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Volumn 74, Issue 7, 1996, Pages 1563-1575

Effect of Electrical Stimulation on Postmortem Titin, Nebulin, Desmin, and Troponin-T Degradation and Ultrastructural Changes in Bovine Longissimus Muscle

Author keywords

Desmin; Electrical Stimulation; Electron Microscopy; Nebulin; Titin; Troponin T

Indexed keywords

ACTININ; CONNECTIN; DESMIN; MUSCLE PROTEIN; NEBULIN; PROTEIN KINASE; TROPONIN; TROPONIN T;

EID: 0030183591     PISSN: 00218812     EISSN: None     Source Type: Journal    
DOI: 10.2527/1996.7471563x     Document Type: Article
Times cited : (106)

References (55)
  • 1
    • 0002204426 scopus 로고
    • An immunological method to assess protein degradation in post-mortem muscle
    • Bandman, E., and D. Zdanis. 1988. An immunological method to assess protein degradation in post-mortem muscle. Meat Sci. 22:1.
    • (1988) Meat Sci. , vol.22 , pp. 1
    • Bandman, E.1    Zdanis, D.2
  • 2
    • 1542743062 scopus 로고
    • Similarity in the contracture bands occurring in thaw-rigor and in other violent treatments of muscle
    • Cassens, R. G., E. J. Briskey, and W. G. Hoekstra. 1963a. Similarity in the contracture bands occurring in thaw-rigor and in other violent treatments of muscle. Biodynamica 9:165.
    • (1963) Biodynamica , vol.9 , pp. 165
    • Cassens, R.G.1    Briskey, E.J.2    Hoekstra, W.G.3
  • 3
    • 1542637891 scopus 로고
    • Electron microscopic observations of a dense, irregularly banded material occurring in some porcine muscle fibres
    • Cassens, R. G., E. J. Briskey, and W. G. Hoekstra. 1963b. Electron microscopic observations of a dense, irregularly banded material occurring in some porcine muscle fibres. Nature (Lond.) 198:1004.
    • (1963) Nature (Lond.) , vol.198 , pp. 1004
    • Cassens, R.G.1    Briskey, E.J.2    Hoekstra, W.G.3
  • 4
    • 0021291156 scopus 로고
    • Gel protein stains: Phosphoproteins
    • Cutting, J. A. 1984. Gel protein stains: Phosphoproteins. Methods Enzymol. 104:451.
    • (1984) Methods Enzymol. , vol.104 , pp. 451
    • Cutting, J.A.1
  • 5
    • 84986535324 scopus 로고
    • Studies in meat tenderness. 8. Ultra-structural changes in meat during aging
    • Davey, C. L., and M. R. Dickson. 1970. Studies in meat tenderness. 8. Ultra-structural changes in meat during aging. J. Food Sci. 35:56.
    • (1970) J. Food Sci. , vol.35 , pp. 56
    • Davey, C.L.1    Dickson, M.R.2
  • 6
    • 84985159248 scopus 로고
    • Structural changes in meat during ageing
    • Davey, C. L., and K. V. Gilbert. 1967. Structural changes in meat during ageing. J. Food Technol. 2:57.
    • (1967) J. Food Technol. , vol.2 , pp. 57
    • Davey, C.L.1    Gilbert, K.V.2
  • 7
    • 84989994459 scopus 로고
    • Studies in meat tenderness. 7. Changes in the fine structure of meat during aging
    • Davey, C. L., and K. V. Gilbert. 1969. Studies in meat tenderness. 7. Changes in the fine structure of meat during aging. J. Food Sci. 34:69.
    • (1969) J. Food Sci. , vol.34 , pp. 69
    • Davey, C.L.1    Gilbert, K.V.2
  • 8
    • 0002741564 scopus 로고
    • Modelling post-mortem tenderisation-III: Role of calpain I in conditioning
    • Dransfield, E. 1992. Modelling post-mortem tenderisation-III: Role of calpain I in conditioning. Meat Sci. 31:85.
    • (1992) Meat Sci. , vol.31 , pp. 85
    • Dransfield, E.1
  • 9
    • 0002741568 scopus 로고
    • Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef
    • Dransfield, E., D. J. Etherington, and M.A.J. Taylor. 1992. Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated beef. Meat Sci. 31:75.
