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Post-mortem changes in chicken muscle

  • F.J.G. Schreurs (a1)

This paper details the post-mortem changes that take place in the muscular tissue of poultry and the consequences of these on the resulting meat quality at the point of consumption. The history of the development if the modern meat type chicken, the form and function of its muscles, the factors that determine muscle growth and their effects on meat quality are all described. Past studies tend to have been concentrated on the processes occuring in mammalian tissue and those mainly on beef, with little attention being directed at the changes taking place in poultry muscle. In this context the view that modern broilers grow “at the edge of what is metabolically possible” is important. This hypothesis owes its origin to the fact that muscle, and thus protein, accretion is accomplished through a dynamic equilibrium between synthesis and degradation. Evidence is provided to show that the muscle cell reaches a certain maximum synthesis capacity, to grow beyond which requires it to decrease its rate of degradation. This property is possibly of considerable influence in meat ageing and forms the basis for the proposition that the breast muscle of poultry is especially suited to study the effects of post-mortem proteolytic degradation on meat ageing and product quality.

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*Deceased. All correspondence should be addressed to T.G. Uijttenboogaart, Institute for Animal Science and Health, PO Box 65, 8200 AB Lelystad, The Netherlands (
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Aberle, E.D., Addis, P.B. and Schoffner, R.N. (1979) Fiber types in skeletal muscle of broiler-and layer-type chickens. Poultry Science 58: 12101212
Addis, P.B. (1986) Poultry muscle as food. In: Muscle as Food (Bechtel, P.J., Ed.), Academic Press, London, pp. 371407
Allen, R.E. and Boxhorn, L.K. (1987) Inhibition of skeletal muscle satellite cell differentiation by transforming growth factor-β. journal of Cell Physiology 133: 567572
Ashgar, A. and Batti, A.R. (1987) Endogenous proteolytic enzymes in skeletal muscle: their significance in muscle physiology and during post mortem aging events in carcasses. Advances in Food Research 31: 343451
Ashgar, A., Morita, J.I., Samejjma, K. and Yasui, T. (1984) Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress. Agricultural and Biological Chemistry 48: 22172224
Ashgar, A., Morita, J.I., Samejima, K. and Yasui, T. (1986) Variation of proteins in subcellular snrcoplasmic fractions of chicken red and white skeletal muscles influenced by under nutrition. Agricultural and Biological Chemistry 50: 19311940
Ashmore, C.R. and Doerr, L. (1971a) Comparative aspects of muscle fiber types in different species. Experimental Neurology 30: 408418
Ashmore, C.R. and Doerr, L. (1971b) Postnatal development of fiber types in normal and dystrophic skeletal muscle of the chick. Experimental Neurology 31: 431446
Azanza, J.L., Rymond, J., Robin, J.M., Cottin, P. and Ducastaing, A. (1979) Purification and some physicochemical and enzymatic properties of a calcium ion-activated neutral proteinase from rabbit skeletal muscle. Biochemical Journal 183: 339347
Ballard, R., Bardsley, R.G. and Buttery, P.J. (1988) Changes in the activity of skeletal muscle calcium-activated neutral proteinase (EC and its specific inhibitor in chickens grown at different rates in response to graded levels of dietary protein. British Journal of Nutrition 59: 141147
Bardsley, R.G., Allcock, S.M.J., Dawson, J.M., Dumelow, N.W., Higgjns, J.A., Lasslett, Y.V., Lockley, A.K., Parr, T. and Buttery, P.J. (1992) Effect of β-agonists on expression of calpain and calpastatin activity in skeletal muscle. Biochimie 74: 267273
Barrett, A.J. (1985) The cystatins: small protein inhibitors of cysteine proteinases. Progress in Clinical Biological Research 180: 105116
