臺灣博碩士論文加值系統

本研究之目的，旨在探討豬隻品種及性別對屠後腰大肌calpain及肌原纖維蛋白質降解之影響。試驗I：比較盤克夏豬及台灣商業黑豬(50 %桃園種與50 %杜洛克種)之變化；試驗II：比較台灣商業黑豬及畜試黑豬(25 %桃園種與75 %杜洛克種)之閹公豬及女豬之變化；試驗III：比較三品種豬(25 %藍瑞斯、25 %約克夏與50 %杜洛克)之公豬、女豬及閹公豬之變化。將屠後12小時之豬腰大肌(Psoas major muscle)真空包裝置於5℃貯存，每隔0、1、3、7及14日逢機採樣。屠後腰大肌之pH結果顯示，無論是試驗I之盤克夏豬與台灣商業黑豬間、試驗II之台灣商業黑豬與畜試黑豬之閹公豬及女豬間、或試驗III 之三品種公豬、女豬及閹公豬間均無顯著差異(P＞0.05)。SDS-PAGE、western blot及casein zymography分析屠後腰大肌titin、desmin、troponin-T、vinculin及&;micro;-calpain之降解速率結果顯示，試驗I為盤克夏豬較台灣商業黑豬為快；試驗II為畜試黑豬較台灣商業黑豬為快，且閹公豬遠快於女豬；試驗III為三品種閹公豬比女豬及公豬為快。綜上所述，豬隻品種及性別可以影響屠後腰大肌calpain及肌原纖維蛋白質降解之變化。

The purpose of this study was to investigate the postmortem proteolysis of porcine Psoas major muscle as affected by breed and sex. There were three experiments in this master thesis. The first experiment was to compare the postmortem proteolysis in Psoas major muscle from Berkshire and Taiwan black pigs (50 % Taoyuan and 50 % Duroc, TD). The second experiment was to compare the postmortem proteolysis in Psoas major muscle between barrows and gilts of TD and Taiwan Livestock Research Institute Black Pig no. 1 (25 % Taoyuan and 75 % Duroc, TBP). The third experiment was to compare the postmortem proteolysis in Psoas major muscle among boars, gilts and barrows of LYD pigs (25 % Landrace, 25 % Yorkshire and 50 % Duroc). Psoas major muscle was removed from the carcasses after 12 hr postmortem, vacuum-packed and stored at 5℃. Myofibrils were prepared from the muscle samples that were randomly taken after 0, 1, 3, 7 and 14 days of storage. The results showed that postmortem pH values were no significant difference (P＞0.05) in each individual experiment. Autolysis of &;micro;-calpain and degradation of titin, desmin, troponin-T and vinculin were analyzed by the SDS-PAGE and western blots. Changes in &;micro;-calpain activity were examined by casein zymography. The results of the first experiment showed that postmortem proteolysis was more rapid in Berkshire than in TD pigs. The results of the second experiment showed that postmortem proteolysis was faster in TBP than in TD pigs. Both the second and third experiments showed that postmortem proteolysis of Psoas major muscle occurred more rapidly in barrows than in gilts or boars. In conclusion, the results indicated that the postmortem proteolysis of porcine Psoas major muscle could be affected by breed and sex.

壹、前言 1
貳、文獻檢討 3
一、屠後貯存期間肌原纖維/細胞骨蛋白質之降解與食肉嫩化
之關係 3
(一) Titin之降解 3
(二) Nebulin之降解 4
(三) Desmin之降解 4
(四) Troponin-T之降解及~30 kDa成分之產生 5
(五) Vinculin與Metavinculin之降解 6
二、中性依鈣酵素系統(Calpain system) 7
(一) &;micro;-及m-calpain之結構特性 7
(二) Calpastatin之結構特性 12
(三) Calpain 3/p94之結構特性 13
(四) Calpain之自體水解 14
(五) Calpain與屠後食肉肌原纖維蛋白質降解之關係 15
(六) 影響calpain活性之因子 16
(七) Casein zymography 17
三、影響屠後食肉嫩化之因子 18
(一) 動物種類 (Species) 18
(二) 性別 (Sex) 19
(三) 年齡 (Age) 20
(四) 肌纖維型態 (Fiber type) 20
(五) 冷收縮 (Cold-shortening) 21
參、材料與方法 23
一、試驗材料之製備 23
試驗I：探討豬隻品種對屠後腰大肌calpain及肌原纖維蛋白質
降解之變化 23
試驗II：探討黑豬品種及性別對屠後腰大肌calpain及肌原纖維
蛋白質降解之影響 23
試驗III：探討豬隻性別對屠後腰大肌calpain及肌原纖維蛋白質
降解之影響 24
二、試驗方法 24
(一) pH值測定 24
(二) 肌原纖維之製備 25
(三) 蛋白質濃度之測定 25
(四) 肌原纖維蛋白質之電泳(SDS-PAGE)測定 26
(五) Vinculin之電泳(SDS-PAGE)測定 26
(六) Western blotting分析 27
(七) Casein zymography 27
肆、結果與討論 29
試驗I：探討豬隻品種對屠後腰大肌calpain及肌原纖維蛋白質
降解之變化 29
一、品種對屠後腰大肌pH值之變化 29
二、品種對屠後腰大肌titin之變化 29
三、品種對屠後腰大肌desmin之變化 32
四、品種對屠後腰大肌troponin-T之降解及其降解成分之
變化 32
五、品種對屠後腰大肌metavinculin及vinculin之變化 35
六、品種對屠後腰大肌μ-calpain自體水解之變化 37
七、品種對屠後腰大肌之casein zymography變化 39
試驗II：探討黑豬品種及性別對屠後腰大肌calpain及肌原纖維
蛋白質降解之影響 42
一、黑豬品種及性別對屠後腰大肌pH值之影響 42
二、黑豬品種及性別對屠後腰大肌titin之影響 42
三、黑豬品種及性別對屠後腰大肌desmin之影響 45
四、黑豬品種及性別對屠後腰大肌troponin-T之降解及其
降解成分之影響 45
五、黑豬品種及性別對屠後腰大肌metavinculin及vinculin
之影響 48
六、黑豬品種及性別對屠後腰大肌μ-calpain自體水解之
影響 48
七、黑豬品種及性別對屠後腰大肌casein zymography之
影響 51
試驗III：探討豬隻性別對屠後腰大肌calpain及肌原纖維蛋白質
降解之影響 54
一、性別對屠後腰大肌pH值之影響 54
二、性別對屠後腰大肌titin之影響 54
三、性別對屠後腰大肌desmin之影響 54
四、性別對屠後腰大肌troponin-T之降解及其降解成分之
影響 58
五、性別對屠後腰大肌metavinculin及vinculin之影響 58
六、性別對屠後腰大肌μ-calpain自體水解之影響 61
七、性別對屠後腰大肌casein zymography之影響 61
伍、結論 65
陸、參考文獻 66
附錄一
附錄二

周榮吉、陳明造、林慶文。1993。食肉的低溫熟成。科學農業41 (9,10)：203-208。