    • (1992) Meat Sci. , vol.31 , pp. 75
    • Dransfield, E.1    Etherington, D.J.2    Taylor, M.A.J.3
  • 10
    • 84985294913 scopus 로고
    • Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting and immunofluorescence microscopy
    • Fritz, J. D., and M. L. Greaser. 1991. Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting and immunofluorescence microscopy. J. Food Sci. 56:607.
    • (1991) J. Food Sci. , vol.56 , pp. 607
    • Fritz, J.D.1    Greaser, M.L.2
  • 12
    • 0024402489 scopus 로고
    • Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins
    • Fritz, J. D., D. R. Swartz, and M. L. Greaser. 1989. Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins. Anal. Biochem. 180: 205.
    • (1989) Anal. Biochem. , vol.180 , pp. 205
    • Fritz, J.D.1    Swartz, D.R.2    Greaser, M.L.3
  • 13
    • 0002374681 scopus 로고
    • The tenderizing effect of electrical stimulation of beef carcasses
    • George, A. R., J. R. Bendall, and R.C.D. Jones. 1980. The tenderizing effect of electrical stimulation of beef carcasses. Meat Sci. 4:51.
    • (1980) Meat Sci. , vol.4 , pp. 51
    • George, A.R.1    Bendall, J.R.2    Jones, R.C.D.3
  • 14
    • 0025868336 scopus 로고
    • Studies of the α-actinin/actin interaction in the Z-disk by using calpain
    • Goll, D. E., W. R. Dayton, I. Singh, and R. M. Robson. 1991. Studies of the α-actinin/actin interaction in the Z-disk by using calpain. J. Biol. Chem. 266:8501.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8501
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3    Robson, R.M.4
  • 15
    • 0014783684 scopus 로고
    • A comparison of shortening and Z line degradation in post-mortem bovine, porcine, and rabbit muscle
    • Henderson, D. W., D. E. Goll, and M. H. Stromer. 1970. A comparison of shortening and Z line degradation in post-mortem bovine, porcine, and rabbit muscle. Am. J. Anat. 128:117.
    • (1970) Am. J. Anat. , vol.128 , pp. 117
    • Henderson, D.W.1    Goll, D.E.2    Stromer, M.H.3
  • 16
    • 0028126638 scopus 로고
    • Identification of the 30-kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T
    • 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.
    • (1994) Biochimie , vol.76 , pp. 369
    • Ho, C.-Y.1    Stromer, M.H.2    Robson, R.M.3
  • 17
    • 0029285632 scopus 로고
    • Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle
    • 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.
    • (1995) J. Anim. Sci. , vol.73 , pp. 1064
    • Huff-Lonergan, E.1    Parrish Jr., F.C.2    Robson, R.M.3
  • 18
    • 84987369453 scopus 로고
    • Studies of desmin and α-actinin degradation in bovine semitendinosus muscle
    • Hwan, S.-F., and E. Bandman. 1989. Studies of desmin and α-actinin degradation in bovine semitendinosus muscle. J. Food Sci. 54:1426.
    • (1989) J. Food Sci. , vol.54 , pp. 1426
    • Hwan, S.-F.1    Bandman, E.2
  • 19
    • 0001166951 scopus 로고
    • A formaldehyde-glutaraldehyde fixative of high osmolality for use in electron microscopy
    • Karnovsky, M. J. 1965. A formaldehyde-glutaraldehyde fixative of high osmolality for use in electron microscopy. J. Cell Biol. 27: 137A.
    • (1965) J. Cell Biol. , vol.27
    • Karnovsky, M.J.1
  • 20
    • 0021248179 scopus 로고
    • SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins
    • Kaufmann, E., N. Geisler, and K. Weber. 1984. SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins. FEBS Lett. 170:81.