Béchet, D.M., Listrat, A., Deval, C., Ferrara, M. and Quirke, J.F. (1990) Cimaterol reduces cathepsin activities but has no anabolic effect in cultured myotubes. American Journal of Physiology 259: E822–827
Bjge, L., Ouali, A. and Valin, C. (1985) Purification and characterisation of a low molecular weight cysteine proteinase inhibitor from bovine muscle. Biochimica Biophysica Acta 843: 269275
Bird, J.W.C., Carter, J.H., Triemer, R.E., Brooks, R.M. and Spanier, A.M. (1980) Proteinases in cardiac and skeletal muscles. Federation Proceedings 39: 2025
Bodensteiner, J.B. and Engel, A.G. (1978) Intracellular calcium accumulation in Duchenne dystrophy and other myopathies: a study of 567,000 muscle fibers in 114 biopsies. Neurology 28: 439446
Bodwell, C.E. and Pearson, A.M. (1964) The activity of partially purified bovine catheptic enzymes on various natural and synthetic substrates. Journal of Food Science 29: 602607
Bowen, S.J., Huybrechts, L.M., Marsh, J.A. and Scanes, C.G. (1987) Influence of triiodothyronine and growth hormone on growth of dwarf and normal chickens. Interactions of hormones and of genotype. Comparative Biochemistry and Physiology 86A: 137142
Busch, W.A., Stromer, M.H., Goll, D.E. and Suzuki, A. (1972) Ca2+ specific removal of Z-lines from rabbit skeletal muscle. Journal of Cell Biology 52: 367381
Buttery, P.J., Dawson, J.M., Beever, D.E. and Bardsley, R.G. (1991) Manipulation of protein deposition in animals and possible consequences on the quality of animal products. Proceedings of the 6th Symposium in Protein Metabolism and Nutrition,Herning,Denmark, pp. 88–102
Carfoli, E. (1982a) The transport of calcium across the inner membrane of mitochondria. In: Membrane Transport of Calcium (Carfoli, E., Ed.), Academic Press, New York, pp. 109117
Carfoli, E. (1982b) The transport of Ca2+ by mitochondria. In: Menbranes and Transport, Volume I (Martonosi, A., Ed.), Plenum Press, New York, pp. 611616
Chambers, J.R., Gavora, J.S. and Fortin, A. (1981) Genetic changes in meat-type chickens in the last twenty years. Canadian journal of Animal Science 61: 555563
Cogburn, L.A. (1991) Endocrine manipulation of body composition in broiler chickens. Critical Reviews in Poultry Biology 3: 283305
Coolican, S.A. and Hathaway, D.R. (1984) Effect of L-alpha-phosphatidylinositol on a vascular smooth muscle Ca2+ -dependent protease. Reduction of the Ca2+ requirement for autolysis. journal of Biological Chemistry 259: 1162711630
Davey, C.L. and Dickson, M.A. (1970) Studies in meat tenderness. 8. Ultrastructural changes in meat during aging. Journal of Food Science 35: 5660
Dayton, W.R. and Hathaway, M.R. (1989) Autocrine, paracrine, and endocrine regulation of myogenesis. In: Animal Growth Regulation (Champion, D.R., Hausman, G.J. and Martin, R.J., Eds), Plenum Press, London, pp. 6990
Dayton, W.R., Goll, D.E., Stromer, M.H., Reville, W.J., Zeece, M.G. and Robson, R.M. (1975) Some properties of a Ca2+ -activated protease that may be involved in myofibrillar protein turnover. In: Protease and Biological Control (Reich, E., Rifkin, D.B. and Show, E., Eds), Cold Spring Harbor Laboratory, New York, pp. 551577
Dayton, W.R., Goll, D.E., Zeece, M.G., Robson, R.M. and Reville, W.J. (1976a) A Ca2+- activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle. Biochemistry 15: 21502158
Dayton, W.R., Reville, W.J., Goll, D.E. and Stromer, M.H. (1976b) A Ca2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterisation of the purified enzyme. Biochemistry 15: 21592167
Dayton, W.R., Schollmeyer, J.V., Chan, A.D. and Allen, C.E. (1979) Elevated levels of acalcium activated muscle protease in rapidly atrophying muscles from vitamin-E deficient rabbits. Biochimica Biophysica Acta 584: 216230
Dayton, W.R., Schollmeyer, J.V., Lepley, R.A. and Cortes, L.R. (1981) A calcium activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calcium requiring form of the protease. Biochimica Biophysica Acta 659: 4861
Defremery, D. (1966) Some aspects of post mortem changes in poultry muscle. In: The Physiology and Biochemistry of Muscle as a Food, Volume 1 (Briskey, E.J., Cassens, R.G. and Trautmann, J.C., Eds), University of Wisconsin Press, Madison, pp. 205212
