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Volumn 66, Issue 3, 2004, Pages 743-752

Method of isolation, rate of postmortem metabolism, and myosin heavy chain isoform composition influence ATPase activity of isolated porcine myofibrils

Author keywords

Myofibril; Myofibrillar ATPase; Myosin heavy chain

Indexed keywords

CATALYST ACTIVITY; COMPOSITION; CONFORMATIONS; ENZYME KINETICS; METABOLISM; MUSCLE; PH EFFECTS; PROTEINS; THERMAL EFFECTS;

EID: 0347622338     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2003.08.002     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0023820311 scopus 로고
    • Three myosin heavy chains in adult rat skeletal muscle
    • Bär, A., & Pette, D. (1988). Three myosin heavy chains in adult rat skeletal muscle. FEBS Letters, 235, 153-155.
    • (1988) FEBS Letters , vol.235 , pp. 153-155
    • Bär, A.1    Pette, D.2
  • 2
    • 0025857245 scopus 로고
    • Force-velocity relations and myosin heavy chain isoform composition of skinned fibres from rat skeletal muscle
    • Bottinelli, R., Schiaffino, S., & Reggiani, C. (1991). Force-velocity relations and myosin heavy chain isoform composition of skinned fibres from rat skeletal muscle. Journal of Physiology, 437, 655-672.
    • (1991) Journal of Physiology , vol.437 , pp. 655-672
    • Bottinelli, R.1    Schiaffino, S.2    Reggiani, C.3
  • 3
    • 0033467560 scopus 로고    scopus 로고
    • Effects of electrical stimulation on early postmortem pH and temperature declines in pigs from different genetic lines and halothane genotypes
    • Bowker, B. C., Wynveen, E. J., Grant, A. L., & Gerrard, D. E. (1999). Effects of electrical stimulation on early postmortem pH and temperature declines in pigs from different genetic lines and halothane genotypes. Meat Science, 53, 125-133.
    • (1999) Meat Science , vol.53 , pp. 125-133
    • Bowker, B.C.1    Wynveen, E.J.2    Grant, A.L.3    Gerrard, D.E.4
  • 4
    • 84982336440 scopus 로고
    • Biochemistry of pork muscle structure. I. Rate of anaerobic glycolysis and temperature change versus the apparent structure of muscle tissue
    • Briskey, E. J., & Wismer-Pedersen, J. (1961). Biochemistry of pork muscle structure. I. Rate of anaerobic glycolysis and temperature change versus the apparent structure of muscle tissue. Journal of Food Science, 26, 297-305.
    • (1961) Journal of Food Science , vol.26 , pp. 297-305
    • Briskey, E.J.1    Wismer-Pedersen, J.2
  • 5
    • 0020681165 scopus 로고
    • Inorganic phosphate assay with malachite green: An improvement and evaluation
    • Carter, S. G., & Karl, D. W. (1982). Inorganic phosphate assay with malachite green: an improvement and evaluation. Journal of Biochemical and Biophysical Methods, 7, 7-13.
    • (1982) Journal of Biochemical and Biophysical Methods , vol.7 , pp. 7-13
    • Carter, S.G.1    Karl, D.W.2
  • 6
    • 0037628074 scopus 로고
    • Effect of temperature and pH on physicochemical properties of sarcoplasmic proteins of pork muscle: Practical consequences
    • Charpentier, J. (1969). Effect of temperature and pH on physicochemical properties of sarcoplasmic proteins of pork muscle: practical consequences. Annales de Biologie Animale, Biochimie, Biophysique, 9, 101-110.
    • (1969) Annales de Biologie Animale, Biochimie, Biophysique , vol.9 , pp. 101-110
    • Charpentier, J.1
  • 7
    • 0036651450 scopus 로고    scopus 로고
    • Paylean alters myosin heavy chain isoform content in pig muscle
    • Depreux, F. F. S., Grant, A. L., & Gerrard, D. E. (2002). Paylean alters myosin heavy chain isoform content in pig muscle. Journal of Animal Science, 80, 1888-1894.
    • (2002) Journal of Animal Science , vol.80 , pp. 1888-1894
    • Depreux, F.F.S.1    Grant, A.L.2    Gerrard, D.E.3
  • 8
    • 0034392780 scopus 로고    scopus 로고
