메뉴 건너뛰기




Volumn 153, Issue 7, 2002, Pages 499-506

Factors and mechanisms responsible for meat ageing;Facteurs et mécanismes responsables de la maturation de la viande

Author keywords

Calcium; Calpains; Cathepsins; Endopeptidases; Meat; Proteasome

Indexed keywords

CALCIUM ION; CALPAIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN H; CATHEPSIN L; INTERSTITIAL COLLAGENASE; MUSCLE PROTEIN; PROTEASOME; PROTEINASE;

EID: 18844480192     PISSN: 00351555     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (64)
  • 1
    • 21844489490 scopus 로고
    • Action of cathepsin B on intramuscular collagen under conditions simulating conventional aging of meat a calorimetric study
    • Beltrán J.A., Galán J., Jaime I. and Roncalés P.: Action of cathepsin B on intramuscular collagen under conditions simulating conventional aging of meat a calorimetric study. Sci. Aliments, 1994, 14, 523-528.
    • (1994) Sci. Aliments , vol.14 , pp. 523-528
    • Beltrán, J.A.1    Galán, J.2    Jaime, I.3    Roncalés, P.4
  • 2
    • 0002175969 scopus 로고    scopus 로고
    • Comparison of proteolytic enzyme levels in chicken, pig, lamb and rabbit muscle at point of slaughter: Role in meat tenderisation post-mortem
    • Blanchard P.J. and Mantle D.: Comparison of proteolytic enzyme levels in chicken, pig, lamb and rabbit muscle at point of slaughter: role in meat tenderisation post-mortem. J. Sci. Food Agric., 1996, 71, 83-91.
    • (1996) J. Sci. Food Agric. , vol.71 , pp. 83-91
    • Blanchard, P.J.1    Mantle, D.2
  • 3
    • 0000068721 scopus 로고
    • Relationships among calcium-dependent protease, cathepsins B and H, meat tenderness and the response of muscle to aging
    • Calkins C.R. and Seideman S.C.: Relationships among calcium-dependent protease, cathepsins B and H, meat tenderness and the response of muscle to aging. J. Animal Sci., 1988, 66, 1186-1193.
    • (1988) J. Animal Sci. , vol.66 , pp. 1186-1193
    • Calkins, C.R.1    Seideman, S.C.2
  • 4
    • 21844497901 scopus 로고
    • Lysosomal integrity in post mortem bovine skeletal muscle
    • Chambers J.J., Reville W.J. and Zeece M.G.: Lysosomal integrity in post mortem bovine skeletal muscle. Sci. Aliments, 1994, 14, 441-457.
    • (1994) Sci. Aliments , vol.14 , pp. 441-457
    • Chambers, J.J.1    Reville, W.J.2    Zeece, M.G.3
  • 5
    • 0031615188 scopus 로고    scopus 로고
    • Measurement of nitric oxide and the effect of enhancing or inhibiting it on tenderness changes of meat
    • Cook C.J., Scott S.M. and Devine C.E.: Measurement of nitric oxide and the effect of enhancing or inhibiting it on tenderness changes of meat. Meat Sci., 1998, 48, 85-89.
    • (1998) Meat Sci. , vol.48 , pp. 85-89
    • Cook, C.J.1    Scott, S.M.2    Devine, C.E.3
  • 7
    • 0023655258 scopus 로고
    • Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes
    • Davies K.J. and Goldberg A.L.: Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes. J. Biol. Chem., 1987, 262, 8220-8226.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8220-8226
    • Davies, K.J.1    Goldberg, A.L.2
  • 8
    • 0000327645 scopus 로고
    • Quantifying changes in tenderness during storage of beef
    • Dransfield E., Jones R.C. and MacFie H. J.: Quantifying changes in tenderness during storage of beef. Meat Sci., 1981, 5, 131-137.
