and dovich I. Critical evaluation of the use of hydroethidine as ameasure of superoxide anion radical[J]. Free Radical Biology&Medicine,1998,25:826–831.
[59]黄明,赵莲,徐幸莲,等.鸡肉在成熟过程中肌原纤维蛋白的降解机制研究[J].2007,23(11):42-45.
[60] Paunas T I.(2011). Effects of exogenous hydrogen sulfide administration on cardiac functionand reactive oxygen species production: a study in hearts from normal rats and rats with hearthypertrophy or ischemia (pp.1–74). Norway: University of Troms.
[61] Wedgwoo S, Dettman R W, and Black S M. ET-1stimulates pulmonary arterial smoothmuscle cell proliferation via induction of reactive oxygen species [J]. American Journal ofPhysiology-Lung Cellular and Molecular Physiology,2001,281:1058–1067.
[62] Mandal D, Moitra P K, Saha H, et al. Caspase-3regulates phosphatidylserine externalizationand phagocytosis of oxidatively stressed erythrocytes [J]. FEBS Letters,2002,513:184–188.
[63] Cao J X, Sun W. Q, Zhou G H, et al. Morphological and biochemical assessment of apoptosisin different skeletal muscles of bulls during conditioning[J]. Journal of animal science,2010,88:3439–3444.
[64] Ferreira K S, Kreutz C, Macnelly S, et al. Caspase-3feeds back on caspase-8, Bid and XIAPin type I Fas signaling in primary mouse hepatocytes[J]. Apoptosis,2012,17:503–515.
[65] Arnold A A, Aboukameel A, Chen J, Yang D, et al. Preclinical studies of Apogossypolone: anew nonpeptidic pan small-molecule inhibitor of Bcl-2, Bcl-XL and Mcl-1proteins inFollicular Small Cleaved Cell Lymphoma model[J]. Molecular Cancer,2008,17:7–20.
[66] Petit A, Zukor D, Antoniou J, et al. Expression of caspase-8and caspase-3proteins in interfacemembranes from aseptically loose total hip arthroplasty[J]. Journal of materials science,2002,13:1001–1005.
[67] The effect of active caspase-3on degradation of chicken myofibrillar proteins and structure ofmyofibrils [J].Food Chemistry,2011,128:22-27.
[68] Wang K, McClure J, and Tu A. Titin: Major myofibrillar components of striated muscle[J].Proceedings of the National Academy of Sciences of USA,1979,76:3698–3702.
[69] Huff-Lonergan E, Parrish F C, and Robson R M. Effects of postmortem aging time, animalage, and sex on degradation of titin and nebulin in bovine longissimus muscle [J]. Journal ofAnimal Science,1995,73:1064–1073.
[70] Harris S E, Huff-Lonergan E, Lonergan S M, Jones W R, et al. Antioxidant status affects colorstability and tenderness of calcium chlorideinjected beef[J]. Journal of Animal Science,2001,79:666–677.
[71] Melody J L, LonerganS. M, RoweL J, et al. Early postmortem biochemical factors influencetenderness and water-holding capacity of three porcine muscles [J]. Animal Science,2004,82:1195-1205.
[72]袁斌,马樱,闫铭,叶正旭.罗卓荆大鼠骨髓基质干细胞的改良培养方法及Hoechst体外标记研究[J].细胞与分子免疫学杂志,2011,27(1):61-63.
[73]卢晓晔,钟雪云.Caspases与细胞凋亡(综述).暨南大学学报（医学版），2000,21(6):121-124.
[74]黄明,罗欣.内源蛋白酶在肉嫩化中的作用[J].肉类研究,1999,11-14.
[75] Taylor R G, Geesink G H, ThomPson V F, et al. ISZ-disk degradation responsible forPostmortem tenderization [J]. Animal Science.1995.73:1351-1367.
[76] Huff-Lonergan E, Tomiko M, DirkD B, et al. proteolysis of specific museke struetural proteinsby μ-calpain at Iow pH and temperature is similar to degradation in postmortemmuscle[J].Animal.Science.1996,74:993-1008.
[77] Geensink G H，Mareko M H, Morton J D,et al. Effects of stress and high voltage electricalstimuiation on tenderness of lambM.longissimus [J]. Meat Science,2000,57:265-271.
