JOURNAL BROWSE
Search
Advanced SearchSearch Tips
Postmortem Proteolysis of Breast and Leg Muscles from Taiwan Colored Chickens and Silkie Bantams
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Postmortem Proteolysis of Breast and Leg Muscles from Taiwan Colored Chickens and Silkie Bantams
Tsai, Shih-Fen; Lin, Chia-Ying; Lu, Jin-Jenn; Chou, Rong-Ghi R.;
  PDF(new window)
 Abstract
Postmortem proteolysis of breast (BM) and leg (LM) muscles from Taiwan colored chickens (TCC) and silkie bantams (SB) at were compared. Myofibrils were prepared from BM and LM samples that were randomly taken from the carcasses of SB and TCC after 0, 1, 3, 7 and 14 days of storage at . pH of samples was determined, and degradation of myofibrillar proteins was analyzed by the SDS-PAGE and western blots. The results showed that pH was lower in BM than in LM samples from both avian strains. Appearance of 30 kDa components and disappearance of titin and nebulin were more rapidly as seen on SDS-PAGE in BM than in LM samples. Western blots labeled with a monoclonal antibody to desmin also demonstrated that desmin degraded more quickly in BM samples. Our data might suggest that postmortem proteolysis occurred more rapidly in BM than in LM from both TCC and SB.
 Keywords
Taiwan Colored Chickens;Silky Bantam;Postmortem Proteolysis;
 Language
English
 Cited by
 References
1.
Boehm, M. L., T. L. Kendall, V. F. Thompson and D. E. Goll. 1988. Changes in the calpains and calpastatin during postmortem storage of bovine muscle. J. Anim. Sci. 76:2415-2434

2.
Cha, S.-T., T.-F. Tseng, S.-S. Ho and R.-G. R. Chou. 2001. Comparison of postmortem proteolysis between breast and leg muscles in Chiayi native chickens. Asian-Aust. J. Anim. Sci. 15:721-724

3.
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 crossref(new window)

4.
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 crossref(new window)

5.
Farouk, M. M., J. F. Price and A. M. Salih. 1992. Postexsanguination infusion of ovine carcasses: Effect on tenderness indicators and muscle microstructure. J. Food Sci. 57:1311-1315 crossref(new window)

6.
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 crossref(new window)

7.
Hay, J. D., R. W. Currie and F. H. Wolfe. 1973. Effect of postmortem aging on chicken muscle fibrils. J. Food Sci. 38:981-987 crossref(new window)

8.
Ho, C.-Y., M. H. Stromer and R. M. Robson. 1994. Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie 76:369-375 crossref(new window)

9.
Hu, D. H., S. Kimura and K. Maruyama. 1986. Sodium dodecyl sulfate gel electrophoresis studies of connectin-like high molecular weight proteins of various types of vertebrate and invertebrate muscles. J. Biochem. 99:1485-1492

10.
Huff-Lonergan, 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

11.
Koohmaraie, K. 1992. The role of $Ca&{2+}$-dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie 74:239-245 crossref(new window)

12.
Koohmaraie, K. 1994. Muscle proteinases and meat aging. Meat Sci. 36:93-104 crossref(new window)

13.
Koohmaraie, M., S. C. Seideman, J. E. Schollmeyer, T. R. Dutson and J. D. Crouse. 1987. Effect of post-mortem storage on $Ca^{++}$- dependent proteases, their inhibitor and myofibril fragmentation. Meat Sci. 19:187-196 crossref(new window)

14.
Koohmaraie, M., S. C. Seideman, J. E. Schollmeyer, T. R. Dutson and A. S. Babiker. 1988. Factors associated with the tenderness of three bovine muscles. J. Food Sci. 53:407-410 crossref(new window)

15.
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685 crossref(new window)

16.
Locker, R. H. and D. J. Wild. 1986. A comparative study of huge molecular weight proteins in various muscles across the animal kingdom. J. Biochem. 99:1473-1484

17.
McBride, M. A. and F. C. Parrish, Jr. 1977. The 30,000-dalton component of tender bovine longissimus muscle. J. Food Sci. 42:1627-1629 crossref(new window)

18.
Moeremans, M., G. Daneels, M. De Raeymaeker, B. De Wever and J. De Mey. 1989. The use of colloidal gold particles for testing the specificity of antibodies and/or the presence of antigen. In: Immuno-Gold Labeling in Cell Biology (Ed. A. J. Verkleij and J. L. M. Leuniissen). CRC Press Inc., Boca Raton, FL, pp. 17- 27

19.
Monin, G., A. Mejenes-Quijano and A. Talmant. 1987. Influence of breed muscle metabolic type on muscle glycolytic potential and meat pH in pigs. Meat Sci. 20:149-158 crossref(new window)

20.
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

21.
Muroya, S., S. Kitamura, S. Tanabe, T. Nishimura, I. Nakajima 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 crossref(new window)

22.
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 crossref(new window)

23.
Robson, R. M., E. Huff-Lonergan, F. C. Parrish, Jr., 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. Proc. Recip. Meat Confer. 50:43-52

24.
Rose, S. P. 1997. Principles of poultry Science. CBS International, Wallingford, Oxon OX10 8DE, UK, pp. 9-30

25.
Samejima, K. and F. H. Wolfe. 1976. Degradation of myofibrillar protein components during postmortem aging of chicken muscle. J. Food Sci. 41:250-254 crossref(new window)

26.
SAS Institute Inc. 1986. User's Guide: Statistics, version 6. Edition SAS Institute Inc., Cary, NC

27.
Schreurs, F. J. G. 2000. Post-mortem changes in chicken muscle. World Poult. Sci. J. 56:319-346 crossref(new window)

28.
Sorimachi, H., A. Freiburg, B. Kolmerer, S. Ishiura, G. Stier, C. C. Gregorio, D. Labeit, W. A. Linke, S. Suzuki and S. Labeit. 1997. Tissue-specific expression and alpha-actinin binding properties of the Z-disc titin: Implications for the nature of vertebrate Z-discs. J. Mol. Biol. 270:688-695 crossref(new window)

29.
Tanabe, R., S. Muroya, I. Nakajima, K. Chikuni and H. Nakai. 1997. Skeletal muscle connectin primary structures as related to animal species and muscle type. J. Food Sci. 62:451-453, 461 crossref(new window)

30.
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

31.
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. USA. 76:4350-4354

32.
Wang, K., J. McClure and A. Tu. 1979. Titin: Major myofibrillar components of striated muscle. Proc. Natl. Acad. Sci. USA. 76:3698-3702

33.
Wang, S.-M., M. L. Greaser, E. Schultz, J. C. Bulinski, J. J.-C. Lin and J. L. Lessard. 1988. Studies on cardiac myofibrillogenesis with antibodies to titin, actin, tropomyosin, and myosin. J. Cell Biol. 107:1075-1083 crossref(new window)