林亭妏。2007。水禽品種、性別與年齡對屠後骨骼肌肌原纖維蛋白質低溫貯存變化之影響。
洪韻絜。2006。比較閹公豬與女豬腰大肌之屠後變化及黑麴菌蛋白&;#37238;對豬腰大肌肌原纖維蛋白質降解之影響。國立嘉義大學碩士論文。
蔡世芬。2006。維生素E及鈣離子對鵝隻屠後骨骼肌肌原纖維蛋白質降解之影響。國立嘉義大學碩士論文。
蔡金生、劉建甫、李茂盛，陳添福、蘇天明、顏念慈、廖宗文、黃鈺嘉、張秀鑾、陳義雄、王政騰。2003。畜試黑豬繁殖及生長性能之探討。畜產研究36(4)：317-325。
顏念慈。2001。台灣黑色豬之遺傳特性之研究。國立中興大學博士論文。
Aoki, K., S. Imajoh, S. Ohno, Y. Emori, M. Koike, G. Kosaki, and K. Suzuki. 1986. Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (mCANP) deduced from its cDNA sequence. FEBS Lett. 205:313-317.
Appelt, D., B. Buenviaje, C. Champ, and C. Franzini-Armstrong. 1989. Quantitation of feet content in two types of muscle fibers from hind limb of the rat. Tissue Cell 21:783-794.
Appelt, D., V. Shen, and C. Franzini-Armstrong. 1991. Quantitation of Ca ATPase, feet and mitochondria in super fast muscle fibers from thetoadfish, Opsanus tau. J. Muscle Res. Cell Motil. 12:543-552.
Arthur, J. S. C., S. Gauthier, and J. S. Elce. 1995. Active site residues in m-calpain: Identification by site-directed mutagenesis. FEBS Lett. 368:397-400.
Ashmore, C. R. and L. Doerr. 1971. Comparative aspects of muscle fiber types in different species. Exper. Neurol. 31:408-418.
Bandman, E. and D. Zdanis. 1988. An immunological method to assess protein degradation in post-mortem muscle. Meat Sci. 22:1-19.
Barnoy, S., Y. Zipser, T. Glaser, Y. Grimberg, and N. S. Kosower. 1999. Association of calpain (Ca2+-dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts. J. Cell. Biochem. 74:522-531.
Baron, C. P., S. Jacobsen, and P. P. Purslow. 2004. Cleavage of desmin by cysteine proteases: Calpains and cathepsin B. Meat Sci. 68:447-456.
Bennett, P. M. and M. Gautel. 1996. Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament. J. Mol. Biol. 259:896-903.
Boehm, M. L., T. L. Kendall, V. F. Thompson, and D. E. Goll. 1998. Changes in the calpains and calpastatin during postmortem storage of bovine muscle. J. Anim. Sci. 76:2415-2434.
Bond, J. J. and R. D. Warner. 2007. Ion distribution and protein proteolysis affect water holding capacity of longissimus thoracis et lumborum in meat of lamb subjected to antemortem exercise. Meat Sci. 75:406-414.
Brodsky, I. G., P. Balagopal, and K. S. Nair. 1996. Effects of testosterone replacement on muscle mass and muscle protein synthesis in hypogonadal men-a clinical research center study. J. Clin. Endocrinol. Metab. 81:3469.
Brooke, M. H. and K. K. Kaiser. 1970. Three myosin adenosine triphosphatase system: The nature of their pH liability and sulphydryl dependence. J. Histochem. Cytochem. 18:670-672.
Brown, N. and C. Crawford. 1993. Structural modifications associated with the change in Ca2+ sensitivity on activation of m-calpain. FEBS. Lett. 322:65-68.
Busch, W. A., M. H. Stromer, D. E. Goll, and A. Suzuki. 1972. Ca2+-specific removal of Z-lines from rabbit skeletal muscle. J. Cell Biol. 52:67-381.
Camou, J. P, J. A. Marchello, V. F. Thompson, S. W. Mares, and D. E. Goll. 2007. Effect of postmortem storage on activity of μ- and m-calpain in five bovine muscles. J. Anim. Sci. 85:2670-2681.
Carragher, N. O. and M. C. Frame. 2002. Calpain: a role in cell transformation and migration. Int. J. Biochem. Cell Biol. 34:1539-1543.
Cha, S. T., T. F. Tseng, S. S. Ho, and R. G. R. Chou. 2002. Comparison of postmortem proteolysis between breast and leg muscles in Chiayi native chickens. Asian-Aust. J. Anim. Sci. 15:21-724.
Channon, H. A., M. G. Kerr, and P. J. Walker. 2004. Effect of Duroc content, sex and ageing period on meat and eating quality attributes of pork loin. Meat Sci. 66:881-888.
Chou, R. G. R., K. J. Lin, and T. F. Tseng. 1996. Post-mortem changes in breast muscles of mule duck. J. Sci. Food Agric. 71:99-102.
Chou, R. G. R., T. F. Tseng, K. J. Lin, and J. H. Yang. 1994. Postmortem changes in myofibrillar proteins of breast and leg muscles from broilers, spent hens and Taiwanese Country Chickens. J. Sci. Food Agric. 65:297-302.
Christensen, M., P. Henckel, and P. P. Purslow. 2004. Effect of muscle type on the rate of post-mortem proteolysis in pigs. Meat Sci. 66:595-601.
