Hostname: page-component-586b7cd67f-g8jcs Total loading time: 0 Render date: 2024-11-28T03:05:39.844Z Has data issue: false hasContentIssue false
  • English
  • Français

Post-mortem changes in chicken muscle

Published online by Cambridge University Press:  18 September 2007

F.J.G. Schreurs
F.J.G. Schreurs*
Affiliation:
Institute for Animal Science and Health, P O Box 65, 8200 AB Lelystad, The Netherlands
*
*Deceased. All correspondence should be addressed to T.G. Uijttenboogaart, Institute for Animal Science and Health, PO Box 65, 8200 AB Lelystad, The Netherlands ([email protected])
Get access

Abstract

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.

Keywords

Ageingmeat qualityproteolysisproteolytic enzymesrigor mortis
Type
Research Article
Information
World's Poultry Science Journal , Volume 56 , Issue 4 , December 2000 , pp. 319 - 346
Copyright
Copyright © Cambridge University Press 2000

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

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: 1210–1212CrossRefGoogle Scholar
Addis, P.B. (1986) Poultry muscle as food. In: Muscle as Food (Bechtel, P.J., Ed.), Academic Press, London, pp. 371–407CrossRefGoogle Scholar
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: 567–572CrossRefGoogle ScholarPubMed
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: 343–451Google Scholar
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: 2217–2224Google Scholar
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: 1931–1940Google Scholar
Ashmore, C.R. and Doerr, L. (1971a) Comparative aspects of muscle fiber types in different species. Experimental Neurology 30: 408–418CrossRefGoogle Scholar
Ashmore, C.R. and Doerr, L. (1971b) Postnatal development of fiber types in normal and dystrophic skeletal muscle of the chick. Experimental Neurology 31: 431–446CrossRefGoogle Scholar
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: 339–347CrossRefGoogle Scholar
Ballard, R., Bardsley, R.G. and Buttery, P.J. (1988) Changes in the activity of skeletal muscle calcium-activated neutral proteinase (EC 3.4.22.17) and its specific inhibitor in chickens grown at different rates in response to graded levels of dietary protein. British Journal of Nutrition 59: 141–147CrossRefGoogle ScholarPubMed
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: 267–273CrossRefGoogle ScholarPubMed
Barrett, A.J. (1985) The cystatins: small protein inhibitors of cysteine proteinases. Progress in Clinical Biological Research 180: 105–116Google ScholarPubMed
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: E822–827Google ScholarPubMed
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: 269–275Google Scholar
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: 20–25Google Scholar
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: 439–446CrossRefGoogle ScholarPubMed
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: 602–607CrossRefGoogle Scholar
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: 137–142CrossRefGoogle Scholar
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: 367–381CrossRefGoogle ScholarPubMed
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. 88–102Google Scholar
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. 109–117Google Scholar
Carfoli, E. (1982b) The transport of Ca2+ by mitochondria. In: Menbranes and Transport, Volume I (Martonosi, A., Ed.), Plenum Press, New York, pp. 611–616Google Scholar
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: 555–563CrossRefGoogle Scholar
Cogburn, L.A. (1991) Endocrine manipulation of body composition in broiler chickens. Critical Reviews in Poultry Biology 3: 283–305Google Scholar
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: 11627–11630CrossRefGoogle ScholarPubMed
Davey, C.L. and Dickson, M.A. (1970) Studies in meat tenderness. 8. Ultrastructural changes in meat during aging. Journal of Food Science 35: 56–60CrossRefGoogle Scholar
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. 69–90Google Scholar
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. 551–577Google Scholar
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: 2150–2158CrossRefGoogle ScholarPubMed
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: 2159–2167CrossRefGoogle ScholarPubMed
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: 216–230CrossRefGoogle Scholar
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: 48–61CrossRefGoogle ScholarPubMed
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. 205–212Google Scholar
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: 12047–12052CrossRefGoogle ScholarPubMed
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: 625–632CrossRefGoogle Scholar
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: 223–245CrossRefGoogle Scholar
Fiskum, G. and Lehninger, A. (1980) The mechanisms and regulation of mitochondria1 Ca2+ transport. Federation Proceedings 39: 2432–2436Google Scholar
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: 16509–16513CrossRefGoogle Scholar