Demartino, G.N., Huff, C.A. and Croall, D.E. (1986) Autoproteolysis of the small subunit of calcium dependent protease II activates and regulates protease activity. Journal of Biological Chemistry 261: 1204712052
Dufour, E., Ouali, A., Obled, A., Deval, C. and Valin, C. (1989) Lysozomal proteinase- sensitive regions in fast and slow skeletal muscle myosins. Biochimie 71: 625632
Dutson, T.R. (1983) Relationship of pH and temperature to disruption of specific muscle proteins and activity of lysozomal proteases. Journal of Food Biochemistry 7: 223245
Fiskum, G. and Lehninger, A. (1980) The mechanisms and regulation of mitochondria1 Ca2+ transport. Federation Proceedings 39: 24322436
Florini, J.R., Roberts, A.B., Ewton, D.Z., Falen, S.L., Flanders, K.C. and Sport, M.B. (1986) Transforming growth factor-β. A very potent inhibitor of myoblast differentiation, identical to the differentiation inhibitor secreted by buffalo rat liver cells. journal of Biological Chemistry 261: 1650916513
Forsberg, N.E., Ilian, M.A., Ali-bar, A., Cheeke, P.R. and Wehr, N.B. (1989) Effects of cimaterol on rabbit growth and myofibrillar protein degradation and on calcium-dependent proteinase and calpastatin activities in skeletal muscle. Journal of Animal Science 67: 33133321
Fritz, J.D. and Greaser, M.L. (1991) Changes in titin and nebulin in post-mortem bovine muscle revealed by gel electrophoresis, western blotting and immunofluorescence microscopy. Journal of Food Science 56: 607610, 615
Fukazawa, T., Briskey, E.J., Takahashi, F. and Yasui, T. (1969) Treatment and post-mortem aging effects on the' Z-line of myofibrils from chicken pectoral muscle. Journal of Food Science 34: 606610
Fukazawa, T., Nakai, H., Ohki, S. and Yasui, T. (1970) Some properties of myofibrillar proteins obtained from low-ionic strength extracts of washed myofibrils from pre-and post-rigor chicken pectoral muscle. Journal of Food Science 35: 464468
Gann, G.L. and Merkel, R.A. (1978) Ultrastructural changes in bovine longissimus dorsi muscle during post-mortem aging. Meat Science 2: 129144
Gibson, W.R. and Nalbandov, A.V. (1966) Lipid mobilisation in obese hypophysectomized cockerels. American Journal of Physiology 211: 13451351
Goldspink, D.F. (1991) Exercise-related changes in protein turnover in mammalian striated muscle. Journal of Experimental Biology 160: 127148
Goll, D.E., Kleese, W.C. and Szpacenko, A. (1989) Skeletal muscle proteases and protein turnover. In: Animal Growth Regulation (Campion, D.R., Hausman, G.J. and Martin, R.J., Eds), Plenum Press, New York, pp. 141182
Goll, D.E., Thompson, V.F., Taylor, R.C. and Zalewska, T. (1992) Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? BioEssnys 14: 549555
Granger, B.I. and Lazarides, E. (1979) Desmin and vimentin coexist at the periphery of the myofibril z-disk. Cell 18: 10531063
Granger, B.I. and Lazarides, E. (1980) Synemin, a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell 22: 727738
Griffin, H.D. and Goddard, C. (1994) Rapidly growing broiler (meat-type) chickens: their origin and use for comparative studies of the regulation of growth. International Journal of Biochemistry 26: 1928
Gwartney, B.L., Calkins, C.R. and Jones, S.J. (1991) The effect of cimaterol and its withdrawal on carcass composition and meat tenderness of broiler chickens. Journal of Animal Science 69: 15511558
Harper, J.M.M., Mackinson, I. and Buttery, P.J. (1990) The effects of beta agonists on muscle cells in culture. Domestic Animal Endocrinology 7: 477484
Hay, J.D., Currie, R.W. and Wolfe, F.H. (1973a) Polyacrylamide disc gel electrophoresis of fresh and aged chicken muscle proteins in sodium dodecyl sulfate. Journal of Food Science 38: 987990
Hay, J.D., Currie, R.W., Wolfe, F.H. and Sanders, E.S. (1973b) The effects of post-mortem aging on chicken muscle fibrils. Journal of Food Science 38: 981986
Hayashi, K., Tomita, Y., Maeda, Y., Shinagawa, Y., Inoue, K. and Ashizume, T. (1985) The rate of degradation of myofibrillar proteins of skeletal muscle in broiler and layer chickens estimated by Nt-methylhistidine in excreta. British Journal of Nutrition 54: 157163
