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Volumn 69, Issue 3, 2005, Pages 479-491

Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams

Author keywords

Dry cured ham; Immunoblotting; MALDI TOF mass spectrometry; Myofibrillar proteins; Two dimensional gel electrophoresis

Indexed keywords

BIOMARKERS; CENTRIFUGATION; CURING; DESORPTION; ELECTROPHORESIS; HYDROLYSIS; MASS SPECTROMETRY; MUSCLE; PROTEINS; TISSUE;

EID: 11444259281     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2004.10.004     Document Type: Article
Times cited : (108)

References (56)
  • 1
    • 0001688050 scopus 로고
    • Isolation of flavor peptide from raw pork meat and dry cured ham
    • G. Charalambous (Ed.). Amsterdam: Elsevier Science
    • Aristoy, M.-C., & Toldrà, F. (1995). Isolation of flavor peptide from raw pork meat and dry cured ham. In G. Charalambous (Ed.), Food flavours: generation, analysis and process influence (pp. 1323-1344). Amsterdam: Elsevier Science.
    • (1995) Food Flavours: Generation, Analysis and Process Influence , pp. 1323-1344
    • Aristoy, M.-C.1    Toldrà, F.2
  • 2
    • 0001003594 scopus 로고
    • Physical and chemical changes occurring in proteins during the maturation of Parma ham. I. Biochemical and functional changes
    • Belletti, M., Dazzi, G., Chizzolini, R., Palmia, F., & Parolai, G. (1983). Physical and chemical changes occurring in proteins during the maturation of Parma ham. I. Biochemical and functional changes. Industria Conserve, 58, 143-146.
    • (1983) Industria Conserve , vol.58 , pp. 143-146
    • Belletti, M.1    Dazzi, G.2    Chizzolini, R.3    Palmia, F.4    Parolai, G.5
  • 3
    • 0027751643 scopus 로고
    • Micropreparative two-dimensional electrophoresis allowing the separation of samples containing milligram amounts of proteins
    • Bjellquist, B., Sanchez, J. C., Pasquali, C., Ravier, F., Paquet, N., Frutiger, S., et al. (1993). Micropreparative two-dimensional electrophoresis allowing the separation of samples containing milligram amounts of proteins. Electrophoresis, 14, 1375-1378.
    • (1993) Electrophoresis , vol.14 , pp. 1375-1378
    • Bjellquist, B.1    Sanchez, J.C.2    Pasquali, C.3    Ravier, F.4    Paquet, N.5    Frutiger, S.6
  • 4
    • 0033793083 scopus 로고    scopus 로고
    • Characterization of micrococcaceae isolated from salt used for Spanish dry-cured ham
    • Cordero, M. R., & Zumalacarregui, J. M. (2000). Characterization of micrococcaceae isolated from salt used for Spanish dry-cured ham. Letters in Applied Microbiology, 31(4), 303-306.
    • (2000) Letters in Applied Microbiology , vol.31 , Issue.4 , pp. 303-306
    • Cordero, M.R.1    Zumalacarregui, J.M.2
  • 7
    • 0032807732 scopus 로고    scopus 로고
    • Characterization of muscle sarcoplasmic and myofibrillar protein hydrolysis caused by Lactobacillus plantarum
    • Fadda, S., Sanz, Y., Vignolo, G., Aristoy, M., Oliver, G., & Toldrà, F. (1999a). Characterization of muscle sarcoplasmic and myofibrillar protein hydrolysis caused by Lactobacillus plantarum. Applied and Environmental Microbiology, 65(8), 3540-3546.
    • (1999) Applied and Environmental Microbiology , vol.65 , Issue.8 , pp. 3540-3546
    • Fadda, S.1    Sanz, Y.2    Vignolo, G.3    Aristoy, M.4    Oliver, G.5    Toldrà, F.6
  • 9
    • 0016156286 scopus 로고
    • The amino acid sequence of the alkali light chains of rabbit skeletal muscle myosin
    • Frank, G., & Weeds, A. G. (1974). The amino acid sequence of the alkali light chains of rabbit skeletal muscle myosin. European Journal of Biochemistry, 44, 317-334.
    • (1974) European Journal of Biochemistry , vol.44 , pp. 317-334
    • Frank, G.1    Weeds, A.G.2
  • 10
    • 11444259387 scopus 로고
    • Structural aspects of raw meat
    • D. E. Johnston, M. K. Knight, & d. A. Ledward (Eds.). Cambridge: The Royal Society of Chemistry
    • Gault, N. F. S. (1992). Structural aspects of raw meat. In D. E. Johnston, M. K. Knight, & d. A. Ledward (Eds.), Chemistry of muscle-based foods (pp. 79-105). Cambridge: The Royal Society of Chemistry.
    • (1992) Chemistry of Muscle-based Foods , pp. 79-105
    • Gault, N.F.S.1
  • 11