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: 3313–3321CrossRefGoogle ScholarPubMed
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: 607–610, 615CrossRefGoogle Scholar
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: 606–610CrossRefGoogle Scholar
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: 464–468CrossRefGoogle Scholar
Gann, G.L. and Merkel, R.A. (1978) Ultrastructural changes in bovine longissimus dorsi muscle during post-mortem aging. Meat Science 2: 129–144CrossRefGoogle Scholar
Gibson, W.R. and Nalbandov, A.V. (1966) Lipid mobilisation in obese hypophysectomized cockerels. American Journal of Physiology 211: 1345–1351CrossRefGoogle ScholarPubMed
Goldspink, D.F. (1991) Exercise-related changes in protein turnover in mammalian striated muscle. Journal of Experimental Biology 160: 127–148CrossRefGoogle ScholarPubMed
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. 141–182Google Scholar
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: 549–555CrossRefGoogle ScholarPubMed
Granger, B.I. and Lazarides, E. (1979) Desmin and vimentin coexist at the periphery of the myofibril z-disk. Cell 18: 1053–1063CrossRefGoogle Scholar
Granger, B.I. and Lazarides, E. (1980) Synemin, a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell 22: 727–738CrossRefGoogle ScholarPubMed
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: 19–28CrossRefGoogle ScholarPubMed
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: 1551–1558CrossRefGoogle ScholarPubMed
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: 477–484CrossRefGoogle ScholarPubMed
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: 987–990CrossRefGoogle Scholar
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: 981–986CrossRefGoogle Scholar
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: 157–163CrossRefGoogle Scholar
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: 117–135CrossRefGoogle Scholar
Hershko, A., Mamont, P., Shields, R. and Tomkins, G.M. (1971) Pleiotypic response. Nature 232: 206–211Google ScholarPubMed
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 3.4.22.17) and calpastatin activities in lambs. BritishJournal of Nutrition 60: 645–652Google Scholar
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: 391–399CrossRefGoogle ScholarPubMed
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: 145–152CrossRefGoogle ScholarPubMed
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: 2116–2122CrossRefGoogle Scholar
Huxley, H. and Hanson, J. (1954) Changes in the cross striations of muscle during contraction and stretch and their structural interpretation. Nature 173: 973–976CrossRefGoogle ScholarPubMed
Ioanescu, V., Zellweger, H. and Conway, T.W. (1971) Ribosomal protein synthesis in Duchenne muscular dystrophy. Archives of Biochemistry and Biophysics 144: 5158Google Scholar
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: 245–253CrossRefGoogle Scholar
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: 269–278CrossRefGoogle ScholarPubMed
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: 579–581Google ScholarPubMed
Johnson, R.J. (1989) Growth physiology and biotechnology: potential to improve broiler production. World's Poultry Science Journal 46: 228–240CrossRefGoogle Scholar
Kar, N.C. and Pearson, C.M. (1976) A calcium activated neutral protease in normal and dystrophic human muscle. Clinica Chimica Acta 73: 293–297CrossRefGoogle ScholarPubMed
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. 49Google Scholar
Kiessling, K.H. (1977) Muscle structure and function in the goose, quail, pheasant, guinea hen and chicken. Comparative Biochemistry and Physiology 578: 287–292Google Scholar
Koohmaraie, M. (1988) The role of endogenous proteases in meat tenderness. Proceedings of the 41st Reciprocal Meat Conference 89–100Google Scholar
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: 1253–1257CrossRefGoogle Scholar
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: 290–291CrossRefGoogle Scholar
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: 292–293CrossRefGoogle Scholar
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: 28–32, 65CrossRefGoogle Scholar
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: 228–235CrossRefGoogle Scholar
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: 1760–1772CrossRefGoogle Scholar
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: 393–401CrossRefGoogle Scholar
Lawrie, R.E. (1966) Chemical and biochemical constituents of muscle. In: Meat Science (Lawrie, R.E., Ed.), Pergamon Press, London, pp. 66–113Google Scholar
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 4344–4348CrossRefGoogle Scholar
Lehmann, K.B. (1907) Studies of the causes of toughness in meat. Archiv für Hygiene 63: 134–179Google Scholar
Lepetit, J., Sale, P. and Ouali, A. (1986) Post. mortem evolution of rheological properties of the myofibrillar structure. Meat Science 16: 161–174CrossRefGoogle ScholarPubMed