[78] Lonergan S M, and Huff-Lonergan E. Postrnortem Proteolysis and tenderization of toploinsteaks from branguscattle [J]. Muscle Foods,2001,12:121-136.
[79]陈琳.caspase-3在鸡肉成熟过程中的作用以及与calpain的交互关系研究[D].南京:南京农业大学,2011:71-98.
[80] Quali A,Herrera-Mendez C H,Coulis G, et al.Revisiting the conversion of muscle into meatand the underlying mechanisms[J].Meat Science,2006,74(1):44-58.
[81] Herrera-Mendez C H,Becila S,Boudjellal A,et al. Meat aging:Reconsideration of the currentconcept[J].Trends In Food Science and Technology,2006,17(8):394-405.
[82] Wolvetang E J, Krauer K. Mitochondrial respiratory chain inhibitors induce apoptosis [J].FebsLetter,1994,339(1-2):40-44.
[83] Marton A,Mihalik R,Bratincsak A,et al. Apoptotic Cell Death Induced by Inhibitors of EnergyConservation[J].European Journal of Biochemistry,1997,250(2):467-475.
[84] Terminella C,Tollefson K,Kroczynski J, et al. Inhibition of apoptosis in pulmonary endothelialcells by altered pH,mitochondrial function, and ATP supply[J].American Journal ofPhysiology Lung Cellular and Molecular Physiology,2002,283(6): L1291-L1302.
[85] Mobasheri A, Avila J, Cozar-Castellano I, et al. Na+,K+ATPase Isozyme Diversity;Comparative Biochemistry and Physiological Implications of Novel Functional Interactions[J].Bioscience Reports,2000,20(2):51-91.
[86] Rajasekaran S A, Barwe S P, and Rajasekaran A K.Multiple Functions of Na,K-ATPase inEpithelial Cells[J].Seminars In Nephrology,2005,25(5):328-334.
[87] Jaisser F,Horisberger J-D, and Rossier B C.The β Subunit Modulates Potassium Activation ofthe Na-K Pumpa [J].Annals of The New York Academy Of Science,1992,671(1):113-119.
[88] Yu S P. Na+,K+ATPase:the new face of an old player in pathogenesis and apoptotic/hybridcell death[J].Biochemical Pharmacology,2003,66(8):1602-1609.
[89] Qin H, Srinivasula S M,Wu G, et al. Structural basis of procaspase-9recruitment by theapoptotic protease-actvating factor1[J]. Nature,1999,399(6736):549-557.
[90]史培磊，闵辉辉，李春保,等.滚揉腌制前后鹅肉品质的变化[J].食品科学,2011,32(11):88-92.
[91]戴四发,闻爱友,王立克,等.肉仔鸡肌肉色泽与品质相关性研究[J].中国农业大学学报,2007,12(1):61-64.
[92] Seemann M. Factor which influence pigmentation [J].Lohmann Information,2000,24:20-24.
[93] Toyomizu M, Sato K, Taroda H, et al. Effects of dietary Spirulina on meat colour in muscleof broiler chickens [J]. British Poultry Science,2001,42:197-202.
[94] Wulf D M, and Wise J W. Measuring muscle color on beef carcasses using the L*a*b*colorspace [J]. Journal of Animal Science,1999,77:2418-2427.
[95] Culler R D, Parrish F C, Smith G C, et al. Relationship of myofibril fragmentation index tocertain chemical、physical and sensory characteristics of bovine longissimus muscle [J].Journal of Food Science,1978,43:1177-1180.
[96]吴菊清,李春保,周光宏,等.宰后成熟过程中冷却牛肉、猪肉色泽和嫩度的变化[J].食品科学,2008,29(10):136-139.
[97] Zhou Y. The protection of selenium on ROS mediated-apoptosis by mitochondria dysfunctionin cadmium-induced LLC-PK1cells[J]. Toxicology in Vitro,2009,(23):288–294
[98]杨月春,王士勇,李钟淑,等.延边黄牛核移植胚胎的活性氧含量的测定[J].西南农业学报,2010,23(1):210-213.
[99]施广璞，杜洪震，刘子文,等. H2O2致WB-F344细胞内活性氧的产生及机理[J].生物物理学报,2002,18(4):462-465.