Claeys, E., S. D. Smet, D. Demeyer, R. Geers, and N. Buys. 2001. Effect of rate of pH decline on muscle enzyme activities in two pig lines. Meat Sci. 57:257-263.
Croall, D. E., K. Moffett, and H. Hatch. 2002. Casein zymography of calpains using a 4-(2-Hydroxyethyl)-1-piperazineethanesulfonic acid imidazole buffer. Anal. Biochem. 304:129-132.
Cullen, M. J, J. J. Fulthorpe, and J. B. Harris. 1992. The distribution of desmin and titin in normal and dystrophic muscle. Acta Neuropathol. 83:158-169.
Da Silva, A. C. R., and F. C. Reinach. 1991. Calcium binding induces conformational changes in muscle regulatory proteins. TIBS 16:53-57.
Dargelos, E., C. Brul&;eacute;, L. Combaret, A. H. Sassi, S. Dulong, S. Poussard, and P. Cottin. 2007. Involvement of the calcium-dependent proteolytic system in skeletal muscle aging. Exp. Gerontol. 42:1088-1098.
Dikeman, M. E., G. B. Reddy, V. H. Arthaud, H. J. Tuma, R. M. Koch, R. W. Mandigo, and J. B. Axe. 1986. Logissimus muscle quality, palatability and connective tissue histological characteristics of bulls and steers fed different energy levels and slaughtered at four ages. J. Anim. Sci. 63:92-101.
Doumit, M. E. and M. Koohmaraie. 1999. Immunoblot analysis of calpastatin degradation: evidence for cleavage by calpain in postmortem muscle. J. Anim. Sci. 77:1467-1473.
Dransfield, E., R. C. D. jones, and H. J. H. Macfie. 1981. Tenderising in M. Longissimus dorsi of beef, veal, rabbit, lamb and pork. Meat Sci. 5:139.
Duckett, S. K., G. D. Snowder, and N. E. Cockett. 2000. Effect of the callipyge gene on muscle growth, calpastatin activity, and tenderness of three muscles across the growth curve. J. Anim. Sci. 78:2836-2841.
Emori, Y., H. Kawasaki, S. Imajoh, S. Kawashima, and K. Suzuki. 1986. Isolation and sequence analysis of cDNA clones for the small subunit of rabbit calcium-dependent protease. J. Biol. Chem. 261:472-9476.
Emori, Y., H. Kawasaki, S. Imajoh, Y. Minami, and K. Suzuki. 1988. All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. J. Biol. Chem. 263:2364-2370.
Ertbjerg, P., M. M. Mielche, L. M. Larsen, and A. J. M&;oslash;ller. 1999. Relationship between proteolytic changes and tenderness in prerigor lactic acid marinated beef. J. Sci. Food Agric. 79:970-978.
Etherington, D. J., M. A. J. Taylor, and E. Dransfield. 1987. Conditioning of meat from different species. Relationship between tenderizing and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase. Meat Sci. 20:1.
Evans, R. R., R. M. Robson, and M. H. Stromer. 1983. Properties of smooth muscle vinculin. J. Biol. Chem. 259:3916-3924.
Farouk, M. M. and J. E. Swan. 1997. Acceptability and functional properties of restructured roast from frozen pre-rigor injected beef. Meat Sci. 46:57-66.
Franzini-Armstrong, C., C. Champ, and D. G. Ferguson. 1988. Discrimination between fast and slow twitch fibers of guinea pig skeletal muscle using the relative surface density of junctional transverse tubule membrane. J. Muscle Res. Cell Motil. 9: 403-414.
Friz, J. D. and M. L. Greaser. 1991. Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, Western blotting and immunofluorescence microscopy. J. Food Sci. 56:607-610.
Geesink, G. H. and M. Koohmaraie. 1999. Effect of calpastatin on degradation of myofibrillar proteins by &;micro;-calpain under postmortem conditions. J. Anim. Sci. 77:2685-2692.
Geesink, G. H. and M. Koohmaraie. 2000. Ionic strength-induced inactivation of μ-calpain in postmortem muscle. J. Anim. Sci. 78:2336-2343.
Geesink, G. H., R. G. Taylor, and M. Koohmaraie. 2005. Calpain 3/p94 is not involved in postmortem proteolysis. J. Anim. Sci. 83:1646-1652.
Geesink, G. H., S. Kuchay, A. H. Chishti, and M. Koohmaraie. 2006. &;micro;-Calpain is essential for postmortem proteolysis of muscle proteins. J. Anim. Sci. 84:2834-2840.
Gil-Parrado, S., O. Popp, T. A. Knoch, T. A. Zahler, F. Bestvater, M. Felgentr&;auml;ger, A. Holloschi, A. Fern&;aacute;ndez-Montalav&;aacute;n, E. Auerswald, H. Fritz, P. Fluentes-Prior, W. Machleidt, and E. Spiess. 2003. Subcellular localization and in vivo subunit interactions of ubiquitous μ-calpain. J. Biol. Chem. 278:16336-16346.
Goll, D. E. 1991. Role of proteinases and protein turnover in muscle growth and meat quality. Recip. Meat Conf. Proc. 44:25-33.
Goll, D. E., R. B. Young, and M. H. Stromer. 1974. Separation of subcellular organelles by differential and density gradient centrifugation. Recip. Meat Conf. Proc. 27:250-255.
Goll, D. E., V. F. Thompson, H. Li, W. Wei, and J. Cong. 2003. The calpain system. Physiol. Rev. 83:731-801.
Goll, D. E., V. F. Thompson, R. G. Taylor, and J. A. Christiansen. 1992. Role of the calpain system in muscle growth. Biochimie. 74:225-237.
Goll, D. E., Y. Otsuka, P. A. Nagainis, J. D. Shannon, S. K. Sathe, and M. Muguruma. 1983. Role of muscle proteinases in maintenance of muscle integrity and mass. J. Food Biochem. 7:137-141.
Gorza, L. 1990. Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of istochemical myosin ATPase and anti-myosin monoclonal antibodies. J. Histochem. Cytochem. 38:257-265.
Grabarek, Z., I. Tao, and J. Gergely. 1992. Molecular mechanism of troponin-C function. J. Muscle Res. Cell. Motil. 13:383-393.