Henderson, D.W., Goll, D.E. and Stromer, M.H. (1970) A comparison of shortening and 2-line degradation in post mortem bovine, porcine and rabbit muscle. American Journal of Anatomy 128: 117135
Hershko, A., Mamont, P., Shields, R. and Tomkins, G.M. (1971) Pleiotypic response. Nature 232: 206211
Higgins, J.A., Lasslett, Y.V., Bardsley, R.G. and Buttery, P.J. (1988) The relation between dietary restriction or clenbuterol (a selective β2 agonist) treatment on muscle growth and calpain proteinase (EC and calpastatin activities in lambs. BritishJournal of Nutrition 60: 645652
Hocking, P.M. and Saunderson, L. (1992) Muscle protein degradation assessed by Nt- methylhistidine excretion in mature White Leghorn, dwarf broiler and normal broiler males maintained on either low- or high-protein diets. British Journal of Nutrition 67: 391399
Honikel, K.O. and Hamm, R. (1974) On the buffering capacity of meat and its changes post mortem. Zeitschrift für Lebensmittel Untersuchung and Forschung 156: 145152
Huston, R.B. and Krebs, E.G. (1968) Activation of skeletal muscle phosphorylase kinase by Ca2+, 11. Identification of the kinase activating factor as a proteolytic enzyme. Biochemistry 7: 21162122
Huxley, H. and Hanson, J. (1954) Changes in the cross striations of muscle during contraction and stretch and their structural interpretation. Nature 173: 973976
Ioanescu, V., Zellweger, H. and Conway, T.W. (1971) Ribosomal protein synthesis in Duchenne muscular dystrophy. Archives of Biochemistry and Biophysics 144: 5158
Ioanescu, V., Zellweger, H., McCornick, W.F. and Conway, T.W. (1973) Comparison of ribosomal protein synthesis in Becker and Duchenne muscular dystrophies. Neurology 23: 245253
Iodice, A.A., Leong, V. and Weinstock, I.M. (1966) Proteolytic activity of skeletal muscle of normal and dystrophic chickens and rabbits. Enzymologia Biologica et Clinica 6: 269278
Ishiura, S., Murofushi, H., Suzuki, K. and Imahori, K. (1979) Studies of a calcium activated neutral protease from chicken skeletal muscle. 11. Substrate specificity Journal of Biocheinistry 86: 579581
Johnson, R.J. (1989) Growth physiology and biotechnology: potential to improve broiler production. World's Poultry Science Journal 46: 228240
Kar, N.C. and Pearson, C.M. (1976) A calcium activated neutral protease in normal and dystrophic human muscle. Clinica Chimica Acta 73: 293297
Khan, A.W. and Van Den Berg, L. (1963) Storage at above freezing temperatures. Proceedings of the Annual Meeting of the Institute of Food Technologists,Detroit, p. 49
Kiessling, K.H. (1977) Muscle structure and function in the goose, quail, pheasant, guinea hen and chicken. Comparative Biochemistry and Physiology 578: 287292
Koohmaraie, M. (1988) The role of endogenous proteases in meat tenderness. Proceedings of the 41st Reciprocal Meat Conference 89–100
Koohmaraie, M., Babiker, A.S., Merkel, R.A. and Dutson, T.R. (1988) Role of Ca++- dependent proteases and lysozomal enzymes in post-mortem changes in bovine skeletal muscle. Journal of Food Science 53: 12531257
Koohmaraie, M., Kennick, W.H., Anglemier, A.F., Elgasim, E.A. and Jones, T.K. (1984a) Effect of post-mortem storage on cold shortened bovine muscle: analysis by SDS- polyacrylamide gel electrophoresis. Journal of Food Science 49: 290291
Koohmaraie, M., Kennick, W.H., Elgasim, E.A. and Anglemier, A.F. (1984b) Effect of post-mortem storage on muscle protein degradation: analysis by SDS-polyacrylamide gel electrophoresis. Journal of Food Science 49: 292293
Koohmaraie, M., Schollmeyer, J.E. and Dutson, T.R. (1986) Effect of low-calcium- requiring calcium activated factor on myofibrils under varying pH and temperature conditions. Journal of Food Science 51: 2832, 65
Kretschmar, D.H., Hathaway, M.R., Epley, R.J. and Dayton, W.R. (1989) In vivo effect of a P-adrenergic agonist on activity of calcium dependent proteinases, theirspecific inhibitor, and cathepsins B and H in skeletal muscle. Archives of Biochemistry and Biophysics 275: 228235