[100]袁长青,丁振华.Caspase的结构与功能[J].国外医学生物学手册，2002,24(3):146-151.
[101]王筱冰,张小翠,夏妙红,等.Caspase的活化机制[J].现代生物医学进展，2006,6(3):53-55.
[102] Huang M, and Huang F. The effect of active caspase-3on degradation of chickenmyofibrillar proteins and structure of myofibrils[J]. Food Chemistry,2011,(128):22–27.
[103]马书燕,李吉跃,彭祚登.人工老化过程中柔枝松种子丙二醛(MDA)含量变化研究[J].2011,7:11-15.
[104] Jaisser F,Horisberger J-D, and Rossier B C.The β Subunit Modulates Potassium Activationof the Na-K Pumpa [J].Annals of The New York Academy Of Science,1992,671(1):113-119.
[105] Yu B P. Cellular defenses against damage from reactive oxygenspecies[J]. Physiological. Reviews,1994,74:139–161.
[106] Hail N, Kim H J, and Lotan R. Mechanisms of fenretinide-induced apoptosis[J].Apoptosis,2006,11:1677-1694.
[107] Groeger G, Quiney C, and Cotter T G. Hydrogen peroxide as a cell-survival signalingmolecule[J]. Antioxid. Redox Signal,2009,11:2655-2671.
[108] Qanungo S, Wang M, and Nieminen A. L. N-Acetyl-L-cysteine enhances apoptosisthrough inhibition of nuclear factor-kappaB in hypoxic murine embryonic fibroblasts[J].National Institutes of Health,2004,279:50455-50464.
[109] Kemp C M, Parr T, Bardsley R G, et al. Comparison of the relative expression ofcaspase isoforms in different porcine skeletal muscles[J]. Meat Science,2006,73:426-431.
[110] Zhai W, Feng R, Huo L, Li J, et al. Mechanism of the protective effects ofN-acetylcysteine on the heart of brain-dead Ba-Ma miniature pigs[J]. TheJournal ofHeart and Lung Transplantation,2009,28:944–949.
[111] Du J, Wang X N, and Miereles C. Activation of caspase-3is an initial step triggeringaccelerated muscle proteolysis in catabolic conditions[J]. The Journal of ClinicalInvestigation,2004,113(1):115-123.
[112] Etlinger J D, Zak R, and Fischman D A. Compositional studies of myofibrils fromrabbit striated muscle[J]. Journal of Cell Biology,1976,68(1):123–141.
[113] Huang M, and Huang F. The effect of active caspase-3on degradation of chickenmyofibrillar proteins and structure of myofibrils [J]. Food Chemistry,2011,128(1):22-27.
[114] Huang X, Li Q, Li H, and Guo L. Neuroprotective and Antioxidative Effect of CactusPolysaccharides In Vivo and In Vitro [J]. Cellular and Molecular Neurobiology,2009,29:1211-1221.
[115] Silveira L R, Pereira-Da-Silva L, Juel C, et al. Formation of hydroric peroxide and nitricoxide in rat skeletal muscle cells during contractions[J]. Free Radical Biology&Medicine,2003,35:455-464.
[116] Taylor R G, Geesink G H, Thompson V F, et al. Is Z-disk degradation responsible forpostmortem tenderization [J]? Journal of Animal Science,1995,73(5),1351-1367.
[117] Chatot C L, Ziomek C A, Bvaister B D, et al. Toerrs.An improved culture mediumSupports development of rardom-bred l-cell mouse embryos in vitro[J]. RePord. Fert.1989,86:679-688.
[118] Yi J Z. The protection of selenium on ROS mediated-apoptosis by mitochondriadysfunction in cadmium-induced LLC-PK1cells [J]. Toxicology in Vitro,2009,(23):288-294.
[2]倪东衍.我国养鹅业前景广阔[J].农民科技培训,2008,(10):40-40.
[3]丁美中.我国鹅业发展状况及消费市场发展趋势[J].水禽世界,2008,(1):7-8.
[4]闵育娜,高玉鹏,侯水生,等.我国养鹅业现状及前景展望[J].中国畜牧杂志,2005,41(5):57-59.
[5]吴军,赵志军.我国养鹅业存在的问题及对策[J].当代畜牧,2010,(1):1-3.