Helman, E. E., E. Huff-Lonergan, G. M. Davenport, and S. M. Lonergan. 2003. Effect of dietary protein on calpastatin in canine skeletal muscle. J. Anim. Sci. 81:2199-2205.
Ho, C. Y., M. H. Stromer, and R. M. Robson. 1994. Identification of the 30 kDa polypeptide in postmortem skeletal muscle as a degradation product of troponin-T. Biochimie. 76:369-375.
Ho, C. Y., M. H. Stromer, and R. M. Robson. 1996. Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle. J. Anim. Sci. 74:1563-1575.
Ho, C. Y., M. H. Stromer, G. Rouse, and R. M. Robson. 1997. Effects of electrical stimulation and postmortem storage on changes in titin, nebulin, desmin, troponin-T, and muscle ultrastructure in Bos indicus crossbred cattle. J. Anim. Sci. 75:366-376.3
Horowits, R., E. S. Kempner, M. E. Bisher, and R. J. Podolsky. 1986. A physiological role for titin and nebulin in skeletal muscle. Nature. 323:160-162.
Hosfield, C. M., J. S. Elce, P. L. Davies, and Z. Jia. 1999. Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation. EMBO J. 18:6880-6889.
Huff-Lonergan, E. and S. M. Lonergan. 2005. Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. Meat Sci. 71:194-204.
Huff-Lonergan, E., T. Mitsuhashi, D. D. Beekman, F. C. Parrish, Jr., D. G. Olson, and R. M. Robson. 1996. Proteolysis of specific muscle structural proteins by mu-calpain at low temperature is similar to degradation in postmortem bovine muscle. J. Anim. Sci. 74:993-1008.
Huff-Longergan, E., F. C. Parrish, Jr., and R. M. Robson. 1995. Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle. J. Anim. Sci. 73:1064-1073.
Hwan, S. F. and E. Bandman. 1989. Studies of desmin and α-actinin degradation in bovine semitendinosus muscle. J. Food Sci. 54:1426-1430.
Hwang, I. H., B. Y. Park, S. H. Cho, and J. M. Lee. 2004. Effects of muscle shortening and proteolysis on Warner-Bratzler shear force in beef longissimus and semitendinosus. Meat Sci. 68:497-505.
Ilian, M. A., A. E. D. Bekhit, and R. Bickerstaffe. 2004. The relationship between meat tenderization, myofibril fragmentation and autolysis of calpain 3 during post-mortem aging. Meat Sci. 66:387-397.
Imajoh, S., H. Kawasaki, and K. Suzuki. 1986. The amino-terminal hydrophobic region of the small subunit of calcium-activated neutralprotease (CANP) is essential for its activation by phosphatidylinositol. J. Biochem. 99:1281-1284.
Imajoh, S., H. Kawasaki, Y. Emori, S. Ishiura, Y. Minami, H. Sugita, K. Imahori, and K. Suzuki. 1987. A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity. FEBS Lett. 215:274-278.
Imajoh, S., K. Aoki, S. Ohno, Y. Emori, H. Kawasaki, H. Sugihara, and K. Suzuki. 1988. Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease. Biochem. 27:8122-8128.
Inomata, M., Y. Kasai, M. Nakamura, and S. Kawashima. 1988. Activation mechanism of calcium activated neutral protease. J. Bio. Chem. 263:19783-19787.
Jin, J. P. and K. Wang. 1991. Nebulin as a giant actin-binding template protein in skeletal muscle sarcomere: Interaction of actin and cloned human nebulin fragments. FEBS Lett. 281:93-96.
Kadim, I. T, O. Mahgoub, W. AI-Marzooqi, S. AI-Zadjali, K. Annamalai, and M. H. Mansour. 2006. Effects of age on composition and quality of muscle Longissimus thoracis of the Omani Arabian camel (Camelus dromedaries). Meat Sci. 73:619-625.
Kendall, T. L., M. Koohmaraie, J. R. Arbona, S. E. Williams, and L. L. Young. 1993. Effect of pH and ionic strength on bovine m-calpain and calpastatin activity. J. Anim. Sci. 71:96-104.
Kent, M. P., M. J. Spencer, and M. Koohmaraie. 2004. Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin. J. Anim. Sci. 82:794-801.
Khorchid, A. and M. Ikura. 2002. How calpain is activated by calcium. Nature Struct. Biol. 9:239-241.
Kim, N. K., J. H. Lim, M. J. Song, O. H. Kim, B. Y. Park, M. J. Kim, I. H. Hwang, and C. S. Lee. 2008. Comparisons of longissimus muscle metabolic enzymes and muscle fiber types in Korean and western pig breeds. Meat Sci. 78:455-460.
Kim, Y. S., R. D. Sainz, and Y. B. Lee. 1993. Note on the comparison of calpains I, II and calpastatin activity in two different types of porcine skeletal muscles. Comp. Biochem. Physiol. 105:235-237.
Koohmaraie, M. 1992. The role of Ca2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness. Biochimie 74:239-245.
Koohmaraie, M. and G. H. Geesink. 2006. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat. Sci. 74:34-43.
Koohmaraie, M., G. Whipple, D. H. Kretchmar, J. D. Crouse, and H. J. Mersmann. 1991. Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. J. Anim. Sci. 69:617-624.
Koohmaraie, M., M. E. Doumit, and T. L. Wheeler. 1996. Meat toughening does not occur when rigor shortening is prevented. J. Anim. Sci. 74:2935-2942.
Koohmaraie, M., S. C. Seideman, J. E. Schollmeyer, T. R. Dutson, and J. D. Crouse. 1987. Effect of post-mortem storage on Ca2+-dependent proteases, their inhibitor and myofibril fragmentation. Meat Sci. 19:187-196.
Koohmaraie, M., S. C. Seideman, J. E. Shollmeyer, T. R. Dutson, and A. S. Babiker. 1988. Factors associate with the tenderness of three bovine muscles. J. Food Sci. 53:407-410.
Koohmaraie, M., S. D. Shackelford, T. L. Wheeler, S. M. Lonergan, and M. E. Doumit. 1995. A muscle hypertrophy condition in lamb (callipyge): Characterization of effects on muscle growth and meat quality traits. J. Anim. Sci. 73:3596-3607.