Kretschmar, D.H., Hathaway, M.R., Epley, R.J. and Dayton, W.R. (1990) Alterations in postmortem degradation of myofibrillar proteins in muscle of lambs fed a P-adrenergic agonist. Journal of Animal Science 68: 17601772
Laurent, G.J., Sparrow, M.P., Bates, P.C. and Millward, D.J. (1978) Turnover of muscle protein in the fowl (Gullus domesticus). Rates of protein synthesis in fast and slow skeletal, cardiac and smooth muscle of the adult fowl. Biochemical Journal 176: 393401
Lawrie, R.E. (1966) Chemical and biochemical constituents of muscle. In: Meat Science (Lawrie, R.E., Ed.), Pergamon Press, London, pp. 66113
Lazarides, E. and Hubbart, B.D. (1976) Immunological characterisation of the subunit of 100 A filaments from muscle cells. Proceedings of the National Academy of Sciences,USA 4344–4348
Lehmann, K.B. (1907) Studies of the causes of toughness in meat. Archiv für Hygiene 63: 134179
Lepetit, J., Sale, P. and Ouali, A. (1986) Post. mortem evolution of rheological properties of the myofibrillar structure. Meat Science 16: 161174
Leung, F.C., Taylor, J.E., Wien, S. and Van Iderstine, A. (1986) Purified chicken growth hormone, (GH) and human pancreatic GH-releasing hormone increase body weight gain in chickens. Endocrinology 118: 1961–1695
Lobley, G.E., Cornell, A., Milne, E., Buchan, V., Calder, A.G., Anderson, S.E. and Vint, H. (1990) Muscle protein synthesis in response to testosterone administration in wether lambs. British Journal of Nutrition 64: 691704
Lochner, J.V., Kauffman, R.G. and Marsh, B.B. (1980) Early post mortem cooling rate and beef tenderness. Meat Science 4: 227241
Locker, R.H. (1987) The non-sliding filaments of the sarcomere. Meat Science 20: 217236
Locker, R.H. and Leet, N.G. (1975) Histology of highly stretched beef muscle. I. The fine structure of grossly stretched single fibers. Journal of Ultrustructure Research 52: 6475
Locker, R.H. and Leet, N.G. (1976a) Histology of highly stretched beef muscle. 11. Further evidence on the location and nature of gap-filaments. Journal of Ultrastructure Research 55: 157172
Locker, R.H. and Leet, N.G. (1976b) Histology of highly stretched beef muscle. IV. Evidence for movement of gap-filaments through the Z-line, using the N,-line and M-line as markers. Journal of Ultrastructure Research 56: 3138
Locker, R.H. and Wild, D.J.C. (1984a) The N-lines of skeletal muscle. Journal of Ultrastructure Research 88: 207222
Locker, R.H. and Wild, D.J.C. (1984b) Tenderization of meat by pressure-heat treatment involves weakening of the gap filaments in the myofibrils. Meat Science 10: 207233
Locker, R.H. and Wild, D.J.C. (1984c) The fate of the large proteins of the myofibril during tenderising treatments. Meat Science 11: 89108
Lusby, M.L., Ridpath, J.F., Parrish, F.C. and Robson, R.M. (1983) Effect of post-mortem storage on degradation of the myofibrillar protein titin in bovine longissimus muscle. Journal of Food Science 48: 17871790
Ma, R.T.-I. and Addis, P.B. (1973) The association of struggle during exsanguination to glycolysis, protein solubility and shear in turkey pectoralis muscle. Journal of Food Science 38: 995997
Macbride, M.A. and Parrish, F.C. Jr. (1977) The 30,000 dalton component of tender bovine longissimus muscle. Journal of Food Science 42: 16271629
Maeda, Y., Hayashi, M., Mizutani, M. and Hashiguchi, T. (1987a) Fractional rates of muscle protein synthesis and degradation in chickens with genetic muscular dystrophy. Poultry Science 66: 757759
Maeda, Y., Hayashi, K., Toyohara, S. and Hashiguchi, T. (1987b) Variation among chicken stocks in the fractional rates of muscle protein synthesis and degradation. Biochemical Genetics 22: 687700
Marks, H.L. (1991) Feed efficiency changes accompanying selection for body weight in chickens and quail. World's Poultry Science Journal 47: 197212
Marsh, B.B., Lochner, J.V., Takahashi, G. and Kragness, D.D. (1981) Effects of early post mortem pH and temperature on beef tenderness. Meat Science 5: 479483