[6]何大乾,侯水生.我国鹅业育种现状与未来发展方向[J].中国禽业导刊,2009,26(9):10-12.
[7]建龙.鹅肉[J].中老年:健身科学,2009,(7):46-47.
[8]尹兆正.养鹅手册[M].北京:中国农业大学出版社,2005.
[9]杨勇,王存堂,任健.鹅肉嫩度的评定方法[J].黑龙江畜牧兽医,2010,(6):32-33.
[10]谢广富.鹅肉营养成分分析及营养价值评定[J].肉品卫生,1999,(4):2-3.
[11]冯小鹿.鹅全身是宝养殖效益高[J].农业知识,2009,(16):4-5.
[12]韩陆奇.鹅肉生产大有可为[J].肉类研究,1995,(4):7-7.
[13]鹅肉及其副产物的深加工[J].技术与市场,2001,(05):17-18.
[14]李良玉,曹荣安,何香伟,等.香辣鹅肉干加工工艺的研究[J].肉类究,2008,(11):35-39.
[15]徐明生.鹅肉肉质分析[J].中国禽产与食品,1997,(05):87-88.
[16]曹宏,蒋云升,包建忠,等.鹅肉食用前景和消费市场初探[J].安徽农业科学,2005,33(12):2480-2480.
[17]唐修君,陈宽维,高玉时,等.影响鹅肉品质的主要因素[J].水禽世界,2008,(4):38-40.
[18]胡献国.益气补虚说鹅肉[J].东方食疗与保健,2004,(1):26-26.
[19]杨勇,任健,王存堂,王文侠,等.鹅肉酶嫩化技术的研究.食品研究与开发，2010,31(10),25-29.
[20]高海燕，潘润淑，马汉军.超高压技术对鹅肉嫩度的影响.食品科学，2011,32(8),107-110.
[21] Armstrong J S, and Whiteman M. Measurement of reactive oxygen species in cell andmitochondria[M]. Methods Cell Biol,2007,80:355-377.
[22] Gomes A, Fernandes E, and Lima J L. Fluorescence probes used for detection of reactiveoxygen species[J]. J. Biochem. Biophys. Methods,2005,65(2-3):45-80.
[23] Bass D A, Parce J W, Dechatelet L R, et al. Flow cytometric studies of oxidative productformation by neutrophils: a graded response to membrane stimulation. The Journal ofImmunology,1983,130:1910–1917.
[24] Wardman P. Fluorescent and luminescent probes for measurement of oxidative and nitrosativespecies in cells and tissues：Progress，pitfalls，and prospects[J]. Free Radic. Biol. Med,2007,43(7):995－1022.
[25]卫惠杰,张徽,刘莹,唐熹.抗坏血酸与乳腺癌MDA-MB-231细胞增殖和凋亡的相关性[J].中国生物制品学杂志,2011,24(1):48-51.
[26] Heath-Engel H M, and Shore G C. Mitochondrial membrane dynamics, cristae remodellingand apoptosis [J]. Biochim Biophys Acta,2006,1763(5-6):549-560.
[27] Adams J M. Ways of dying: Multiple pathways to apoptosis. Genes and Development,2003,17:2481-2495.
[28] Kerr J F, Wyllie A H, and Currie A R. Apoptosis: a basic biological phenomenon withwide-ranging implications in tissue kinetics [J]. British Journal of Cancer,1972,26:239-257.
[29] Fuentes-Prior P, and Salvesen G S. The protein structures that shape caspase-activity,specificity, activation, and inhibition [J]. Biochemical Journal,2004,384:201-232.
[30]李小明,孙志贤.细胞凋亡中的关键蛋白酶-Caspase-3[J].国外医学分子生物学分册,1999,21(1):6-9.
[31] Kim H E, Du F, Fang M, and Wang X. Formation of apoptosome is initiated by cytochromec-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1[J]. Proceedings ofthe National Academy of Sciences of the United States of America,2005,102:17545-17550.
[32] Dayton W R，and Sehollmeyer J V. Isolation from porcine eardiac muscle of a Ca2+-activatedprotease that partially degades myofibrils [J].Joumal of Moleeular And Cellular Cardiology,1980,12(6):533-551.