    • Quantification of myosin heavy chain isoform in porcine muscle using an enzymelinked immunosorbent assay
    • Depreux, F. F. S., Okamura, C. S., Swartz, D. R., Grant, A. L., Brandstetter, A. M., & Gerrard, D. E. (2000). Quantification of myosin heavy chain isoform in porcine muscle using an enzymelinked immunosorbent assay. Meat Science, 56, 261-269.
    • (2000) Meat Science , vol.56 , pp. 261-269
    • Depreux, F.F.S.1    Okamura, C.S.2    Swartz, D.R.3    Grant, A.L.4    Brandstetter, A.M.5    Gerrard, D.E.6
  • 9
    • 38249030499 scopus 로고
    • Fiber optic probe measurements in Landrace pigs of different halothane phenotypes
    • Eikelenboom, G., & Nanni Costa, L. (1988). Fiber optic probe measurements in Landrace pigs of different halothane phenotypes. Meat Science, 23, 9-19.
    • (1988) Meat Science , vol.23 , pp. 9-19
    • Eikelenboom, G.1    Nanni Costa, L.2
  • 10
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato, A. (1988). Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods in Enzymology, 157, 378-417.
    • (1988) Methods in Enzymology , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 11
    • 0037966361 scopus 로고
    • Influence of pH and temperature on solubility of muscle protein in pigs
    • Goutefongea, R. (1971). Influence of pH and temperature on solubility of muscle protein in pigs. Annales de Biologie Animale, Biochimie, Biophysique, 11, 233-244.
    • (1971) Annales de Biologie Animale, Biochimie, Biophysique , vol.11 , pp. 233-244
    • Goutefongea, R.1
  • 12
    • 84989999942 scopus 로고
    • Postmortem changes in subcellular fractions from normal and pale, soft, exudative porcine muscle. 1. Calcium accumulation and adenosine triphosphatase activities
    • Greaser, M. L., Cassens, R. G., Briskey, E. J., & Hoekstra, W. G. (1969). Postmortem changes in subcellular fractions from normal and pale, soft, exudative porcine muscle. 1. Calcium accumulation and adenosine triphosphatase activities. Journal of Food Science, 34, 120-124.
    • (1969) Journal of Food Science , vol.34 , pp. 120-124
    • Greaser, M.L.1    Cassens, R.G.2    Briskey, E.J.3    Hoekstra, W.G.4
  • 13
    • 0000210970 scopus 로고
    • Causes of the development of PSE pork
    • Honikel, K. O., & Kim, C. J. (1986). Causes of the development of PSE pork. Fleischwirtschaft, 66, 349-353.
    • (1986) Fleischwirtschaft , vol.66 , pp. 349-353
    • Honikel, K.O.1    Kim, C.J.2
  • 14
    • 0026528029 scopus 로고
    • Muscle fiber pattern is independent of cell lineage in postnatal rodent development
    • Hughes, S. M., & Blau, H. M. (1992). Muscle fiber pattern is independent of cell lineage in postnatal rodent development. Cell, 68, 659-671.
    • (1992) Cell , vol.68 , pp. 659-671
    • Hughes, S.M.1    Blau, H.M.2
  • 15
    • 0033416154 scopus 로고    scopus 로고
    • The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle
    • Joo, S. T., Kauffman, R. G., Kim, B. C., & Park, G. B. (1999). The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle. Meat Science, 52, 291-297.
    • (1999) Meat Science , vol.52 , pp. 291-297
    • Joo, S.T.1    Kauffman, R.G.2    Kim, B.C.3    Park, G.B.4
  • 18
    • 0017194944 scopus 로고
    • Histology of highly-stretched beef muscle III. Abnormal contraction patterns in ox muscle produced by overstretching during prerigor blending
    • Locker, R. H., Daines, G. J., & Leet, N. G. (1976). Histology of highly-stretched beef muscle III. Abnormal contraction patterns in ox muscle produced by overstretching during prerigor blending. Journal of Ultrastructure Research, 55, 173-181.
    • (1976) Journal of Ultrastructure Research , vol.55 , pp. 173-181
    • Locker, R.H.1    Daines, G.J.2    Leet, N.G.3
  • 22
    • 0039165779 scopus 로고    scopus 로고
    • Adaptations in muscle fiber characteristics induced by physical activity in pigs