Marsh, J.A., Gause, W.C., Sandhu, S. and Scanes, C.G. (1984) Enhanced growth and immune development in dwarf chickens treated with mammalian growth hormone and thyroxine. Proceedings of the Society for Experimental Biology and Medicine 175: 351360
Martonosi, A.M. (1984) Mechanisms of Ca2+ release from sarcoplasmic reticulum of skeletal muscle. Physiology Reviews 64: 12401320
Maruyama, K., Natori, K. and Nonomura, Y. (1981) New elastic protein from muscle. Nature 262: 5860
Maruyama, K., Kimura, S., Ohashi, K. and Kuwano, J. (1976) Connectin, an elastic protein of muscle. Identification of titin with connectin. Journal of Biochemistry 86: 701709
Massague, J., Cheifetz, S., Endo, T. and Nadal-Ginard, B. (1986) Type β transforming growth factor is an inhibitor of myogenic differentiation. Proceedings of the National Academy of Sciences, USA 83: 82068210
Matsukura, U., Okitani, A., Nishimuro, T. and Kato, H. (1981) Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L. Biochimica Biophysica Acta 662: 4147
McCarthy, J.C. and Siegel, P.B. (1983) A review of genetical and physiological effects of selection in meat-type poultry. Animal Breeding Abstracts 51: 8794
Mellgren, R.L. (1980) Canine cardiac calcium-dependent proteases: resolution of two forms with different requirements for calcium. FEBS Letters 109: 129133
Mellgren, R.L. (1987) Calcium dependent proteases: an enzyme system active at cellular membranes? FASEB Journal 1: 110115
Murachi, T., Tanaka, K., Hatanaka, M. and Murakami, T. (1981) Intracellular Ca2+- dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin). Aduances in Enzyme Regulation 19: 407424
Muramatsu, T., Aoyagi, Y., Okumura, J. and Tasaki, I. (1987) Contribution of whole-body protein synthesis to basal metabolism in layer and broiler chickens. British Journal of Nutrition 57: 8794
Muramatsu, T., Hiramoto, K. and Okumura, J. (1990) Strain differences in whole-body protein turnover in the chicken embryo. British Poultry Science 31: 9199
Nalbandov, A.V. and Card, L.E. (1942) Effect of hypophysectomy of growing chicks upon their basal metabolism. Proceedings of the Society for Experimental Biology and Medicine 51: 294296
Obinata, T., Maruyama, K., Sugita, H., Kohamara, K. and Ebashi, S. (1981) Dynamic aspects of structural proteins in vertebrate skeletal muscle. Muscle Nerve 4: 456488
Okitani, A., Matsukara, U., Kato, H. and Fujimaki, M. (1980) Purification and some properties of a myofibrillar protein degrading protease, cathepsin L, from rabbit skeletal muscle. Journal of Biochemistry 87: 11331143
Olson, D.G., Parrish, F.C. Jr and Stromer, M.H. (1976) Myofibril fragmentation and shear resistance of three bovine muscles during post mortem storage. Journal of Food Science 41: 10361041
Olson, D.G., Parrish, F.C. Jr, Dayton, W.R. and Goll, D.E. (1977) Effect of post mortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle. Journal of Food Science 42: 117124
Olson, E.N., Sternberg, E., Hu, H.S., Spizz, G. and Wilcox, C. (1986) Regulation of myogenic differentiation by type β transforming growth factor. Journal of Cell Biology 103: 17991805
Orcutt, M.W. and Dutson, T.R. (1985) Post-mortem degradation of gap filaments at different post-mortem pHs and temperatures. Meat Science 14: 221241
Orcutt, M.W. and Young, R.B. (1982) Cell differentiation, protein synthesis rate and protein accumulation in muscle cell cultures isolated from embryos of layer and broiler chickens. Journal of Animal Science 54: 769776
Orlowski, M. (1990) The multicatalytic proteinase complex, a major extra lysozomal proteolytic system. Biochemistry 29: 1028910297
Ou, B.R., Meyer, H.H. and Forsberg, N.E. (1991) Effects of age and castration on activities of calpains and calpastatin in sheep skeletal muscle. Journal of Animal Science 69: 19191942
Ouali, A. (1984) Sensitivity to ionic strength of Mg-Ca-enhanced ATP-ase activity as an index of myofibrillar aging in beef. Meat Science 11: 7988
Ouali, A. (1990) Meat tenderization: possible causes and mechanisms. A review. Journal of Muscle Foods 1: 251265