[33] Huang M, Huang F, Xue M, et al. The effect of active caspase-3on degradation of chickenmyofibrillar proteins and structure of myofibrils[J]. Food Chemistry,2011,128:22–27.
[34] Boyer-Berri C, and Greaser M L. Effect of postmortem storage on the Z-Iine region of titinin bovine muscle[J]. J.Animal Science,1998,76:1034-1044.
[35] Prates J M. Contribution of major structural changes in myofibrils to rabbit meat tenderizationduring aging[J].Meat science,2002,61:103-113.
[36] McElhinny A S, Kazmierski S T, Labeit S, et al. Nebulin: the nebulous, multifunctional giantof striated muscle[J]. Trends in Cardiovascular Medicine,2003,13:195–201.
[37] Negishi H，Yamamoto E, and Kuwata T. The origin of the30kDa component appearingduring Post-mortem ageing of bovine musele [J]. Meat Scienee,1996,42(3):289-303.
[38] Samejima K，and Wolfe F H. Degradation of myofibrillar Protein components duringPost-mortem aging of chicken musele[J]. Joumal of Food Seienee,1976,41(2):250-254.
[39] Koohmaraie M, WhiPPle G, Kretchmar D H, et al. Postmortem Proteolysis in Longissimusmuscle from beef, lamb and pork carcasses[J]. Joumal of Animal Seienee,1991,69:617-624.
[40] WhiPPle G，and Koohmaraie M. Effects of lamb age，muscle type，and24-hour activity ofendogenous proteinases on postmortem proteolysis[J].Journal of Animal Scienee,1992,70:798-804.
[41] Huff-Lonergan E，Mitsuhashi T，BeelQnan D D，et al. Proteolysis of Specific musclestruetural Proteins by u-calpain at low PH and temperature is similar to degradation inPostmortem bovine Musele [J]. Journal of Animal Seience,1996,74(5):993-1008.
[42] Hughes M C，Geary S，Dransfield E，et al.Charaeterization of peptides released from rabbitskeletal muscle troponin-T by u-calpain under conditions of low temperature and high ionicstrength[J]. Meat Seienee,2001,59(1):61-69.
[43] Tsitsilonis O E，Stoeva S，Eehner H，et al. A skeletal muscle troponin-T specific ELISA basedon the use of anantibody against the soluble troponin-T(16-31) fragment [J]. Joumal ofImmunological Methods,2002,268(2):141-145.
[44] Miros L F. Properties of refrigerated ground beef treated with potassium lactate and sodiumdiaeetate [J]. Joumal of The Science Of Food And Agriculture,2008,88(l):91-99.
[45] Kanduc D, Mittelman A, Serpico R, et al. Cell death:apoptosis versus necrosis[J].International Journal of Molecular Medicine,2002,21:165-170.
[46] Eguchi Y, Shimizu S, and Tsujimoto Y. Intracellular ATP Levels Determine Cell Death Fate byApoptosis or Necrosis[J], Cancer Research,1997,57:1835-1840.
[47] Liu X, Kim C N, Yang J, et al. Induction of Apoptotic Program in Cell-Free Extracts:Requirement for dATP and Cytochrome c[J].cell,1996,86:147-157.
[48] Saraster A, and Pulkki K. Morphologic and biochemical hallmarks of apoptosis[J].CardiovascResearch,2000,45:528-537.
[49]吴军,赵志军.我国养鹅业存在的问题及对策[J].当代畜牧,2010,(1):1-3.
[50]翟洪民.介绍八个中型鹅品种[J].当代畜禽养殖业,2008,(3):59-60.
[51] Ji J R, and Takahashi K. Changes in concentration of sarcoplasm ic free calcium duringpost-mortem aging of meat[J]. Meat Science,2006,73:395–403.
[52] Herrera-mendez C H, Becila S, and Boudjellal A. Ouali, A. Meataging: reconsideration of thecurrent concept [J]. Trendsin Food Science and Technology,2006,17:394-405.
[53] Geesink G H, Kuchay S, Chishti A H, et al. μ-Calpain is essential for postmortem proteolysisof muscle proteins[J]. Animal Science,2006,84:834-2840.
[54]张英君,陈有亮.钙激活蛋白酶在肉成熟中的作用机理[J].肉类工业，2000,(8):31-36.