Koohmaraie, M., W. H. Kennick, A. F. Anglemier, E. A. Elgasim, and T. K. Jones. 1984. Effect of postmortem storage on cold shortened bovine muscle: Analysis by SDS-polyacrylamide gel electrophoresis. J. Food Sci. 49:290-291.
Kristensen, L. and P. P. Purslow. 2001. The effect of ageing on the water-holding capacity of pork: Role of cytoskeletal proteins. Meat Sci. 58:17-23.
Labeit, S., B. Kolmerer, and W. A. Linke. 1997. The giant protein titin. Emerging roles in physiology and pathophysiology. Circ. Res. 80:290-294.
Labeit, S., T. Gibson, A. Lakey, K. Leonard, M. Zevani, P. Knight, J. Wardale, and J. Trinick. 1991. Evidence that nebulin is a protein-ruler in muscle thin filaments. FEBS Lett. 282:313-331.
Laemmli, U, K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
Lametsch, R., R. Peter, and B. Emoke. 2002. Identification of protein degradation during postmortem storage of pig meat. J. Agric. Food Chem. 50:5508-5512.
Lee, H. L., V. S. Lhoutellier, S. Vigouroux. Y. Briand, and M. Briand. 2007. Calpain specificity and expression in chicken tissues. Comp. Biochem. Physiol. 146:88-93.
Li, H., V. F. Thompson, and D. E. Goll. 2004. Effect of autolysis on properties of μ- and m-calpain. Biochim. Biophys. Acta. 1691:91-103.
Lin, C. S. and C. W. Hsu. 2005. Differentially transcribed genes in skeletal muscle of Duroc and Taoyuan pigs. J. Anim. Sci. 83:2075-2086.
Locker, R. H. and D. J. C. Wild. 1984. “Aging” of cold shortened meat depends on the criterion. Meat Sci. 10:235-238.
Lonergan, S. M., E. Huff-Lonergan, B. R. Wiegand, and L. A. Kriese-Anderson. 2001. Postmortem proteolysis and tenderization of top loin steaks from Brangus cattle. J. Muscle Food. 12:121-136.
Maddock, K. R., E. Huff-Lonergan, L. J. Rowe, and S. M. Lonergan. 2005. Effect of pH and ionic strength on &;micro;-and m-calpain inhibition by calpastatin. J. Anim. Sci. 83:1370-1376.
Maddock, K. R., E. Huff-Lonergan, L. J. Rowe, and S. M. Lonergan. 2006. Effect of oxidation, pH, and ionic strength on calpastatin inhibition of &;micro;-and m-calpain. J. Anim. Sci. 84:925-937.
Maki, M., E. Takano, H. Mori, A. Sato, T. Murachi, and M. Hatanaka. 1987. All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II. FEBS Lett. 223:174-180.
Maki, M., S. Narayana, and K. Hitomi. 1997. A growing family of the Ca2+-binding proteins with five EF-hand motifs. J. Biochem. 328:718-720.
Maruyama, K. 1997. Connectin/titin, giant elastic protein of muscle. FASEB J. 11:341-345.
Melloni, E. and S. Pontremoli. 1989. The calpains. Trends Neurosci. 12:438-444.
Melloni, E. and S. Pontremoli. 1991. The calpain-calpastatin system: Structaral and functional properties. J. Nutr. Biochem. 2:467-475.
Melody, J. L., S. M. Lonergan, L. J. Rowe, T. W. Huiatt, M. S. Mayes, and E. Huff-Lonergan. 2004. Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. J. Anim. Sci. 82:1195-1205.
Milic, A., N. Daniele, H. Lochm&;uuml;ller, M. Mora, G. P. Comi, M. Moggio, F. Noulet, M. C. Walter, L. Morandi, J. Poupiot, C. Roudaut, R. E. Bittner, M. Bartoli, and I. Richard. 2007. A third of LGMD2A biopsies have normal calpain 3 proteolytic activity as determined by an in vitro assay. Neuromuscul. Disord. 17:148-156.
Morgan, J. B., T. L. Wheeler, M. Koohmaraie, J.W. Savell, and J. D. Crouse. 1993. Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers. J. Anim. Sci. 71:1471-1476.
Morrison, E. H., H. A. Bremner, and P. P. Purslow. 2000. Location of and post-mortem changes in some cytoskeletal proteins in pork and cod muscle. J. Sci. Food Agric. 80:691-697.
Muroya, S., I. Nakajima, and K. Chikuni. 2003. Amino acid sequences of multiple fast and slow troponin T isoforms expressed in adult bovine skeletal muscles. J. Anim. Sci. 81:1185-1192.
Muroya, S., S. Kitamura, S. Tanabe, T. Nishimura, I. Nkajima, and K. Chikuni. 2004. N-terminal amino acid sequences of troponin-T fragments, including 30 kDa one, produced during postmortem aging of bovine longissimus muscle. Meat Sci. 67:19-24.
Musa, H. H., G. H. Chen, J. H. Cheng, E. S. Shuiep, and W. B. Bao. 2006. Breed and sex effect on meat quality of chicken. Int. J. Poult. Sci. 5:566-568.
Nakamura, M., Inomata, M. Imajoh, S. Suzuki, and S. Kawashima. 1989. Fragmentation of an endogenous inhibitor upon complex formation with high- and low-Ca2+-requiring forms of calcium-activated neutral proteases. Biochem. 28:449-455.
Neath, K. E., A. N. D. Barrio, R. M. Lapitan, J. R.V. Herrera, L. C. Cruz, T. Fujihara, S. Muroya, K. Chikuni, M. Hirabayashi, and Y. Kanai. 2007. Difference in tenderness and pH deline between water buffalo meat and beef during postmortem aging. Meat Sci. 75:499-505.
Negishi, H., E. Yamamoto, and T. Kuwata. 1996a. The origin of the 30 kDa component appearing during post-mortem aging of bovine muscle. Meat Sci. 42:289-303.
Negishi, H., E. Yamamoto, and T. Kuwata. 1996b. Separation and amino acid composition of three troponin components from bovine muscle. Meat Sci. 42:431-442.
Nishimura, T. and D. E. Goll. 1991. Binding of calpain fragments to calpastatin. J. Biol. Chem. 266:11842-11850.