    • 0020627295 scopus 로고
    • Human muscle proteins: Analysis by two-dimensional electrophoresis
    • Giometti, C. S., Danon, M. J., & Anderson, N. G. (1983). Human muscle proteins: analysis by two-dimensional electrophoresis. Neurology, 33, 1152-1156.
    • (1983) Neurology , vol.33 , pp. 1152-1156
    • Giometti, C.S.1    Danon, M.J.2    Anderson, N.G.3
  • 14
    • 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, F. C., Jr., Olson, D. G., & Robson, R. M. (1996). Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. Journal of Animal Science, 74, 993-1008.
    • (1996) Journal of Animal Science , vol.74 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Beekman, D.D.3    Parrish Jr., F.C.4    Olson, D.G.5    Robson, R.M.6
  • 15
    • 0002927661 scopus 로고
    • Proteolysis of actomyosin by cathepsin B, L, 1-like and X from mackerel (Scomber australasicus)
    • Jiang, S. T., Lee, J. J., & Chen, C. S. (1992). Proteolysis of actomyosin by cathepsin B, L, 1-like and X from mackerel (Scomber australasicus). Journal of Agricultural and Food Chemistry, 44, 769-773.
    • (1992) Journal of Agricultural and Food Chemistry , vol.44 , pp. 769-773
    • Jiang, S.T.1    Lee, J.J.2    Chen, C.S.3
  • 16
    • 0000682148 scopus 로고
    • Lysosomal enzyme effect on the postmortem changes in tilapia (Tilapia nilotica x T. aurea)
    • Jiang, S. T., Wang, Y. T., & Chen, C. S. (1992). Lysosomal enzyme effect on the postmortem changes in tilapia (Tilapia nilotica x T. aurea). Journal of Agricultural and Food Chemistry, 39, 237-241.
    • (1992) Journal of Agricultural and Food Chemistry , vol.39 , pp. 237-241
    • Jiang, S.T.1    Wang, Y.T.2    Chen, C.S.3
  • 18
    • 0002349320 scopus 로고
    • Breakdown of connectin during cooking of meat
    • King, N. L. (1984). Breakdown of connectin during cooking of meat. Meat Science, 11, 27-43.
    • (1984) Meat Science , vol.11 , pp. 27-43
    • King, N.L.1
  • 19
    • 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(3), 239-245.
    • (1992) Biochimie , vol.74 , Issue.3 , pp. 239-245
    • Koohmaraie, M.1
  • 21
    • 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, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0034769635 scopus 로고    scopus 로고
    • Proteome analysis applied to meat science: Characterizing post mortem changes in porcine muscle
    • Lametsch, R., & Bendixen, E. (2001). Proteome analysis applied to meat science: characterizing post mortem changes in porcine muscle. Journal of Agricultural and Food Chemistry, 49, 4531-4537.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , pp. 4531-4537
    • Lametsch, R.1    Bendixen, E.2
  • 24
    • 84985248827 scopus 로고
    • Effect of postmortem storage on degradation of the myofibrillar protein titin in bovine longissimus muscle
    • Lusby, M. L., Ridpath, J. F., Parrish, F. C., Jr., & Robson, R. M. (1983). Effect of postmortem storage on degradation of the myofibrillar protein titin in bovine longissimus muscle. Journal of Food Science, 48, 1787-1790.
    • (1983) Journal of Food Science , vol.48 , pp. 1787-1790
    • Lusby, M.L.1    Ridpath, J.F.2    Parrish Jr., F.C.3    Robson, R.M.4
  • 25
    • 84981850662 scopus 로고
    • Free amino acids in ham muscle during successive aging periods and their relation to flavor
    • MacCain, G. R., Blumer, T. N., Craig, H. B., & Steel, R. G. (1968). Free amino acids in ham muscle during successive aging periods and their relation to flavor. Journal of Food Science, 33, 142-148.
    • (1968) Journal of Food Science , vol.33 , pp. 142-148
    • MacCain, G.R.1    Blumer, T.N.2    Craig, H.B.3    Steel, R.G.4
  • 28
    • 0000457142 scopus 로고    scopus 로고
    • Western Blotting of native and denatured bovine β-lactoglobulin to detect addition of bovine milk in cheese
    • Molina, E., Fernandez-Fournier, A., De Frutos, M., & Ramos, M. (1996). Western Blotting of native and denatured bovine β-lactoglobulin to detect addition of bovine milk in cheese. Journal of Dairy Science, 79, 191-197.
    • (1996) Journal of Dairy Science , vol.79 , pp. 191-197
    • Molina, E.1    Fernandez-Fournier, A.2    De Frutos, M.3    Ramos, M.4
  • 29