[55]袁长青,丁振华.Caspase的结构与功能[J].国外医学生物学手册，2002,24(3):146-151.
[56]王筱冰,张小翠,夏妙红,等.Caspase的活化机制[J].现代生物医学进展，2006,6(3):53-55.
[57] Menazza S, Blaauw B, Tiepolo T, et al. Oxidative stress by monoamine oxidasesis causallyinvolved in myofiber damage in muscular dystrophy[J]. Human Molecular Genetics,2010,19:4207–4215.
[58] Benov L, Sztejnberg L, and dovich I. Critical evaluation of the use of hydroethidine as ameasure of superoxide anion radical[J]. Free Radical Biology&Medicine,1998,25:826–831.
[59]黄明,赵莲,徐幸莲,等.鸡肉在成熟过程中肌原纤维蛋白的降解机制研究[J].2007,23(11):42-45.
[60] Paunas T I.(2011). Effects of exogenous hydrogen sulfide administration on cardiac functionand reactive oxygen species production: a study in hearts from normal rats and rats with hearthypertrophy or ischemia (pp.1–74). Norway: University of Troms.
[61] Wedgwoo S, Dettman R W, and Black S M. ET-1stimulates pulmonary arterial smoothmuscle cell proliferation via induction of reactive oxygen species [J]. American Journal ofPhysiology-Lung Cellular and Molecular Physiology,2001,281:1058–1067.
[62] Mandal D, Moitra P K, Saha H, et al. Caspase-3regulates phosphatidylserine externalizationand phagocytosis of oxidatively stressed erythrocytes [J]. FEBS Letters,2002,513:184–188.
[63] Cao J X, Sun W. Q, Zhou G H, et al. Morphological and biochemical assessment of apoptosisin different skeletal muscles of bulls during conditioning[J]. Journal of animal science,2010,88:3439–3444.
[64] Ferreira K S, Kreutz C, Macnelly S, et al. Caspase-3feeds back on caspase-8, Bid and XIAPin type I Fas signaling in primary mouse hepatocytes[J]. Apoptosis,2012,17:503–515.
[65] Arnold A A, Aboukameel A, Chen J, Yang D, et al. Preclinical studies of Apogossypolone: anew nonpeptidic pan small-molecule inhibitor of Bcl-2, Bcl-XL and Mcl-1proteins inFollicular Small Cleaved Cell Lymphoma model[J]. Molecular Cancer,2008,17:7–20.
[66] Petit A, Zukor D, Antoniou J, et al. Expression of caspase-8and caspase-3proteins in interfacemembranes from aseptically loose total hip arthroplasty[J]. Journal of materials science,2002,13:1001–1005.
[67] The effect of active caspase-3on degradation of chicken myofibrillar proteins and structure ofmyofibrils [J].Food Chemistry,2011,128:22-27.
[68] Wang K, McClure J, and Tu A. Titin: Major myofibrillar components of striated muscle[J].Proceedings of the National Academy of Sciences of USA,1979,76:3698–3702.
[69] Huff-Lonergan E, Parrish F C, and Robson R M. Effects of postmortem aging time, animalage, and sex on degradation of titin and nebulin in bovine longissimus muscle [J]. Journal ofAnimal Science,1995,73:1064–1073.
[70] Harris S E, Huff-Lonergan E, Lonergan S M, Jones W R, et al. Antioxidant status affects colorstability and tenderness of calcium chlorideinjected beef[J]. Journal of Animal Science,2001,79:666–677.
[71] Melody J L, LonerganS. M, RoweL J, et al. Early postmortem biochemical factors influencetenderness and water-holding capacity of three porcine muscles [J]. Animal Science,2004,82:1195-1205.
[72]袁斌,马樱,闫铭,叶正旭.罗卓荆大鼠骨髓基质干细胞的改良培养方法及Hoechst体外标记研究[J].细胞与分子免疫学杂志,2011,27(1):61-63.
[73]卢晓晔,钟雪云.Caspases与细胞凋亡(综述).暨南大学学报（医学版），2000,21(6):121-124.
[74]黄明,罗欣.内源蛋白酶在肉嫩化中的作用[J].肉类研究,1999,11-14.
[75] Taylor R G, Geesink G H, ThomPson V F, et al. ISZ-disk degradation responsible forPostmortem tenderization [J]. Animal Science.1995.73:1351-1367.