Northcutt, J. K., T. D. Pringle, J. A. Dickens, R. J. Buhr, and L. L. Young. 1998. Effect of age and tissue type on the calpain proteolytic system in turkey skeletal muscle. Poult. Sci. 77:367-372.
O’Halloran, G. R., D. J. Troy, D. J. Buckley, and W. J. Reville. 1997. The role of endogenous proteases in the tenderization of fast glycolysing muscle. Meat Sci. 47:187-210.
Ohno, S., S. Minoshima, J. Kudoh, R. Fukuyama, Y. Shimizu, S. Ohmi-Imajoh, N. Shimizu, and K. Suzuki. 1990. Four genes for the calpain family locate on four distinct human chromosomes. Cytogenet. Cell Genet. 33:225-229.
Ohno, S., Y. Emori, and S. Suzuki. 1986. Nucleotide sequence of a cDNA coding for the small subunit of human calcium-dependent protease. Nucl. Acids. Res. 14:55-59.
Oliv&;eacute;, M., A. Judith, M. Francesc, P. Adolf, F. Michel, G. Laura, M. Francesca, F. Dirk, A. M. M. Juan, S. Alexey, G. Lev, and F. Isidre. 2007. Phenotypic patterns of desminopathy associated with three novel mutations in the desmin gene. Neuromuscul. Disord. 17:443-450.
Olson, D. G. and F. C. Parrish, Jr. 1977. Relationship of myofibril fragmentation index to measures of beef steak tenderness. J. Food Sci. 42:506-509.
Olson, D. G., F. C. Parrish, Jr., and M. H. Stromer. 1976. Myofibril fragmentation and shear resistance of three bovine muscles during postmortem storage. J. Food Sci. 41:1036-1041.
Oual, A. and A. Talmant. 1990. Calpains and calpastatin distribution in bovine, procine and ovine skeletal muscle. Meat Sci. 28:331-348.
Panaviene, Z., A. D. Xiaodi, E. Michael, and L. M. Carole. 2007. Targeting of nebulin fragments to the cardiac sarcomere. Exp. Res. 313:896-909.
Pardo, J. V., J. D. Siliciano, and S. W. Craig. 1983. A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements (“costameres”) mark sites of attachment between myofibers and sarcolemma. Proc. Natl. Acad. Sci. (USA) 80:1008-1012.
Park, B. Y., N. K. Kim, C. S. Lee, and I. H. Hwang. 2007. Effect of fiber type on postmortem proteolysis in longissimus muscle of Landrace and Korean native black pigs. Meat Sci. 77:482-491.
Parrish, F. C. Jr., R. G. Young, B. E. Miner, and L. D. Anderson. 1973. Effect of postmortem conditions on certain chemical, morphological, and organoleptic propertiec of bovine muscle. J. Food Sci. 38:690-695.
Penny, I. F. and E. Dransfield. 1979. Relationship between toughness and troponin-T in conditioned beef. Meat Sci. 3:135-141.
Pomponio, L., R. Lametsch, A. H. Karlsson, L. N. Costa, A. Grossi, and P. Ertbjerg. 2008. Evidence for post-mortem m-calpain autolysis in porcine muscle. Meat Sci. in press.
Raha, S. and B. H. Robinson. 2000. Mitochondria, oxygen free radicals, disease and ageing. Trends. Biochem. Sci. 25:502-508.
Raser, K. J., A. Posner, and K. W. Wang. 1995. Casein zymography: A method to study μ-calpain, m-calpain and their inhibitory agents. Arch. Biochem. Biophys. 319:211-216.
Reverter, D., H. Sorimachi, and W. Bode. 2001. The structure of calcium-free human m-calpain. Implications for calcium activation and function. Trends. Cardiovasc. Med. 11:222-229.
Richardson, F. L., M. H. Stromer, T. W. Huiatt, and R. M. Robson. 1981. Immunoelectron and fluorescence microscope localization of desmin in mature avian muscles. Eur. J. Cell Biol. 26:91-101.
Richter, C., V. Gogvadze, R. Laffranchi, R. Schlapbach, M. Schweizer, M. Suter, P. Walter, and M. Yaffee. 1995. Oxidants in mitochondria: from physiology to diseases. Biochim. Biophys. Acta 1271:67-74.
Rizo, J. and T. C. S&;uuml;dhof. 1998. C2-domains, structure and function of a universal Ca2+-binding domain. J. Biol. Chem. 273: 15879-15882.
Robson, R. M. 1989. Intermediate filaments. Curr. Opin. Cell Biol. 1:36-43.
Robson, R. M., D. E. Goll, and M. J. Temple. 1968. Determination of protein in “Tris” buffer by the biuret reaction. Anal. Biochem. 24:339-341.
Robson, R. M., E. Huff-Lonergan, F. C. Parrish, C. Y. Ho, M. H. Stromer, T. W. Huiatt, R. M. Bellin, and S. W. Sernett. 1997. Postmortem changes in the myofibrillar and other cytoskeletal proteins in muscle. Recip. Meat Conf. Proc. 50:43-52.
Robson, R. M., J. M. O’Shea, and M. K. Hartzer. 1984. Role of new cytoskeletal elements in maintenance of muscle integrity. J. Food Biochem. 8:1-24.
Robson, R. M., T. W. Huiatt, and F. C. Parrish. Jr. 1991. Biochemical and structural properties of titin, nebulin and intermediate filaments in muscle. Recip. Meat Conf. Proc. 44:7-20.
Root, D. D. and K. Wang. 1994. Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin. Biochem. 33:12581-12591.
Rowe, L. J., K. R. Maddock, S. M. Lonergan, and E. Huff-Longergan. 2004. Oxidative environments decrease tenderization of beef steaks through inactivation of &;micro;-calpain. J. Anim. Sci. 82:3254-3266.
Ryu, Y. C., Y. M. Choi, S. H. Lee, H. G. Shin, J. H. Choe, J. M. Kim, K. C. Hong, and B. C. Kim. 2008. Comparing the histochemical characteristics and meat quality traits of different pig breeds. Meat Sci. in press.
Saido, T. C., H. Sorimachi, and K. Suzuki. 1994. Calpain: New perspectives in molecular diversity and physiological-pathological involvement. FASEB J. 8:814-822.