    • Petersen, J. S., Henckel, P., & Oksbjerg, N. & Sørensen, M. T. (1998). Adaptations in muscle fiber characteristics induced by physical activity in pigs. Animal Science, 66, 733-740.
    • (1998) Animal Science , vol.66 , pp. 733-740
    • Petersen, J.S.1    Henckel, P.2    Oksbjerg, N.3    Sørensen, M.T.4
  • 23
    • 49049152727 scopus 로고
    • Fiber types in longissimus dorsi from wild and highly selected pig breeds
    • Rahelic, S., & Puac, S. (1981). Fiber types in longissimus dorsi from wild and highly selected pig breeds. Meat Science, 5, 439-450.
    • (1981) Meat Science , vol.5 , pp. 439-450
    • Rahelic, S.1    Puac, S.2
  • 26
    • 0016232706 scopus 로고
    • Studies with a reconstituted muscle glycolytic system: The rate and extent of glycolysis in simulated postmortem conditions
    • Scopes, R. K. (1974). Studies with a reconstituted muscle glycolytic system: the rate and extent of glycolysis in simulated postmortem conditions. Biochemical Journal, 142, 79-86.
    • (1974) Biochemical Journal , vol.142 , pp. 79-86
    • Scopes, R.K.1
  • 27
    • 0000614704 scopus 로고
    • Myosin ATPase and acto-heavy meromyosin ATPase in normal and in pale, soft and exudative (PSE) porcine muscle
    • Sung, S. K., Ito, T., & Izumi, K. (1981). Myosin ATPase and acto-heavy meromyosin ATPase in normal and in pale, soft and exudative (PSE) porcine muscle. Agricultural and Biological Chemistry, 45, 953-957.
    • (1981) Agricultural and Biological Chemistry , vol.45 , pp. 953-957
    • Sung, S.K.1    Ito, T.2    Izumi, K.3
  • 28
    • 43949172570 scopus 로고
    • Structural studies of rigor bovine myofibrils using fluorescence microscopy. II. Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils
    • Swartz, D. R., Greaser, M. L., & Marsh, B. B. (1993). Structural studies of rigor bovine myofibrils using fluorescence microscopy. II. Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils. Meat Science, 33, 157-190.
    • (1993) Meat Science , vol.33 , pp. 157-190
    • Swartz, D.R.1    Greaser, M.L.2    Marsh, B.B.3
  • 29
    • 0033033719 scopus 로고    scopus 로고
    • Crossbridge-dependent activation of contraction in cardiac myofibrils at low pH
    • Swartz, D. R., Zhang, D., & Yancey, K. W. (1999). Crossbridge-dependent activation of contraction in cardiac myofibrils at low pH. American Journal of Physiology, 276, H1460-H1467.
    • (1999) American Journal of Physiology , vol.276
    • Swartz, D.R.1    Zhang, D.2    Yancey, K.W.3
  • 30
    • 0031286893 scopus 로고    scopus 로고
    • Muscle protein changes postmortem in relation to pork quality traits
    • Warner, R. D., Kauffman, R. G., & Greaser, M. L. (1997). Muscle protein changes postmortem in relation to pork quality traits. Meat Science, 45, 339-352.
    • (1997) Meat Science , vol.45 , pp. 339-352
    • Warner, R.D.1    Kauffman, R.G.2    Greaser, M.L.3
  • 31
    • 21144467507 scopus 로고
    • Quality attributes of major porcine muscles: A comparison with the long-issimus lumborum
    • Warner, R. D., Kauffman, R. G., & Russell, R. L. (1993). Quality attributes of major porcine muscles: a comparison with the long-issimus lumborum. Meat Science, 33, 359-372.
    • (1993) Meat Science , vol.33 , pp. 359-372
    • Warner, R.D.1    Kauffman, R.G.2    Russell, R.L.3
  • 32
    • 0029313171 scopus 로고
    • Consequences of selection on muscle composition. A comparative study on gracilis muscle in wild and domestic pigs
    • Weiler, U., Apell, H. J., Kermser, M., Hofacker, S., & Claus, R. (1995). Consequences of selection on muscle composition. A comparative study on gracilis muscle in wild and domestic pigs. Anatomy Histology and Embryology, 24, 77-80.
    • (1995) Anatomy Histology and Embryology , vol.24 , pp. 77-80
    • Weiler, U.1    Apell, H.J.2    Kermser, M.3    Hofacker, S.4    Claus, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.