[76] Huff-Lonergan E, Tomiko M, DirkD B, et al. proteolysis of specific museke struetural proteinsby μ-calpain at Iow pH and temperature is similar to degradation in postmortemmuscle[J].Animal.Science.1996,74:993-1008.
[77] Geensink G H，Mareko M H, Morton J D,et al. Effects of stress and high voltage electricalstimuiation on tenderness of lambM.longissimus [J]. Meat Science,2000,57:265-271.
[78] Lonergan S M, and Huff-Lonergan E. Postrnortem Proteolysis and tenderization of toploinsteaks from branguscattle [J]. Muscle Foods,2001,12:121-136.
[79]陈琳.caspase-3在鸡肉成熟过程中的作用以及与calpain的交互关系研究[D].南京:南京农业大学,2011:71-98.
[80] Quali A,Herrera-Mendez C H,Coulis G, et al.Revisiting the conversion of muscle into meatand the underlying mechanisms[J].Meat Science,2006,74(1):44-58.
[81] Herrera-Mendez C H,Becila S,Boudjellal A,et al. Meat aging:Reconsideration of the currentconcept[J].Trends In Food Science and Technology,2006,17(8):394-405.
[82] Wolvetang E J, Krauer K. Mitochondrial respiratory chain inhibitors induce apoptosis [J].FebsLetter,1994,339(1-2):40-44.
[83] Marton A,Mihalik R,Bratincsak A,et al. Apoptotic Cell Death Induced by Inhibitors of EnergyConservation[J].European Journal of Biochemistry,1997,250(2):467-475.
[84] Terminella C,Tollefson K,Kroczynski J, et al. Inhibition of apoptosis in pulmonary endothelialcells by altered pH,mitochondrial function, and ATP supply[J].American Journal ofPhysiology Lung Cellular and Molecular Physiology,2002,283(6): L1291-L1302.
[85] Mobasheri A, Avila J, Cozar-Castellano I, et al. Na+,K+ATPase Isozyme Diversity;Comparative Biochemistry and Physiological Implications of Novel Functional Interactions[J].Bioscience Reports,2000,20(2):51-91.
[86] Rajasekaran S A, Barwe S P, and Rajasekaran A K.Multiple Functions of Na,K-ATPase inEpithelial Cells[J].Seminars In Nephrology,2005,25(5):328-334.
[87] Jaisser F,Horisberger J-D, and Rossier B C.The β Subunit Modulates Potassium Activation ofthe Na-K Pumpa [J].Annals of The New York Academy Of Science,1992,671(1):113-119.
[88] Yu S P. Na+,K+ATPase:the new face of an old player in pathogenesis and apoptotic/hybridcell death[J].Biochemical Pharmacology,2003,66(8):1602-1609.
[89] Qin H, Srinivasula S M,Wu G, et al. Structural basis of procaspase-9recruitment by theapoptotic protease-actvating factor1[J]. Nature,1999,399(6736):549-557.
[90]史培磊，闵辉辉，李春保,等.滚揉腌制前后鹅肉品质的变化[J].食品科学,2011,32(11):88-92.
[91]戴四发,闻爱友,王立克,等.肉仔鸡肌肉色泽与品质相关性研究[J].中国农业大学学报,2007,12(1):61-64.
[92] Seemann M. Factor which influence pigmentation [J].Lohmann Information,2000,24:20-24.
[93] Toyomizu M, Sato K, Taroda H, et al. Effects of dietary Spirulina on meat colour in muscleof broiler chickens [J]. British Poultry Science,2001,42:197-202.
[94] Wulf D M, and Wise J W. Measuring muscle color on beef carcasses using the L*a*b*colorspace [J]. Journal of Animal Science,1999,77:2418-2427.
[95] Culler R D, Parrish F C, Smith G C, et al. Relationship of myofibril fragmentation index tocertain chemical、physical and sensory characteristics of bovine longissimus muscle [J].Journal of Food Science,1978,43:1177-1180.
[96]吴菊清,李春保,周光宏,等.宰后成熟过程中冷却牛肉、猪肉色泽和嫩度的变化[J].食品科学,2008,29(10):136-139.