    • (1984) FEBS Lett. , vol.170 , pp. 81
    • Kaufmann, E.1    Geisler, N.2    Weber, K.3
  • 21
    • 0027302407 scopus 로고
    • Biochemical characterization and ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin)
    • Knudson, C. M., K. K. Stang, A. O. Jorgensen, and K. P. Campbell. 1993a. Biochemical characterization and ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin). J. Biol. Chem. 268:12637.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12637
    • Knudson, C.M.1    Stang, K.K.2    Jorgensen, A.O.3    Campbell, K.P.4
  • 22
    • 0027242015 scopus 로고
    • Primary structure and topological analysis of a skeletal muscle-specific junctional sarcoplasmic reticulum glycoprotein (triadin)
    • Knudson, C. M., K. K. Stang, C. R. Moomaw, C. A. Slaughter, and K. P. Campbell. 1993b. Primary structure and topological analysis of a skeletal muscle-specific junctional sarcoplasmic reticulum glycoprotein (triadin). J. Biol. Chem. 268:12646.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12646
    • Knudson, C.M.1    Stang, K.K.2    Moomaw, C.R.3    Slaughter, C.A.4    Campbell, K.P.5
  • 23
    • 0026591107 scopus 로고
    • 2+ dependent proteases (calpains) in post mortem proteolysis and meat tenderness
    • 2+ dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie 74:239.
    • (1992) Biochimie , vol.74 , pp. 239
    • Koohmaraie, M.1
  • 24
    • 0002451154 scopus 로고
    • Effect of low-calcium-requiring calcium activated factor on myofibrils under varying pH and temperature conditions
    • Koohmaraie, M., J. E. Schollmeyer, and T. R. Dutson. 1986. Effect of low-calcium-requiring calcium activated factor on myofibrils under varying pH and temperature conditions. J. Food Sci. 51: 28.
    • (1986) J. Food Sci. , vol.51 , pp. 28
    • Koohmaraie, M.1    Schollmeyer, J.E.2    Dutson, T.R.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227: 680.
    • (1970) Nature (Lond.) , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 26
    • 0002631525 scopus 로고
    • The fate of the large proteins of the myofibril during tenderizing treatments
    • Locker, R. H., and D.J.C. Wild. 1984. The fate of the large proteins of the myofibril during tenderizing treatments. Meat Sci. 11:89.
    • (1984) Meat Sci. , vol.11 , pp. 89
    • Locker, R.H.1    Wild, D.J.C.2
  • 27
    • 84985248827 scopus 로고
    • Effect of postmortem storage on degradation of the myofibrillar protein titin in bovine Longissimus muscle
    • Lusby, M. L., J. F. Ridpath, F. C. Parrish, Jr., and R. M. Robson. 1983. Effect of postmortem storage on degradation of the myofibrillar protein titin in bovine Longissimus muscle. J. Food Sci. 48:1787.
    • (1983) J. Food Sci. , vol.48 , pp. 1787
    • Lusby, M.L.1    Ridpath, J.F.2    Parrish Jr., F.C.3    Robson, R.M.4
  • 29
    • 0003866964 scopus 로고
    • The use of colloidal gold particles for testing the specificity of antibodies and/or the presence of antigen
    • A.J.J. Verkleij and J.L.M. Leunissen (Ed.) CRC Press, Boca Raton, FL
    • 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: A.J.J. Verkleij and J.L.M. Leunissen (Ed.) Immuno-Gold Labeling in Cell Biology, p 17. CRC Press, Boca Raton, FL.
    • (1989) Immuno-Gold Labeling in Cell Biology , pp. 17
    • Moeremans, M.1    Daneels, G.2    De Raeymaeker, M.3    De Wever, B.4    De Mey, J.5
  • 30
    • 85025180875 scopus 로고
    • Meat tenderization: Possible causes and mechanisms. A review
    • Ouali, A. 1990. Meat tenderization: Possible causes and mechanisms. A review. J. Muscle Foods 1:129.
    • (1990) J. Muscle Foods , vol.1 , pp. 129
    • Ouali, A.1
  • 31
    • 84985251653 scopus 로고
    • SDS-PAGE conditions for detection of titin and nebulin in tender and tough bovine muscles
    • Paterson, B. C., and F. C. Parrish, Jr. 1987. SDS-PAGE conditions for detection of titin and nebulin in tender and tough bovine muscles. J. Food Sci. 52:509.