    • (1981) Meat Sci. , vol.5 , pp. 131-137
    • Dransfield, E.1    Jones, R.C.2    MacFie, H.J.3
  • 9
    • 49149135249 scopus 로고
    • Tenderising in M. longissimus dorsi of beef, veal, rabbit, lamb and pork
    • Dransfield E., Jones R.C. and MacFie H.J.: Tenderising in M. longissimus dorsi of beef, veal, rabbit, lamb and pork. Meat Sci., 1981, 5, 139-147.
    • (1981) Meat Sci. , vol.5 , pp. 139-147
    • Dransfield, E.1    Jones, R.C.2    MacFie, H.J.3
  • 11
    • 0002741564 scopus 로고
    • Modelling post-mortem tenderisation: III. Role of calpain I in conditioning
    • Dransfield E.: Modelling post-mortem tenderisation: III. Role of calpain I in conditioning. Meat Sci., 1992, 31, 85-94.
    • (1992) Meat Sci. , vol.31 , pp. 85-94
    • Dransfield, E.1
  • 12
    • 0001383470 scopus 로고
    • Optimisation of tenderisation, ageing and tenderness
    • Dransfield E.: Optimisation of tenderisation, ageing and tenderness. Meat Sci., 1994, 36, 105-121.
    • (1994) Meat Sci. , vol.36 , pp. 105-121
    • Dransfield, E.1
  • 13
    • 0001906486 scopus 로고
    • Conditioning of meat from different species: Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase
    • Etherington D.J., Taylor M.A. and Dransfield E.: Conditioning of meat from different species: relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase. Meat Sci., 1987, 20, 1-18.
    • (1987) Meat Sci. , vol.20 , pp. 1-18
    • Etherington, D.J.1    Taylor, M.A.2    Dransfield, E.3
  • 14
    • 0002563814 scopus 로고
    • Proteinase (cathepsin B, D, L and calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle
    • Etherington D.J., Taylor M.A., Wakefield D.K., Cousins A. and Dransfield E.: Proteinase (cathepsin B, D, L and calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle. Meat Sci., 1990, 28, 99-109.
    • (1990) Meat Sci. , vol.28 , pp. 99-109
    • Etherington, D.J.1    Taylor, M.A.2    Wakefield, D.K.3    Cousins, A.4    Dransfield, E.5
  • 17
    • 0018313994 scopus 로고
    • Studies on the post-mortem fragmentation of myofibrils
    • Hattori A. and Takahashi K.: Studies on the post-mortem fragmentation of myofibrils. J. Biochem., 1979, 85, 47-56.
    • (1979) J. Biochem. , vol.85 , pp. 47-56
    • Hattori, A.1    Takahashi, K.2
  • 19
    • 0029285632 scopus 로고
    • Effect of post-mortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle
    • Huff-Lonergan E., Parrish Jr. and Robson R.M.: Effect of post-mortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle. J. Animal Sci., 1995, 73, 1064-1073.
    • (1995) J. Animal Sci. , vol.73 , pp. 1064-1073
    • Huff-Lonergan, E.1    Parrish, Jr.2    Robson, R.M.3
  • 20
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle
    • Huff-Lonergan E., Mitsuhashi T., Beekman D.D., Parrish Jr. F.C., Olson D.J. and Robson R.M.: Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J. Animal Sci., 1996, 59, 993-1008.
    • (1996) J. Animal Sci. , vol.59 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Beekman, D.D.3    Parrish F.C., Jr.4    Olson, D.J.5    Robson, R.M.6
  • 21
    • 0025469157 scopus 로고
    • Differences in cathepsin B + L and calcium-dependent protease activities among breed type and their relationship to beef tenderness
    • Johnson M.H., Calkins C.R., Huffman R.D., Johnson D.D. and Hargrove D.D.: Differences in cathepsin B + L and calcium-dependent protease activities among breed type and their relationship to beef tenderness. J. Animal Sci., 1990, 68, 2371-2379.
    • (1990) J. Animal Sci. , vol.68 , pp. 2371-2379
    • Johnson, M.H.1    Calkins, C.R.2    Huffman, R.D.3    Johnson, D.D.4    Hargrove, D.D.5
  • 22
    • 43949154597 scopus 로고
    • Oxidative processes in meat and meat products: Quality implications
    • Kanner J.: Oxidative processes in meat and meat products: quality implications. Meat Sci., 1994, 36, 169-189.