[97] Zhou Y. The protection of selenium on ROS mediated-apoptosis by mitochondria dysfunctionin cadmium-induced LLC-PK1cells[J]. Toxicology in Vitro,2009,(23):288–294
[98]杨月春,王士勇,李钟淑,等.延边黄牛核移植胚胎的活性氧含量的测定[J].西南农业学报,2010,23(1):210-213.
[99]施广璞，杜洪震，刘子文,等. H2O2致WB-F344细胞内活性氧的产生及机理[J].生物物理学报,2002,18(4):462-465.
[100]袁长青,丁振华.Caspase的结构与功能[J].国外医学生物学手册，2002,24(3):146-151.
[101]王筱冰,张小翠,夏妙红,等.Caspase的活化机制[J].现代生物医学进展，2006,6(3):53-55.
[102] Huang M, and Huang F. The effect of active caspase-3on degradation of chickenmyofibrillar proteins and structure of myofibrils[J]. Food Chemistry,2011,(128):22–27.
[103]马书燕,李吉跃,彭祚登.人工老化过程中柔枝松种子丙二醛(MDA)含量变化研究[J].2011,7:11-15.
[104] Jaisser F,Horisberger J-D, and Rossier B C.The β Subunit Modulates Potassium Activationof the Na-K Pumpa [J].Annals of The New York Academy Of Science,1992,671(1):113-119.
[105] Yu B P. Cellular defenses against damage from reactive oxygenspecies[J]. Physiological. Reviews,1994,74:139–161.
[106] Hail N, Kim H J, and Lotan R. Mechanisms of fenretinide-induced apoptosis[J].Apoptosis,2006,11:1677-1694.
[107] Groeger G, Quiney C, and Cotter T G. Hydrogen peroxide as a cell-survival signalingmolecule[J]. Antioxid. Redox Signal,2009,11:2655-2671.
[108] Qanungo S, Wang M, and Nieminen A. L. N-Acetyl-L-cysteine enhances apoptosisthrough inhibition of nuclear factor-kappaB in hypoxic murine embryonic fibroblasts[J].National Institutes of Health,2004,279:50455-50464.
[109] Kemp C M, Parr T, Bardsley R G, et al. Comparison of the relative expression ofcaspase isoforms in different porcine skeletal muscles[J]. Meat Science,2006,73:426-431.
[110] Zhai W, Feng R, Huo L, Li J, et al. Mechanism of the protective effects ofN-acetylcysteine on the heart of brain-dead Ba-Ma miniature pigs[J]. TheJournal ofHeart and Lung Transplantation,2009,28:944–949.
[111] Du J, Wang X N, and Miereles C. Activation of caspase-3is an initial step triggeringaccelerated muscle proteolysis in catabolic conditions[J]. The Journal of ClinicalInvestigation,2004,113(1):115-123.
[112] Etlinger J D, Zak R, and Fischman D A. Compositional studies of myofibrils fromrabbit striated muscle[J]. Journal of Cell Biology,1976,68(1):123–141.
[113] Huang M, and Huang F. The effect of active caspase-3on degradation of chickenmyofibrillar proteins and structure of myofibrils [J]. Food Chemistry,2011,128(1):22-27.
[114] Huang X, Li Q, Li H, and Guo L. Neuroprotective and Antioxidative Effect of CactusPolysaccharides In Vivo and In Vitro [J]. Cellular and Molecular Neurobiology,2009,29:1211-1221.
[115] Silveira L R, Pereira-Da-Silva L, Juel C, et al. Formation of hydroric peroxide and nitricoxide in rat skeletal muscle cells during contractions[J]. Free Radical Biology&Medicine,2003,35:455-464.
[116] Taylor R G, Geesink G H, Thompson V F, et al. Is Z-disk degradation responsible forpostmortem tenderization [J]? Journal of Animal Science,1995,73(5),1351-1367.
[117] Chatot C L, Ziomek C A, Bvaister B D, et al. Toerrs.An improved culture mediumSupports development of rardom-bred l-cell mouse embryos in vitro[J]. RePord. Fert.1989,86:679-688.
[118] Yi J Z. The protection of selenium on ROS mediated-apoptosis by mitochondriadysfunction in cadmium-induced LLC-PK1cells [J]. Toxicology in Vitro,2009,(23):288-294.