Ouali, A. (1992) Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie, 74: 251265
Ouali, A., Garrel, N., Obled, C., Deval, C. and Valin, C. (1987) Comparative action of cathepsins D, B, H, L and of a new lysozomal cysteine proteinase on rabbit myofibrils. Meat Science 19: 83100
Parkhouse, W.S. (1988) Regulation of skeletal muscle myofibrillar protein degradation: Relation- ships to fatigue and exercise. International Journal of Biochemistry 20: 769775
Parrish, F.C., Selvig, C.J., Culler, R.D. and Zeece, M.G. (1981) CAF activity, calcium concentration and the 30,000 dalton component of tough an tender bovine longissimus dorsi muscle. Journal of Food Science 46: 308309
Pearson, A.M. and Young, R.B. (1989) Muscle and Meat Biochemistry. Academic Press, San Diego, USA
Penny, I.F. (1974) The action of a muscle proteinase on the myofibrillar proteins of bovine muscle. Journal of the Science of food and Agiculture 25: 12731284
Penny, I.F. and Dransfield, E. (1979) Relationship between toughness and troponin T in conditioned beef. Meat Science 3: 135141
Penny, I.F. and Ferguson-Pryce, R. (1979) Measurement of autolysis in beef muscle homogenates. Meat Science 3: 121134
Penny, I.F., Etherington, D.J., Reeves, D.E. and Taylor, M.A.J. (1984) The action of cathepsin L and Ca-activated neutral proteases on myofibrillar proteins. Proceedings of the 30th European Meeting on Meat Research Work,Bristol, pp. 133–134
Petäjä, E., Kukkonen, E. and Puolanne, E. (1985) Effects of post mortem temperature on beef tenderness. Meat Science 12: 145154
Pontremoli, S., Melloni, E., Michetti, M., Salamino, F., Sparatore, B. and Horecker, B.L. (1988) An endogenous activator of the Ca2+ dependent proetinase of human neutrophils that increases its affinity for Ca2+. Proceedings of the National Academy of Sciences,USA 1740–1741
Pontremoli, S., Melloni, E., Viotti, P.L., Michetti, M., Di Lisa, F. and Siliprandi, N. (1990) Isovalerylcarnitine is a specific activator of the high calcium requiring calpain isoform. Biochemical and Biophysical Research Communications 167: 373380
Pontremoli, S., Salamino, F., Sparatore, B., Michetti, M., Sacco, O. and Melloni, E. (1985) Following association to the membrane, human erythrocyte procalpain is converted and released as fully active calpain. Biochimica Biophysica Acta 831: 335339
Prigge, J.T., Keller, D.C. and Killefer, J. (1996) Characterisation of a calpain activator in chicken pectoralis muscle. Poultry Science 75 (Supplement): 51
Reeds, P.J., Hay, S.M., Dorwood, P.M. and Palmer, R.M. (1986) Stimulation of muscle growth by clenbuterol: lack of effect on muscle protein biosynthesis. British Joural of Nutrition 56: 249258
Robson, R.M. and Huiatt, T.W. (1983) Roles of cytoskeletal proteins desmin, titin and nebulin in muscle. Proceedings of the 36th Reciprocal Meat Conference 116–124
Robson, R.M., Yamaguchi, M., Huiatt, T.W., Richardson, F.L., O'Shea, J.M., Hartzer, M.K., Rathbun, W.E., Schreiner, P.J., Kasang, L.E., Stromer, M.H., Pang, Y.Y.S., Evans, R.R. and Ridpath, J.F. (1981) Biochemistry and molecular architecture of muscle cell 10 nm filaments and Z-line: roles of desmin and α-actinin. Proceedings of the 34th Reciprocal Meat Conference 511
Rosochacki, S.J. (1985) Changes in cathepsin D activity, proteolytic activity and RNA and DNA content in the anterior and posterior latissimus dorsi muscle of the adult fowl as affected by the induced hypertrophy. Archiv für Geflügelkunde 49: 8190
Rosochacki, S.J., Grosley, B. and Keller, J.S. (1986) proteolytic activities in pectoral and leg muscles of growing chicken. Archiv für Geflügelkunde 50: 712
Samejima, K. and Wolfe, F.H. (1976) Degradation of myofibrillar protein components during post-mortem aging of chicken muscle. Journal of Food Science 41: 250254
Saunderson, C.L. and Leslie, S. (1988) Muscle growth and protein degradation during early development in chicks of fast and slow growing strains. Comparative Biochemistry and Physiology 89A: 333337
Sayre, R.N. (1970) Chicken myofibril fragmentation in relation to factors influencing tenderness. Journal of Food Science 35: 710