    • (1987) J. Food Sci. , vol.52 , pp. 509
    • Paterson, B.C.1    Parrish Jr., F.C.2
  • 32
    • 38149144384 scopus 로고
    • Effect of low voltage electrical stimulation on the distribution of cathepsin D and the palatability of Longissimus dorsi from Holstein veal calves fed a corn or barley diet
    • Pommier, S. A., L. M. Poste, and G. Butler. 1987. Effect of low voltage electrical stimulation on the distribution of cathepsin D and the palatability of Longissimus dorsi from Holstein veal calves fed a corn or barley diet. Meat Sci. 21:203.
    • (1987) Meat Sci. , vol.21 , pp. 203
    • Pommier, S.A.1    Poste, L.M.2    Butler, G.3
  • 33
    • 1542428178 scopus 로고
    • A performance and carcass evaluation of extended feeding of small-framed steers to meet the Japanese beef demand
    • (A. S. Leaflet R 813). Ames, IA
    • Reiling, B., G. Rouse, D. G. Olson, D. Duello, and D. Maxwell. 1991. A performance and carcass evaluation of extended feeding of small-framed steers to meet the Japanese beef demand. ISU Beef/Sheep Report (A. S. Leaflet R 813). p 71. Ames, IA.
    • (1991) ISU Beef/Sheep Report , pp. 71
    • Reiling, B.1    Rouse, G.2    Olson, D.G.3    Duello, D.4    Maxwell, D.5
  • 34
    • 0347136808 scopus 로고
    • Roles of the cytoskeletal proteins desmin, titin and nebulin in muscle
    • Robson, R. M., and T. W. Huiatt. 1983. Roles of the cytoskeletal proteins desmin, titin and nebulin in muscle. Proc. Recip. Meat. Conf. 36:116.
    • (1983) Proc. Recip. Meat. Conf. , vol.36 , pp. 116
    • Robson, R.M.1    Huiatt, T.W.2
  • 35
    • 0002552533 scopus 로고
    • Biochemical and structural properties of titin, nebulin and intermediate filaments in muscle
    • Robson, R. M., T. W. Huiatt, and F. C. Parrish, Jr. 1991. Biochemical and structural properties of titin, nebulin and intermediate filaments in muscle. Proc. Recip. Meat. Conf. 44:7.
    • (1991) Proc. Recip. Meat. Conf. , vol.44 , pp. 7
    • Robson, R.M.1    Huiatt, T.W.2    Parrish Jr., F.C.3
  • 38
  • 39
  • 40
    • 84987263087 scopus 로고
    • Effect of electrical stimulation on palatability of beef, lamb and goat meat
    • Savell, J. W., G. C. Smith, T. R. Dutson, Z. L. Carpenter, and D. A. Suter. 1977. Effect of electrical stimulation on palatability of beef, lamb and goat meat. J. Food Sci. 42:702.
    • (1977) J. Food Sci. , vol.42 , pp. 702
    • Savell, J.W.1    Smith, G.C.2    Dutson, T.R.3    Carpenter, Z.L.4    Suter, D.A.5
  • 42
    • 0010681302 scopus 로고
    • Accelerated processing to improve the ageing response of meat
    • F.J.M. Smulders, F. Toldrá, J. Flores, and M. Prieto (Ed.) ECCEAMST, Audet Tijdschriften B. V., Kroonstaadt, The Netherlands
    • Smulders, R.J.M., and L.J.M. van Laack. 1992. Accelerated processing to improve the ageing response of meat. In: F.J.M. Smulders, F. Toldrá, J. Flores, and M. Prieto (Ed.) New Technologies for Meat and Meat Products, p 181. ECCEAMST, Audet Tijdschriften B. V., Kroonstaadt, The Netherlands.
    • (1992) New Technologies for Meat and Meat Products , pp. 181
    • Smulders, R.J.M.1    Van Laack, L.J.M.2
  • 43
    • 0001923155 scopus 로고
    • Mechanisms of ultrastructural changes in electrically stimulated beef longissimus muscle
    • Sorinmade, S. O., H. R. Cross, K. Ono, and W. P. Wergin. 1982. Mechanisms of ultrastructural changes in electrically stimulated beef longissimus muscle. Meat Sci. 6:71.