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: 1961–1695CrossRefGoogle ScholarPubMed
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: 691–704CrossRefGoogle ScholarPubMed
Lochner, J.V., Kauffman, R.G. and Marsh, B.B. (1980) Early post mortem cooling rate and beef tenderness. Meat Science 4: 227–241CrossRefGoogle ScholarPubMed
Locker, R.H. (1987) The non-sliding filaments of the sarcomere. Meat Science 20: 217–236CrossRefGoogle ScholarPubMed
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: 64–75CrossRefGoogle ScholarPubMed
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: 157–172CrossRefGoogle Scholar
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: 31–38CrossRefGoogle Scholar
Locker, R.H. and Wild, D.J.C. (1984a) The N-lines of skeletal muscle. Journal of Ultrastructure Research 88: 207–222CrossRefGoogle ScholarPubMed
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: 207–233CrossRefGoogle Scholar
Locker, R.H. and Wild, D.J.C. (1984c) The fate of the large proteins of the myofibril during tenderising treatments. Meat Science 11: 89–108CrossRefGoogle ScholarPubMed
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: 1787–1790CrossRefGoogle Scholar
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: 995–997CrossRefGoogle Scholar
Macbride, M.A. and Parrish, F.C. Jr. (1977) The 30,000 dalton component of tender bovine longissimus muscle. Journal of Food Science 42: 1627–1629CrossRefGoogle Scholar
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: 757–759CrossRefGoogle ScholarPubMed
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: 687–700CrossRefGoogle Scholar
Marks, H.L. (1991) Feed efficiency changes accompanying selection for body weight in chickens and quail. World's Poultry Science Journal 47: 197–212CrossRefGoogle Scholar
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: 479–483CrossRefGoogle ScholarPubMed
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: 351–360CrossRefGoogle ScholarPubMed
Martonosi, A.M. (1984) Mechanisms of Ca2+ release from sarcoplasmic reticulum of skeletal muscle. Physiology Reviews 64: 1240–1320CrossRefGoogle ScholarPubMed
Maruyama, K., Natori, K. and Nonomura, Y. (1981) New elastic protein from muscle. Nature 262: 58–60CrossRefGoogle Scholar
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: 701–709Google Scholar
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: 8206–8210CrossRefGoogle ScholarPubMed
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: 41–47CrossRefGoogle ScholarPubMed
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: 87–94Google Scholar
Mellgren, R.L. (1980) Canine cardiac calcium-dependent proteases: resolution of two forms with different requirements for calcium. FEBS Letters 109: 129–133CrossRefGoogle ScholarPubMed
Mellgren, R.L. (1987) Calcium dependent proteases: an enzyme system active at cellular membranes? FASEB Journal 1: 110–115CrossRefGoogle ScholarPubMed
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: 407–424CrossRefGoogle Scholar
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: 87–94CrossRefGoogle ScholarPubMed
Muramatsu, T., Hiramoto, K. and Okumura, J. (1990) Strain differences in whole-body protein turnover in the chicken embryo. British Poultry Science 31: 91–99CrossRefGoogle ScholarPubMed
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: 294–296CrossRefGoogle Scholar
Obinata, T., Maruyama, K., Sugita, H., Kohamara, K. and Ebashi, S. (1981) Dynamic aspects of structural proteins in vertebrate skeletal muscle. Muscle Nerve 4: 456–488CrossRefGoogle ScholarPubMed
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: 1133–1143Google ScholarPubMed
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: 1036–1041CrossRefGoogle Scholar
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: 117–124CrossRefGoogle Scholar
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: 1799–1805CrossRefGoogle ScholarPubMed
Orcutt, M.W. and Dutson, T.R. (1985) Post-mortem degradation of gap filaments at different post-mortem pHs and temperatures. Meat Science 14: 221–241CrossRefGoogle ScholarPubMed
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: 769–776CrossRefGoogle ScholarPubMed
Orlowski, M. (1990) The multicatalytic proteinase complex, a major extra lysozomal proteolytic system. Biochemistry 29: 10289–10297CrossRefGoogle Scholar
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: 1919–1942CrossRefGoogle ScholarPubMed
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: 79–88CrossRefGoogle Scholar
Ouali, A. (1990) Meat tenderization: possible causes and mechanisms. A review. Journal of Muscle Foods 1: 251–265CrossRefGoogle Scholar
Ouali, A. (1992) Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie, 74: 251–265Google ScholarPubMed
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: 83–100CrossRefGoogle Scholar
Parkhouse, W.S. (1988) Regulation of skeletal muscle myofibrillar protein degradation: Relation- ships to fatigue and exercise. International Journal of Biochemistry 20: 769–775CrossRefGoogle Scholar