Scanes, C.G. (1987) The physiology of growth, growth hormone, and other growth factors in poultry. Critical Reviews in Poultry Biology 1: 51105
Scanes, C.G., Duyka, D.R., Lauterio, T.J., Bowen, S.J., Huybrechts, L.M., Bacon, W.L. and King, D.B. (1986) Effects of chicken growth hormone, triiodothyronine and hypophysectomy in growing domestic fowl. Growth 50: 1231
Schreurs, F.J.G. (1995) Post mortem processes in breast muscle of chickens with different growth rates and protein efficiencies. Proceedings of the 41st lnternational Congress on Meat Science and Technology,San Antonio, Texas, USA, pp. 41–49
Schwartz, W.N. and Bird, J.W.C. (1977) Degradation of myofibrillar proteins by cathepsins B and D. Biochemical Journal 167: 811820
Strehler, E.E., Pelloni, G., Heizmann, W. and Eppenberger, H.M. (1979) M-protein in chicken cardiac muscle. Experimental Cell Research 124: 3945
Sugita, H., Ishiura, S., Suzuki, K. and Imahori, K. (1980) Ca2+-activated neutral protease and its inhibitors: in vitro effect on intact myofibrils. Muscle Nerve 3: 335339
Suzuki, K., Imajoh, S., Kawasaki, H., Minami, Y. and Ohno, S. (1988) Regulation of activity of calcium-activated neutral protease. Advances in Enzyme Regulation 27: 153169
Suzuki, A., Sawaki, T., Hosaka, Y., Ikarashi, Y. and Nonami, Y. (1985) Post-mortem changes of connectin in chicken skeletal muscle. Meat Science 15: 7783
Taylor, R.G., Geesink, G.H., Thompson, V.F., Koohmaraie, M. and Goll, D.E. (1994) Is Z-line degradation responsible for postmortem tenderization? Journal of Animal Science 73: 13511367
Trinick, J., Knight, P. and Whiting, A. (1984) Purification and properties of native titin. Journal of Molecular Biology 180: 331356
Wallimann, T., Pelloni, G., Turner, D.C. and Eppenberger, H.M. (1978) Monovalent antibodies against MM-creatine kinase remove the M-line from myofibrils. Proceedings of the National Academy of Sciences, USA 75: 42964300
Wang, K. (1981) Nebulin, a giant protein component of N2-line of striated muscle. Journal of Cell Biology 91: 355
Wang, K., McClure, J. and Tu, A. (1979) Titin: major myofibrillar components of striated muscle. Proceedings of the National Academy of Sciences,USA 3698–3702
Wang, S.Y. and Beermann, D.H. (1988) Reduced calcium-dependent proteinase activity in cimaterol-induced muscle hypertrophy in lambs. journal of Animal Science 66: 25452550
Weber, A. (1984) Aging of bovine muscle: desmin degradation observed via enzyme linked immuno- sorbent assay. Proceedings of the 30th European Meeting on Meat Research Work,Bristol, pp. 135–136
West, B. and Zhou, B.-X. (1989) Did chickens go north? New evidence for domestication. World's Poultry Science journal 45: 205218
Wheeler, T.L. and Koohmaraie, M. (1992) Effects of the β-adrenergic agonist L644,969 on muscle protein turnover, endogenous proteinase activities, and meat tenderness in steers. journal of Animal Science 70: 30353043
Winnick, M. and Noble, A. (1966) Cellular response in rats during malnutrition at various ages. Journal of Nutrition 89: 300306
Wiskus, K.J., Addis, P.B. and Ma, R.T.-I. (1973) Post mortem changes in dark turkey muscle. Journal of Food Science 38: 313315
Wismer-Pedersen, J. and Weber, A. (1987) Immunochemischer Index für dieRindfleischreifung. Fleischwirtschaft 67: 351352, 355
Wood, L., Yorke, G., Roisen, F. and Bird, J.W.C. (1985) A low molecular weight cysteine proteinase inhibitor from chicken skeletal muscle. Progress in Clinical Biology Research 180: 8190
Young, O.A., Graafhuis, A.E. and Davey, C.L. (1980) Post mortem changes in cytoskeletal proteins of muscle. Meat Science 5: 4155
Zabari, M., Berri, M., Rouchon, P. and Ouali, A. (1991) Fractionation and characterisation of proteinase inhibitors from bovine skeletal muscle. Proceedings of the 37th International Congress on Meat Science and Technology,Kulmbach,Germany 510
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World's Poultry Science Journal
  • ISSN: 0043-9339
  • EISSN: 1743-4777
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