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Volumn 79, Issue 1, 2000, Pages 105-109

Denaturation of myofibrillar proteins from chicken as affected by pH, temperature, and adenosine triphosphate concentration

Author keywords

Exudative; Pale; Poultry; Protein denaturation; Soft

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHELATING AGENT; EGTAZIC ACID; MUSCLE PROTEIN;

EID: 0033629370     PISSN: 00325791     EISSN: None     Source Type: Journal    
DOI: 10.1093/ps/79.1.105     Document Type: Article
Times cited : (32)

References (25)
  • 1
    • 0001968155 scopus 로고
    • Poultry muscle as a food
    • P. J. Bechtel, ed. Academic Press, Inc., Orlando, FL
    • Addis, P. B., 1986. Poultry muscle as a food. Pages 372-401 in: Muscle as a Food. P. J. Bechtel, ed. Academic Press, Inc., Orlando, FL.
    • (1986) Muscle as a Food , pp. 372-401
    • Addis, P.B.1
  • 2
    • 0032221681 scopus 로고    scopus 로고
    • Estimating the magnitude of the PSE problem in poultry
    • Barbut, S., 1998. Estimating the magnitude of the PSE problem in poultry. J. Muscle Foods 9:35-50.
    • (1998) J. Muscle Foods , vol.9 , pp. 35-50
    • Barbut, S.1
  • 3
    • 45549117556 scopus 로고
    • A review of the relationships of pH with physical aspects of pork quality
    • Bendall, J. R., and H. J. Swatland, 1988. A review of the relationships of pH with physical aspects of pork quality. Meat Sci. 24:85-126.
    • (1988) Meat Sci. , vol.24 , pp. 85-126
    • Bendall, J.R.1    Swatland, H.J.2
  • 5
    • 0017688620 scopus 로고
    • Polymorphism of myosin among skeletal muscle fiber types
    • Gauthier, G. F., and S. Lowey, 1977. Polymorphism of myosin among skeletal muscle fiber types. J. Cell Biol. 74:760-779.
    • (1977) J. Cell Biol. , vol.74 , pp. 760-779
    • Gauthier, G.F.1    Lowey, S.2
  • 6
    • 0018382366 scopus 로고
    • Distribution of myosin isoenzymes among skeletal muscle fiber types
    • Gauthier, G. F., and S. Lowey, 1979. Distribution of myosin isoenzymes among skeletal muscle fiber types. J. Cell Biol. 81:10-25.
    • (1979) J. Cell Biol. , vol.81 , pp. 10-25
    • Gauthier, G.F.1    Lowey, S.2
  • 7
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall, A. G., C. J. Bardawill, and M. D. Maxima, 1949. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    Maxima, M.D.3
  • 8
    • 0015544147 scopus 로고
    • Temperature sensitivity of myosin and actomyosin
    • Jacobson, A. L., and J. Henderson, 1973. Temperature sensitivity of myosin and actomyosin. Can. J. Biochem. 51:71-86.
    • (1973) Can. J. Biochem. , vol.51 , pp. 71-86
    • Jacobson, A.L.1    Henderson, J.2
  • 9
    • 84986531978 scopus 로고
    • Effects of pre- and post-mortem glycolysis on poultry tenderness
    • Khan, A. W., and R. Nakamura, 1970. Effects of pre-and post-mortem glycolysis on poultry tenderness. J. Food Sci. 35:266-267.
    • (1970) J. Food Sci. , vol.35 , pp. 266-267
    • Khan, A.W.1    Nakamura, R.2
  • 10
    • 84991184569 scopus 로고
    • Biochemical and technological characteristics of hot chicken meat
    • Kijowski, J. A., A. Niewiarowicz, and B. Kujawska-Biernat, 1982. Biochemical and technological characteristics of hot chicken meat. J. Food Technol. 17:553-560.
    • (1982) J. Food Technol. , vol.17 , pp. 553-560
    • Kijowski, J.A.1    Niewiarowicz, A.2    Kujawska-Biernat, B.3
  • 11
    • 0001636246 scopus 로고
    • The association of struggle during exsanguination to glycolysis, protein solubility and shear in turkey pectoralis muscle
    • Ma, R. T., and P. B. Addis, 1973. The association of struggle during exsanguination to glycolysis, protein solubility and shear in turkey pectoralis muscle. J. Food Sci. 38:995-997.
    • (1973) J. Food Sci. , vol.38 , pp. 995-997
    • Ma, R.T.1    Addis, P.B.2
  • 12
    • 84987306158 scopus 로고