    • (1994) Meat Sci. , vol.36 , pp. 169-189
    • Kanner, J.1
  • 26
    • 0001619142 scopus 로고
    • Inhibition of postmortem tenderization in ovine carcasses through infusion of zinc
    • Koohmaraie M.: Inhibition of postmortem tenderization in ovine carcasses through infusion of zinc. J. Animal Sci., 1990, 68, 1476-1483.
    • (1990) J. Animal Sci. , vol.68 , pp. 1476-1483
    • Koohmaraie, M.1
  • 27
    • 0002514983 scopus 로고
    • Muscle proteinases and meat aging
    • Koohmaraie M.: Muscle proteinases and meat aging. Meat Sci., 1994, 1-2, 93-104.
    • (1994) Meat Sci. , vol.1-2 , pp. 93-104
    • Koohmaraie, M.1
  • 28
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S. and Kolmerer B.: Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science, 1995, 270, 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 29
    • 0002640005 scopus 로고    scopus 로고
    • The conversion of muscle to meat
    • Woodhead Publishing Limited, Cambridge
    • Lawrie R.A.: The conversion of muscle to meat. In: Lawrie's Meat Science, Woodhead Publishing Limited, Cambridge, 1998, 96-118.
    • (1998) Lawrie's Meat Science , pp. 96-118
    • Lawrie, R.A.1
  • 31
    • 0001375225 scopus 로고    scopus 로고
    • Comparison of oxidative processes on myofibrillar proteins from beef during maturation and by different model oxidation systems
    • Martinaud A., Mercier Y., Marinova P., Tassy C., Gatellier P. and Renerre M.: Comparison of oxidative processes on myofibrillar proteins from beef during maturation and by different model oxidation systems. J. Agricultural Food Chem., 1997, 45, 2481-2487.
    • (1997) J. Agricultural Food Chem. , vol.45 , pp. 2481-2487
    • Martinaud, A.1    Mercier, Y.2    Marinova, P.3    Tassy, C.4    Gatellier, P.5    Renerre, M.6
  • 32
  • 33
    • 0031286043 scopus 로고    scopus 로고
    • Proteasome from rabbit skeletal muscle: Some properties and effects on muscle proteins
    • Matsuishi M. and Okitani A.: Proteasome from rabbit skeletal muscle: some properties and effects on muscle proteins. Meat Sci., 1997, 45, 451-462.
    • (1997) Meat Sci. , vol.45 , pp. 451-462
    • Matsuishi, M.1    Okitani, A.2
  • 34
    • 0030306557 scopus 로고    scopus 로고
    • Relationship between degradation of proteoglycans and weakening of the intramuscular connective tissue during post-mortem ageing of beef
    • Nishimura T., Hattori A. and Takahashi K.: Relationship between degradation of proteoglycans and weakening of the intramuscular connective tissue during post-mortem ageing of beef. Meat Sci., 1996, 42, 251-260.
    • (1996) Meat Sci. , vol.42 , pp. 251-260
    • Nishimura, T.1    Hattori, A.2    Takahashi, K.3
  • 35
    • 0031992372 scopus 로고    scopus 로고
    • Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef
    • Nishimura T., Liu A., Hattori A. and Takahashi K.: Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef. J. Animal Sci., 1998, 76, 528-532.
    • (1998) J. Animal Sci. , vol.76 , pp. 528-532
    • Nishimura, T.1    Liu, A.2    Hattori, A.3    Takahashi, K.4
  • 36
    • 0032219241 scopus 로고    scopus 로고
    • Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure
    • Otsuka Y., Homma N., Shiga K., Ushiki J., Ikeuchi Y. and Suzuki A.: Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure. Meat Sci., 1998, 49, 365-378.