    • 0001388311 scopus 로고
    • Study of the microbial flora in dry-cured ham. II. Micrococaceae
    • Molina, I., Silla, M. H., Flores, J., & Monzò, J. L. (1989a). Study of the microbial flora in dry-cured ham. II. Micrococaceae. fieischwirtsch, 69, 1433-1434.
    • (1989) Fieischwirtsch , vol.69 , pp. 1433-1434
    • Molina, I.1    Silla, M.H.2    Flores, J.3    Monzò, J.L.4
  • 30
    • 0038962833 scopus 로고
    • Study of the microbial flora in dry-cured ham. Ill Lactic acid bacteria
    • Molina, I., Silla, M. H., Flores, J., & Monzò, J. L. (1989b). Study of the microbial flora in dry-cured ham. Ill Lactic acid bacteria. Fleischwirtsch, 69, 1709-1710.
    • (1989) Fleischwirtsch , vol.69 , pp. 1709-1710
    • Molina, I.1    Silla, M.H.2    Flores, J.3    Monzò, J.L.4
  • 31
    • 0000557245 scopus 로고
    • Detection of proteolytic activity in microrganisms isolated from dry-cured ham
    • Molina, I., & Toldrà, F. (1992). Detection of proteolytic activity in microrganisms isolated from dry-cured ham. Journal of Food Science, 57, 1308-1310.
    • (1992) Journal of Food Science , vol.57 , pp. 1308-1310
    • Molina, I.1    Toldrà, F.2
  • 32
    • 0031231909 scopus 로고    scopus 로고
    • Chemical and structural changes in dry-cured hams (Bayonne Hams) during processing and effects of the dehairing technique
    • Monin, G., Marinova, P., Talmant, A., Martin, J. F., Cornet, M., Lanore, D., et al. (1997). Chemical and structural changes in dry-cured hams (Bayonne Hams) during processing and effects of the dehairing technique. Meat Science, 47, 29-47.
    • (1997) Meat Science , vol.47 , pp. 29-47
    • Monin, G.1    Marinova, P.2    Talmant, A.3    Martin, J.F.4    Cornet, M.5    Lanore, D.6
  • 33
    • 0021252528 scopus 로고
    • Alternative transcription and two modes of splicing result in two myosin light chains from one gene
    • Nabeshima, Y., Fujii-Kuriyama, Y., Muramatsu, M., & Ogata, K. (1984). Alternative transcription and two modes of splicing result in two myosin light chains from one gene. Nature, 308, 333-338.
    • (1984) Nature , vol.308 , pp. 333-338
    • Nabeshima, Y.1    Fujii-Kuriyama, Y.2    Muramatsu, M.3    Ogata, K.4
  • 34
    • 84985046283 scopus 로고    scopus 로고
    • Effect of postmortem storage and calcium activated factor on myofibrillar proteins of bovine skeletal muscle
    • Olson, D. G., Parrish, F. G., Jr., Dayton, W. R., & Goll, D. E. (1997). Effect of postmortem storage and calcium activated factor on myofibrillar proteins of bovine skeletal muscle. Journal of Food Science, 42, 117-124.
    • (1997) Journal of Food Science , vol.42 , pp. 117-124
    • Olson, D.G.1    Parrish Jr., F.G.2    Dayton, W.R.3    Goll, D.E.4
  • 35
    • 21344494078 scopus 로고
    • Relationship between cathepsin B activity and compositional parameters in drycured hams normal and defective texture
    • Parolari, G., Virgili, R., & Schivazappa, C. (1994). Relationship between cathepsin B activity and compositional parameters in drycured hams normal and defective texture. Meat Science, 35, 117-122.
    • (1994) Meat Science , vol.35 , pp. 117-122
    • Parolari, G.1    Virgili, R.2    Schivazappa, C.3
  • 36
    • 0016116634 scopus 로고
    • The action of a muscle proteinase on the myofibrillar proteins of bovine muscle
    • Penny, I. F. (1974). The action of a muscle proteinase on the myofibrillar proteins of bovine muscle. Journal of the Science of Food and Agriculture, 25(10), 1273-1284.
    • (1974) Journal of the Science of Food and Agriculture , vol.25 , Issue.10 , pp. 1273-1284
    • Penny, I.F.1
  • 38
    • 0021679054 scopus 로고
    • Fast skeletal muscle myosin light chains 1 and 3 are produced from a single gene by combined process of differential RNA transcripton and splicing
    • Periasamy, M., Strehler, E. E., Garfinkel, L. I., Gubits, R. M., Ruiz-Opazo, N., & Nadal-Ginard, B. (1984). Fast skeletal muscle myosin light chains 1 and 3 are produced from a single gene by combined process of differential RNA transcripton and splicing. Journal of Biological Chemistry, 259(21), 13595-13604.
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.21 , pp. 13595-13604