    • Response to electrical stimulation and post-mortem changes in turkey pectoralis muscle
    • Ma, R. T., P. B. Addis, and E. Allen, 1971. Response to electrical stimulation and post-mortem changes in turkey pectoralis muscle. J. Food Sci. 36:125-129.
    • (1971) J. Food Sci. , vol.36 , pp. 125-129
    • Ma, R.T.1    Addis, P.B.2    Allen, E.3
  • 13
    • 0027439382 scopus 로고
    • The evolutionary relationship of avian and mammalian myoson heavy-chain genes
    • Moore, L. A., W. E. Tidyman, M. J. Arricubieta, and E. Bandman, 1993. The evolutionary relationship of avian and mammalian myoson heavy-chain genes. J. Mol. Evol. 36:21-30.
    • (1993) J. Mol. Evol. , vol.36 , pp. 21-30
    • Moore, L.A.1    Tidyman, W.E.2    Arricubieta, M.J.3    Bandman, E.4
  • 14
    • 44949286385 scopus 로고
    • Modelling of the formation of pale, soft, exudative meat: Effects of chilling regime and rate and extent of glycolysis
    • Offer, G., 1991. Modelling of the formation of pale, soft, exudative meat: Effects of chilling regime and rate and extent of glycolysis. Meat Sci. 30:157-184.
    • (1991) Meat Sci. , vol.30 , pp. 157-184
    • Offer, G.1
  • 15
    • 0002878025 scopus 로고
    • The structural basis of water holding in meat
    • R. A. Lawrie, ed. Elsevier Applied Science, London, United Kingdom
    • Offer, G., and P. Knight, 1988. The structural basis of water holding in meat. Pages 63-243 in: Developments in Meat Science - 4. R. A. Lawrie, ed. Elsevier Applied Science, London, United Kingdom.
    • (1988) Developments in Meat Science - 4 , pp. 63-243
    • Offer, G.1    Knight, P.2
  • 17
    • 0014117619 scopus 로고
    • The influence of pH and temperature on the properties of myosin
    • Penny, I. F., 1967a. The influence of pH and temperature on the properties of myosin. Biochem. J. 104:609-615.
    • (1967) Biochem. J. , vol.104 , pp. 609-615
    • Penny, I.F.1
  • 18
    • 84995188386 scopus 로고
    • The effect of post-mortem conditions on the extractability and adenosine triphosphatase activity of myofibrillar proteins of rabbit muscle
    • Penny, I. F., 1967b. The effect of post-mortem conditions on the extractability and adenosine triphosphatase activity of myofibrillar proteins of rabbit muscle. J. Food Technol. 2:325-338.
    • (1967) J. Food Technol. , vol.2 , pp. 325-338
    • Penny, I.F.1
  • 21
    • 0004155427 scopus 로고
    • W.H. Freeman and Company, New York, NY
    • Stryer, L., 1988. Biochemistry. 3rd ed. W.H. Freeman and Company, New York, NY.
    • (1988) Biochemistry. 3rd Ed.
    • Stryer, L.1
  • 22
    • 0042886240 scopus 로고    scopus 로고
    • Overview of atypical poultry meat in relation to PSE pork from a global level
    • New Orleans, LA, Abstract 2-1
    • Vimini, R. J., 1996. Overview of atypical poultry meat in relation to PSE pork from a global level. IFT 1996 Annu. Mtg., New Orleans, LA, Abstract 2-1.
    • (1996) IFT 1996 Annu. Mtg.
    • Vimini, R.J.1
  • 23
    • 84987290994 scopus 로고
    • Changes in protein solubility and gelation properties of chicken myofibrils during storage
    • Xiong, Y. L., and C. J. Brekke, 1989. Changes in protein solubility and gelation properties of chicken myofibrils during storage. J. Food Sci. 54:1141-1146.
    • (1989) J. Food Sci. , vol.54 , pp. 1141-1146
    • Xiong, Y.L.1    Brekke, C.J.2
  • 24
    • 0001481513 scopus 로고
    • Thermal denaturation of muscle proteins from different species and muscle types as studied by differential scanning calorimetry
    • Xiong, Y. L., C. J. Brekke, and H. K. Leung, 1987. Thermal denaturation of muscle proteins from different species and muscle types as studied by differential scanning calorimetry. Can. Inst. Food Sci. J. 20:357-362.
    • (1987) Can. Inst. Food Sci. J. , vol.20 , pp. 357-362
    • Xiong, Y.L.1    Brekke, C.J.2    Leung, H.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.