    • (1998) Meat Sci. , vol.49 , pp. 365-378
    • Otsuka, Y.1    Homma, N.2    Shiga, K.3    Ushiki, J.4    Ikeuchi, Y.5    Suzuki, A.6
  • 37
    • 85025180875 scopus 로고
    • Meat tenderization: Possible causes and mechanisms. A review
    • Ouali A.: Meat tenderization: possible causes and mechanisms. A review. J. Muscle Foods, 1990, 1, 129-165.
    • (1990) J. Muscle Foods , vol.1 , pp. 129-165
    • Ouali, A.1
  • 38
    • 0026539218 scopus 로고
    • Proteolytic and physicochemical mechanisms involved in meat texture development
    • Ouali A.: Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie, 1992, 74, 251-265.
    • (1992) Biochimie , vol.74 , pp. 251-265
    • Ouali, A.1
  • 39
    • 0035545437 scopus 로고    scopus 로고
    • Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes
    • Prates J.A.M., Ribeiro A.M.R. and Correia A.A.D.: Role of cysteine endopeptidases (EC 3.4.22) in rabbit meat tenderisation and some related changes. Meat Sci., 2001, 57, 283-290.
    • (2001) Meat Sci. , vol.57 , pp. 283-290
    • Prates, J.A.M.1    Ribeiro, A.M.R.2    Correia, A.A.D.3
  • 40
    • 0036019634 scopus 로고    scopus 로고
    • Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing
    • Prates J.A.M., Costa F.J.S., Ribeiro A.M.R. and Correia A.A.D.: Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing. Meat Sci., 2002, 61, 103-113.
    • (2002) Meat Sci. , vol.61 , pp. 103-113
    • Prates, J.A.M.1    Costa, F.J.S.2    Ribeiro, A.M.R.3    Correia, A.A.D.4
  • 41
    • 0002416979 scopus 로고
    • Myofibrillar and cytoskeletal structures and proteins in mature skeletal muscle cells
    • A. Ouali, D.I. Demeyer, F.J. Smulders (Eds.), ECCEAMST, Utrecht
    • Robson R.M.: Myofibrillar and cytoskeletal structures and proteins in mature skeletal muscle cells. In : A. Ouali, D.I. Demeyer, F.J. Smulders (Eds.): Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality, ECCEAMST, Utrecht, 1995, 311-332.
    • (1995) Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality , pp. 311-332
    • Robson, R.M.1
  • 43
    • 38149143277 scopus 로고
    • The effect of acidification on myofibrillar proteins
    • Saunders A.B.: The effect of acidification on myofibrillar proteins. Meat Sci., 1994, 37, 271-280.
    • (1994) Meat Sci. , vol.37 , pp. 271-280
    • Saunders, A.B.1
  • 44
    • 0032061666 scopus 로고    scopus 로고
    • Liberation of phospholipids from Z-disks of chicken skeletal muscle myofibrils by 0.1 mM calcium ions: Weakening mechanism for Z-disks during post-mortem aging of meat
    • Shimada K., Ahn D.H. and Takahashi K.: Liberation of phospholipids from Z-disks of chicken skeletal muscle myofibrils by 0.1 mM calcium ions: weakening mechanism for Z-disks during post-mortem aging of meat. Biosci., Biotechn. and Biochem., 1998, 62, 919-926.
    • (1998) Biosci., Biotechn. and Biochem. , vol.62 , pp. 919-926
    • Shimada, K.1    Ahn, D.H.2    Takahashi, K.3
  • 45
    • 0025674536 scopus 로고
    • Metal ion-catalysed oxidation of proteins: Biochemical mechanism and biological consequences
    • Stadtman E.R.: Metal ion-catalysed oxidation of proteins: biochemical mechanism and biological consequences. Free Radical Biol. Med., 1990, 8, 315-325.
    • (1990) Free Radical Biol. Med. , vol.8 , pp. 315-325
    • Stadtman, E.R.1
  • 46
    • 0026607643 scopus 로고
    • Non-enzymatic weakening of myofibrillar structures during conditioning of meat: Calcium ions at 0.1 mM and their effect on meat tenderization
    • Takahashi K.: Non-enzymatic weakening of myofibrillar structures during conditioning of meat: calcium ions at 0.1 mM and their effect on meat tenderization. Biochimie, 1992, 74, 247-250.