Samejima, K. and F. H. Wolfe. 1976. Degradation of myofibrillar protein components during post-mortem aging of chicken muscle. J. Food Sci. 41:250-254.
SAS Institute Inc. 1986. User's Guide: Statistics, version 6. Ed. SAS Institute, Inc., Cary, NC.
Sazili, A. Q., G. K. Lee, T. Parr, P. L. Sensky, R. G. Bardsley, and P. J. Buttery. 2003. The effect of altered growth rates on the calpain proteolytic system and meat tenderness in cattle. Meat Sci. 66:195-201.
Sazili, A. Q., T. Parr, P. L. Sensky, S. W. Jones, R. G. Bardsley, and P. J. Buttery. 2005. The relationship between slow and fast myosin heavy chain content, calpastatin and meat tenderness in different ovine skeletal muscles. Meat Sci. 69:17-25.
Seideman, S. C., J. D. Crouse, and H. R. Cross. 1986. The effect of sex condition and growth implants on bovine muscle fiber characteristics. Meat Sci. 17:79-95.
Serrano, M. P., D. G. Valencia, M. Nieto, R. L&;aacute;zaro, and G. G. Mateos. 2008. Influence of sex and terminal sire line on performance and carcass and meat quality of Iberian pigs reared under intensive production systems. Meat Sci. 78:420-428.
Shackelford, S. D., T. L. Wheeler, and M. Koohmaraie. 1995. The effects of in utero exposure of lambs to a β-adrenergic agonist on prenatal and postnatal muscle growth, carcass cutability, and meat tenderness. J. Anim. Sci. 73:2986-2993.
Shear, C. R. and R. J. Bloch. 1985. Vinculin in subsarcolemmal densities in chicken skeletal muscle: Localization and relationship to intracellular and extracellular structures. J. Cell Biol. 101:240-256.
Sorimachi, H. S., S. Imajoh-Ohmi, Y. Emori, H. Kawasaki, S. Ohno, Y. Minami, and K. Suzuki. 1989. Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and μ-types. J. Biol. Chem. 264:20106-20111.
Sorimachi, H., N. E. Forsberg, H. J. Lee, S. Y. Joeng, I. Richard, J. S. Beekmann, S. Ishiura, and K. Suzuki. 1996. Highly conserved structure in the promoter region of the gene for muscle specific calpain, p94. J. Biol. Chem. 377:859-864.
Sorimachi, H., S. Ishiura, and K. Suzuki. 1997. Structure and physiological function of calpains. Biochem. J. 328:721-732.
Sorimachi, H., T. C. Saido, and K. Suzuki. 1994. New era of calpain research. Discovery of tissue-specific calpains. FEBS Lett. 343:1-5.
Steen, D., E. Claeys, L. Uytterhaegen, D. DeSmet, and D. Demeyer. 1997. Early post-mortem conditions and the calpain/calpastatin system in relation to tenderness of double-muscled beef. Meat Sci. 45:307-319.
Strasser, P., M. Gimona, M. Herzog, B. Geiger, and J. V. Small. 1993. Variable and constant regions in the C-terminus of vinculin and metavinculin. FEBS Lett. 317:189-194.
Strobl, S., C. Fernandez-Catalan, M. Braun, R. Huber, H. Masumoto, K. Nakagawa, A. Irie, H. Sorimachi, G. Bourenkow, H. Bartunik, K. Suzuki, and W. Bode. 2000. The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc. Natl. Acad. Sci. (USA) 97:588-592.
Stromer, M. H. 1990. Intermediate filaments (10 nm) in muscle. Pages 19-36 in R. D. Goldman and P. M. Steinert, eds. Cellular and molecular biology of intermediate filaments. Plenum Publishing Corp., New York, NY.
Stromer, M. H., D. E. Goll, W. J. Reville, D. G. Olson, W. R. Dayton, and R. M. Robson. 1974. Structural changes in muscle during postmortem storage. In: Proc. fouth International Congress on Food Science and Technology, Vol 1, Pages 401-408. Institute de Agroquimica y Tecnologia de Alimentos, Jaime Roig, II, Valencia-10, Spain.
Suzuki, K. 1990. The structure of calpains and the calpain genes. Pages 25-35 In R. L. Mellgren, and T. Murachi, eds. Intracellular calcium-dependent proteolysis. CRC Press, Boca Raton, FL.
Suzuki, K. and S. Ohno. 1990. Calcium activated neutral protease-structure-function relationship and functional implications. Cell Struct. Funct. 15:1-6.
Suzuki, K., S. Imajoh, Y. Emori, H. Kawasaki, Y. Minami, and S. Ohno. 1987. Calcium-activated neutral protease and its endogenous inhibitor: Activation at the cell membrane and biological function. FEBS Lett. 220:271-277.
Takano, E. and M. Maki. 1999. Structure of calpastatin and its inhibitory control of calpain. Pages 25-49 In K. Wang, and P. W. Yuen. R. T., eds. Calpain: Pharmacology and toxicology of calcium-dependent protease. Taylor &; Francis, Philadelphia, PA.
Taveau, M., N. Bourg, G. Sillon, C. Roudaut, M. Bartoli, and I. Richard. 2003. Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol. Cell Biol. 23:9127-9135.
Taylor, R. G. and M. Koohmaraie. 1998. Effects of postmortem storage on the ultrastructure of the endomysium and myofibrils in normal and callipyge longissimus. J. Anim. Sci. 76:2811-2817.
Taylor, R. G., G. H. Geesink, V. F. Thompson, M. Koohmaraie, and D. E. Goll. 1995. Is Z-disk degradation responsible for postmortem tenderization? J. Anim. Sci. 73:1351-1367.
Termin, A., R. S. Staon, and D. Pette. 1989. Myosin heavy chain isoforms in histochemically defines fibre types of rat muscle. Histochem. 92:453-457.
Tiidus, P. M., D. Holden, E. Bombardier, S. Zajchowski, D. Enns, and A. Belcastro. 2001. Estrogen effect on post-exercise skeletal muscle neutrophil infiltration and calpain activity. Can. J. Physiol. Pharmacol. 79:400-406.
Tomaszewska-Gras, J., K. Jacek, and J. G. S. Franciscus. 2002. Quantitative determination of titin and nebulin in poultry meat by SDS-PAGE with an internal standard. Meat Sci. 62:61-66.