    • (1982) Meat Sci. , vol.6 , pp. 71
    • Sorinmade, S.O.1    Cross, H.R.2    Ono, K.3    Wergin, W.P.4
  • 44
    • 0023716339 scopus 로고
    • Arrangement of desmin intermediate filaments in smooth muscle cells as shown by high-resolution immunocytochemistry
    • Stromer, M. H., and M. Bendayan. 1988. Arrangement of desmin intermediate filaments in smooth muscle cells as shown by high-resolution immunocytochemistry. Cell Motil. Cytoskel. 11: 117.
    • (1988) Cell Motil. Cytoskel. , vol.11 , pp. 117
    • Stromer, M.H.1    Bendayan, M.2
  • 46
    • 0014117637 scopus 로고
    • Morphology of rigor-shortened bovine and the effect of trypsin on pre-and postrigor myofibrils
    • Stromer, M. H., D. E. Goll, and L. E. Roth. 1967. Morphology of rigor-shortened bovine and the effect of trypsin on pre-and postrigor myofibrils. J. Cell Biol. 34:431.
    • (1967) J. Cell Biol. , vol.34 , pp. 431
    • Stromer, M.H.1    Goll, D.E.2    Roth, L.E.3
  • 47
    • 0000110891 scopus 로고
    • Effect of low-frequency electrical stimulation on beef tenderness
    • Takahashi, G., J. V. Lochner, and B. B. Marsh. 1984. Effect of low-frequency electrical stimulation on beef tenderness. Meat Sci. 11:207.
    • (1984) Meat Sci. , vol.11 , pp. 207
    • Takahashi, G.1    Lochner, J.V.2    Marsh, B.B.3
  • 48
    • 0002151477 scopus 로고
    • Effects of 2-Hz and 60-Hz electrical stimulation on the microstructure of beef
    • Takahashi, G., S.-M. Wang, J. V. Lochner, and B. B. Marsh. 1987. Effects of 2-Hz and 60-Hz electrical stimulation on the microstructure of beef. Meat Sci. 19:65.
    • (1987) Meat Sci. , vol.19 , pp. 65
    • Takahashi, G.1    Wang, S.-M.2    Lochner, J.V.3    Marsh, B.B.4
  • 49
    • 0026690389 scopus 로고
    • Calcium-induced splitting of connectin filaments into β-connectin and a 1,200-kDa subfragment
    • Takahashi, K., A. Hattori, R. Tatsumi, and K. Takai. 1992. Calcium-induced splitting of connectin filaments into β-connectin and a 1,200-kDa subfragment. J. Biochem. 111:778.
    • (1992) J. Biochem. , vol.111 , pp. 778
    • Takahashi, K.1    Hattori, A.2    Tatsumi, R.3    Takai, K.4
  • 51
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 52
    • 0026550071 scopus 로고
    • The effect of electrical stimulation on beef tenderness, protease activity and myofibrillar protein fragmentation
    • Uytterhaegen, L., E. Claeys, and D. Demeyer. 1992. The effect of electrical stimulation on beef tenderness, protease activity and myofibrillar protein fragmentation. Biochimie 74:275.
    • (1992) Biochimie , vol.74 , pp. 275
    • Uytterhaegen, L.1    Claeys, E.2    Demeyer, D.3
  • 53
    • 0028435234 scopus 로고
    • Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility
    • Uytterhaegen, L., E. Claeys, and D. Demeyer. 1994. Effects of exogenous protease effectors on beef tenderness development and myofibrillar degradation and solubility. J. Anim. Sci. 72: 1209.
    • (1994) J. Anim. Sci. , vol.72 , pp. 1209
    • Uytterhaegen, L.1    Claeys, E.2    Demeyer, D.3
  • 54
    • 0020012724 scopus 로고
    • Purification of titin and nebulin
    • Wang, K. 1982. Purification of titin and nebulin. Methods Enzymol. 85:264.
    • (1982) Methods Enzymol. , vol.85 , pp. 264
    • Wang, K.1
  • 55
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: Immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line
    • Wang, K. and J. Wright. 1988. Architecture of the sarcomere matrix of skeletal muscle: Immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol. 107:2199.
    • (1988) J. Cell Biol. , vol.107 , pp. 2199
    • Wang, K.1    Wright, J.2


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