    • (1992) Biochimie , vol.74 , pp. 247-250
    • Takahashi, K.1
  • 47
    • 0026690389 scopus 로고
    • Calcium-induced splitting of connectin filaments into β-connectin and a 1,200-kDa subfragment
    • Takahashi K., Hattori A., Tatsumi R. and Takai K.: Calcium-induced splitting of connectin filaments into β-connectin and a 1,200-kDa subfragment. J. Biochem., 1992, 111, 778-782.
    • (1992) J. Biochem. , vol.111 , pp. 778-782
    • Takahashi, K.1    Hattori, A.2    Tatsumi, R.3    Takai, K.4
  • 48
    • 58149365129 scopus 로고
    • Relationship between the translocation of paratropomyosin and the restoration of rigor-shortened sarcomeres during post-mortem ageing of meat: A molecular mechanism of meat tenderization
    • Takahashi K., Hattori A. and Kuroyanagi H.: Relationship between the translocation of paratropomyosin and the restoration of rigor-shortened sarcomeres during post-mortem ageing of meat: a molecular mechanism of meat tenderization. Meat Sci., 1995, 40, 413-423.
    • (1995) Meat Sci. , vol.40 , pp. 413-423
    • Takahashi, K.1    Hattori, A.2    Kuroyanagi, H.3
  • 49
    • 0030305246 scopus 로고    scopus 로고
    • Structural weakening of skeletal muscle tissue during post-mortem ageing of meat: The non-enzymatic mechanism of meat tenderization
    • Takahashi K.: Structural weakening of skeletal muscle tissue during post-mortem ageing of meat: the non-enzymatic mechanism of meat tenderization. Meat Sci., 1996, 43S, S67-S80.
    • (1996) Meat Sci. , vol.43 S
    • Takahashi, K.1
  • 50
    • 0028066754 scopus 로고
    • Purification and characterization of the 1,200-kDa subfragment of connectin filaments produced by 0.1 mM calcium ions
    • Tanabe R., Tatsumi R. and Takahashi K.: Purification and characterization of the 1,200-kDa subfragment of connectin filaments produced by 0.1 mM calcium ions. J. Biochem., 1994, 115, 351-355.
    • (1994) J. Biochem. , vol.115 , pp. 351-355
    • Tanabe, R.1    Tatsumi, R.2    Takahashi, K.3
  • 51
    • 1842330885 scopus 로고    scopus 로고
    • Skeletal muscle connectin primary structures as related to animal species and muscle type
    • Tanabe R., Muroya S., Nakajima I., Chikuni K. and Nakai H.: Skeletal muscle connectin primary structures as related to animal species and muscle type. J. Food Sci., 1997, 62, 451-453 and 461.
    • (1997) J. Food Sci. , vol.62 , pp. 451-453
    • Tanabe, R.1    Muroya, S.2    Nakajima, I.3    Chikuni, K.4    Nakai, H.5
  • 52
    • 0027055107 scopus 로고
    • Calcium-induced fragmentation of skeletal muscle nebulin filaments
    • Tatsumi R. and Takahashi K.: Calcium-induced fragmentation of skeletal muscle nebulin filaments. J. Biochem., 1992, 112, 775-779.
    • (1992) J. Biochem. , vol.112 , pp. 775-779
    • Tatsumi, R.1    Takahashi, K.2
  • 56
    • 0005161318 scopus 로고
    • Use of exogenous protease effectors to investigate postmortem tenderness development and related myofibrillar protein fragmentation: A review
    • A. Ouali, D.I. Demeyer, F.J. Smulders (Eds.), ECCEAMST, Utrecht
    • Uytterhaegen L., Claeys E. and Demeyer D.I.: Use of exogenous protease effectors to investigate postmortem tenderness development and related myofibrillar protein fragmentation: a review. In: A. Ouali, D.I. Demeyer, F.J. Smulders (Eds.): Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality, ECCEAMST, Utrecht, 1995, 333-346.