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: 308–309CrossRefGoogle Scholar
Pearson, A.M. and Young, R.B. (1989) Muscle and Meat Biochemistry. Academic Press, San Diego, USAGoogle Scholar
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: 1273–1284CrossRefGoogle ScholarPubMed
Penny, I.F. and Dransfield, E. (1979) Relationship between toughness and troponin T in conditioned beef. Meat Science 3: 135–141CrossRefGoogle ScholarPubMed
Penny, I.F. and Ferguson-Pryce, R. (1979) Measurement of autolysis in beef muscle homogenates. Meat Science 3: 121–134CrossRefGoogle ScholarPubMed
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. 133–134Google Scholar
Petäjä, E., Kukkonen, E. and Puolanne, E. (1985) Effects of post mortem temperature on beef tenderness. Meat Science 12: 145–154CrossRefGoogle ScholarPubMed
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 1740–1741CrossRefGoogle Scholar
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: 373–380CrossRefGoogle Scholar
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: 335–339CrossRefGoogle Scholar
Prigge, J.T., Keller, D.C. and Killefer, J. (1996) Characterisation of a calpain activator in chicken pectoralis muscle. Poultry Science 75 (Supplement): 51Google Scholar
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: 249–258CrossRefGoogle ScholarPubMed
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 116–124Google Scholar
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 511Google Scholar
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: 81–90Google Scholar
Rosochacki, S.J., Grosley, B. and Keller, J.S. (1986) proteolytic activities in pectoral and leg muscles of growing chicken. Archiv für Geflügelkunde 50: 7–12Google Scholar
Samejima, K. and Wolfe, F.H. (1976) Degradation of myofibrillar protein components during post-mortem aging of chicken muscle. Journal of Food Science 41: 250–254CrossRefGoogle Scholar
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: 333–337CrossRefGoogle Scholar
Sayre, R.N. (1970) Chicken myofibril fragmentation in relation to factors influencing tenderness. Journal of Food Science 35: 7–10CrossRefGoogle Scholar
Scanes, C.G. (1987) The physiology of growth, growth hormone, and other growth factors in poultry. Critical Reviews in Poultry Biology 1: 51–105Google Scholar
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: 12–31Google ScholarPubMed
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. 41–49Google Scholar
Schwartz, W.N. and Bird, J.W.C. (1977) Degradation of myofibrillar proteins by cathepsins B and D. Biochemical Journal 167: 811–820CrossRefGoogle ScholarPubMed
Strehler, E.E., Pelloni, G., Heizmann, W. and Eppenberger, H.M. (1979) M-protein in chicken cardiac muscle. Experimental Cell Research 124: 39–45CrossRefGoogle ScholarPubMed
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: 335–339CrossRefGoogle Scholar
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: 153–169CrossRefGoogle ScholarPubMed
Suzuki, A., Sawaki, T., Hosaka, Y., Ikarashi, Y. and Nonami, Y. (1985) Post-mortem changes of connectin in chicken skeletal muscle. Meat Science 15: 77–83CrossRefGoogle ScholarPubMed
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: 1351–1367CrossRefGoogle Scholar
Trinick, J., Knight, P. and Whiting, A. (1984) Purification and properties of native titin. Journal of Molecular Biology 180: 331–356CrossRefGoogle ScholarPubMed
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: 4296–4300CrossRefGoogle ScholarPubMed
Wang, K. (1981) Nebulin, a giant protein component of N2-line of striated muscle. Journal of Cell Biology 91: 355Google Scholar
Wang, K., McClure, J. and Tu, A. (1979) Titin: major myofibrillar components of striated muscle. Proceedings of the National Academy of Sciences,USA 3698–3702CrossRefGoogle Scholar
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: 2545–2550CrossRefGoogle ScholarPubMed
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. 135–136Google Scholar
West, B. and Zhou, B.-X. (1989) Did chickens go north? New evidence for domestication. World's Poultry Science journal 45: 205–218CrossRefGoogle Scholar
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: 3035–3043CrossRefGoogle ScholarPubMed
Winnick, M. and Noble, A. (1966) Cellular response in rats during malnutrition at various ages. Journal of Nutrition 89: 300–306CrossRefGoogle Scholar
Wiskus, K.J., Addis, P.B. and Ma, R.T.-I. (1973) Post mortem changes in dark turkey muscle. Journal of Food Science 38: 313–315CrossRefGoogle Scholar
Wismer-Pedersen, J. and Weber, A. (1987) Immunochemischer Index für dieRindfleischreifung. Fleischwirtschaft 67: 351–352, 355Google Scholar
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: 81–90Google ScholarPubMed
Young, O.A., Graafhuis, A.E. and Davey, C.L. (1980) Post mortem changes in cytoskeletal proteins of muscle. Meat Science 5: 41–55CrossRefGoogle ScholarPubMed
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 510Google Scholar