Tompa, P., Y. Emori, H. Sorimachi, K. Suzuki, and P. Friedrich. 2001. Domain III of calpain is a Ca2+-regulated phospholipids-binding domain. Biochem. Biophys. Res. Comm. 280:1333-1339.
Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheet: Procedure and some application. Proc. Natl. Acad. Sci. 76:4350-4354.
Trinick, J. 1992. Molecular rulers in muscle? Curr. Biol. 2:75-77.
Tullio, R. D., M. Passalacqua, M. Averna, F. Salamino, E. Melloni, and S. Pontremoli. 1999. Changes in intracellular localization of calpastatin during calpain activation. J. Biochem. 343:467-472.
van den Maagdenberg, K., E. Claeys, A. Stinckens, N. Buys, and S. De Smet. 2007. Effect of age, muscle type, and insulin-like growth factor-II genotype on muscle proteolytic and lipolytic enzyme activities in boars. J. Anim. Sci. 85:952-960.
Veiseth, E., S. D. Shackelford, T. L. Wheeler, and M. Koohmaraie. 2001. Effect of postmortem storage on &;micro;-calpain and m-calpain in ovine skeletal muscle. J. Anim. Sci. 79:1502-1508.
Veiseth, E., S. D. Shackelford, T. L. Wheeler, and M. Koohmaraie. 2004. Indicators of tenderization are detectable by 12 h postmortem in ovine longissimus. J. Anim. Sci. 82:1428-1436.
Volpelli, L. A., S. Failla, A. Sepulcri, and E. Piasentier. 2005. Calpain system in vitro activity and myofibril fragmentation index in fallow deer (Dama dama): Effects of age and supplementary feeding. Meat Sci. 69:579-582.
Wang, J. H. and S. T. Jiang. 1991. Properties of calpain II from Tilapia muscle (Tilapia nilotica × Tilapia aurea). Agric. Biol. Chem. 55:339-345.
Wang, K., J. McClure, and A. Tu. 1979. Titin: Major Myofibrillar Components of Striated Muscle. Proc. Natl. Acad. Sci. 76:3698-3702.
Wang, K., M. Knipfer, Q. Q. Huang, A. van Heerden, L. C. L. Hsu, G. Gutierrez, X. L. Quian, and H. Stedman. 1996. Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3. J. Biol. Chem. 271:4303-4314.
Wang, S. M., M. L. Greaser, E. Schultz, J. C. Bulinski, J. C. J. Lin, and J. L. Lessard. 1988. Studies on cardiac myofibrillogenesis with antibodies to titin, actin, tropomyosin, and myosin. J. Cell Biol. 107:1075-1083.
Wegner, J., E. Albrecht, I. Fiedler, F. Teuscher, H. J. Papstein, and K. Ender. 2000. Growth- and breed-related changes of muscle fiber characteristics in cattle. J. Anim. Sci. 78:1485-1496.
Weller, P. A., E. P. Ogryzko, E. B. Corben, N. I. Zhidkova, B. Patel, G. J. Price, N. K. Spurr, V. E. Koteliansky, and D. R. Critchley. 1990. Complete sequence of human vinculin and assignment of the gene to chromosome-10. Proc. Natl. Acad. Sci. 87:5667-5671.
Wendt, A., V. F. Thompson, and D. E. Goll. 2004. Interaction of calpastatin with calpain: A review. Biol. Chem. 385:465-472.
Wheeler, T. L., J. W. Savell, H. R. Cross, D. K. Lunt, and S. B. Smith. 1990. Mechanisms associated with the variation in tenderness of meat from Brahman and Hereford cattle. J. Anim. Sci. 68:4206-4220.
Wheeler, T. L., S. D. Shackelford, and M. Koohmaraie. 2000. Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. J. Anim. Sci. 78:958-965.
Whipple, G. and M. Koohmarale. 1992. Effect of lamb age: Muscle type, and 24 hour activity of endogenous proteinases on postmortem proteolysis. J. Anim. Sci. 70:708-804.
Whipple, G., M. Koohmaraie, M. E. Dikeman, J. D. Crouse, M. C. Hunt, and R. D. Klemm. 1990. Evaluation of attributes that affect longissimus muscle tenderness in Bos Taurus and Bos indicus cattle. J. Anim. Sci. 68:2716-2728.
White, A., A. O’Sullivan, E. E. O’Neill, and D. J. Troy. 2006. Manipulation of the pre-rigor phase to investigate the significance of proteolysis and sarcomere length in determining the tenderness of bovine M. longissimus dorsi. Meat Sci. 73:204-208.
Xie, X., M. D. Dwyer, L. Swenson, M. H. Parker, and M. C. Botfield. 2001. Crystal structure of calcium-free human sorcin: A member of the penta-EF-hand protein family. Protein Sci. 10:2419-2425.
Xiong, Y. L., O. E. Mullins, J. F. Stika, J. Chen, S. P. Blanchard, and W. G. Moody. 2007. Tenderness and oxidative stability of post-mortem muscles from mature cows of various ages. Meat Sci. 77:105-113.
Yen, N. T., M. C. Huang, and C. Tai. 2001. Genetic variations of randomly amplified polymorphic DNA polymorphisms in Taoyuan and Duroc pigs. J. Anim. Breed Genet. 118:111-118.
Yialamas, M. A. and F. J. Hayes. 2003. Androgens and the ageing male and female. Best Pract. Res. Clin. Endocrinol. Metab. 17:223-236.
Young, P., C. Ferguson, S. Banuelos, and M. Gautel. 1998. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EMBO J. 17:1614-1624.
Zaho, X., R. Posmantur, A. Kampfl, S. J. Liu, K. K. W. Wang, J. K. Newcomb, B. Pike, G. L. Clifton, and R. L. Hayes. 1998. Subcellular localization and duration of &;micro;-calpain and m-calpain activity following traumatic brain injury in the rat, a casein zymography study. J. Cereb. Blood Flow Metab. 18:161-167.
Zamora, F., F. Cha&;iuml;b, and E. Dransfueld. 1998. Calpains and calpastatin from cold-shortened bovine M. longissimus lunborum. Meat Sci. 49:127-133.