    • (1995) Expression of Tissue Proteinases and Regulation of Protein Degradation as Related to Meat Quality , pp. 333-346
    • Uytterhaegen, L.1    Claeys, E.2    Demeyer, D.I.3
  • 57
    • 0001862015 scopus 로고
    • Proteolytic muscle enzymes and post mortem meat tenderization
    • F.J. Smulders, F. Toldrá, J. Flores and M. Prieto (Eds.), Audet Tijdschriften B.V., Nijmegen
    • Valin C. and Ouali A.: Proteolytic muscle enzymes and post mortem meat tenderization. In: F.J. Smulders, F. Toldrá, J. Flores and M. Prieto (Eds.): New Technologies for Meat and Meat Products: Part II. Muscle Enzymology and Meat Ageing, Audet Tijdschriften B.V., Nijmegen, 1992, 163-179.
    • (1992) New Technologies for Meat and Meat Products: Part II. Muscle Enzymology and Meat Ageing , pp. 163-179
    • Valin, C.1    Ouali, A.2
  • 59
    • 0025485110 scopus 로고
    • Evaluation of attributes that affect longissimus muscle tenderness in bos taurus and bos indicus cattle
    • Whipple G., Koohmaraie M., Dikeman M.E., Crouse J.D., Hunt M.C. and Klemm R.D.: Evaluation of attributes that affect longissimus muscle tenderness in bos taurus and bos indicus cattle. J. Animal Sci., 1990, 68, 2716-2728.
    • (1990) J. Animal Sci. , vol.68 , pp. 2716-2728
    • Whipple, G.1    Koohmaraie, M.2    Dikeman, M.E.3    Crouse, J.D.4    Hunt, M.C.5    Klemm, R.D.6
  • 60
    • 0026248168 scopus 로고
    • Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride
    • Whipple G. and Koohmaraie M.: Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. Meat Sci., 1991, 69, 4449-4460.
    • (1991) Meat Sci. , vol.69 , pp. 4449-4460
    • Whipple, G.1    Koohmaraie, M.2
  • 61
    • 0000479874 scopus 로고
    • Osmotic properties of post-rigor beef muscle
    • Winger R.J. and Pope C.G.: Osmotic properties of post-rigor beef muscle. Meat Sci., 1981, 5, 355-369.
    • (1981) Meat Sci. , vol.5 , pp. 355-369
    • Winger, R.J.1    Pope, C.G.2
  • 62
    • 0023392333 scopus 로고
    • Ionic strenght and myofibrillar protein solubilization
    • Wu F.Y. and Smith S.B.: Ionic strenght and myofibrillar protein solubilization. J. Animal Sci., 1987, 65, 597-608.
    • (1987) J. Animal Sci. , vol.65 , pp. 597-608
    • Wu, F.Y.1    Smith, S.B.2
  • 63
    • 0024005733 scopus 로고
    • Effect of tropomyosin on the increase in sarcomere length of rigor-shortened skeletal muscles
    • Yamanoue M. and Takahashi K.: Effect of tropomyosin on the increase in sarcomere length of rigor-shortened skeletal muscles. J. Biochem., 1988, 103, 843-847.
    • (1988) J. Biochem. , vol.103 , pp. 843-847
    • Yamanoue, M.1    Takahashi, K.2
  • 64
    • 0030176663 scopus 로고    scopus 로고
    • Predicting variability of ageing and toughness in beef M. longissimus lumborum et thoracis
    • Zamora F., Debiton E., Lepetit J., Lebert A., Dransfield E. and Ouali A.: Predicting variability of ageing and toughness in beef M. longissimus lumborum et thoracis. Meat Sci., 1996, 43, 321-333.
    • (1996) Meat Sci. , vol.43 , pp. 321-333
    • Zamora, F.1    Debiton, E.2    Lepetit, J.3    Lebert, A.4    Dransfield, E.5    Ouali, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.