    • Periasamy, M.1    Strehler, E.E.2    Garfinkel, L.I.3    Gubits, R.M.4    Ruiz-Opazo, N.5    Nadal-Ginard, B.6
  • 39
    • 0025293138 scopus 로고
    • Human skeletal muscle myosin light chains analyzed by immobilized pH gradients during ontogenesis: Identification of new phosphorylatable isoforms of light chain 2
    • Pernelle, J. J., Righetti, P. G., Wahrmann, J. P., & Herve, B. (1990). Human skeletal muscle myosin light chains analyzed by immobilized pH gradients during ontogenesis: identification of new phosphorylatable isoforms of light chain 2. Electrophoresis, 11(4), 325-332.
    • (1990) Electrophoresis , vol.11 , Issue.4 , pp. 325-332
    • Pernelle, J.J.1    Righetti, P.G.2    Wahrmann, J.P.3    Herve, B.4
  • 43
    • 0036010115 scopus 로고    scopus 로고
    • Investigation of candidate genes for meat quality in dry-cured ham production: The porcine cathepsin B (CTSB) and cystatin B (CSTB) genes
    • Russo, V., Fontanesi, L., Davoli, R., Nanni Costa, L., Cagnazzo, M., Buttazzoni, L., et al. (2002). Investigation of candidate genes for meat quality in dry-cured ham production: the porcine cathepsin B (CTSB) and cystatin B (CSTB) genes. Animal Genetics, 33, 123-131.
    • (2002) Animal Genetics , vol.33 , pp. 123-131
    • Russo, V.1    Fontanesi, L.2    Davoli, R.3    Nanni Costa, L.4    Cagnazzo, M.5    Buttazzoni, L.6
  • 46
    • 0024465908 scopus 로고
    • Identification of the functional promoter regions in the human gene encoding the myosin alkali light chains MLC1 and MLC3 of fast skeletal muscle
    • Seidel, U., & Arnold, H. H. (1989). Identification of the functional promoter regions in the human gene encoding the myosin alkali light chains MLC1 and MLC3 of fast skeletal muscle. Journal of Biological Chemistry, 264, 16109-16117.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 16109-16117
    • Seidel, U.1    Arnold, H.H.2
  • 47
    • 18144441911 scopus 로고
    • The complete nucleotide sequences of cDNA clones coding for human myosin light chains 1 and 3
    • Seidel, U., Bober, E., Winter, B., Lenz, S., Lohse, P., & Arnold, H. H. (1987). The complete nucleotide sequences of cDNA clones coding for human myosin light chains 1 and 3. Nucleic Acids Research, 15, 4989.
    • (1987) Nucleic Acids Research , vol.15 , pp. 4989
    • Seidel, U.1    Bober, E.2    Winter, B.3    Lenz, S.4    Lohse, P.5    Arnold, H.H.6
  • 48
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., & Mann, M. (1996). Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Analytical Chemistry, 68, 850-858.
    • (1996) Analytical Chemistry , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 51
    • 0032064706 scopus 로고    scopus 로고
    • The role of muscle proteases and lipases in flavor development during the processing of dry-cured ham
    • Toldrà, F., & Flores, M. (1998). The role of muscle proteases and lipases in flavor development during the processing of dry-cured ham. Critical Reviews in Food Science and Nutrition, 38(4), 331-352.
    • (1998) Critical Reviews in Food Science and Nutrition , vol.38 , Issue.4 , pp. 331-352
    • Toldrà, F.1    Flores, M.2
  • 52
    • 41149153921 scopus 로고
    • Examination of cathepsins B,D,H and L activities in dry-cured hams
    • Toldrà, F., & Etherington, D. J. (1988). Examination of cathepsins B,D,H and L activities in dry-cured hams. Meat Science, 23, 1-7.
    • (1988) Meat Science , vol.23 , pp. 1-7
    • Toldrà, F.1    Etherington, D.J.2
  • 53
    • 0030964937 scopus 로고    scopus 로고
    • Dry-cured ham flavour: Enzymatic generation and process influence
    • Toldrà, F., Flores, M., & Sanz, Y. (1997). Dry-cured ham flavour: enzymatic generation and process influence. Food Chemistry, 59, 523-530.
    • (1997) Food Chemistry , vol.59 , pp. 523-530
    • Toldrà, F.1    Flores, M.2    Sanz, Y.3
  • 55
    • 0026825122 scopus 로고
    • Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis
    • Whipple, G., & Koohmaraie, M. (1992). Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis. Journal of Animal Science, 70(3), 798-804.
    • (1992) Journal of Animal Science , vol.70 , Issue.3 , pp. 798-804
    • Whipple, G.1    Koohmaraie, M.2
  • 56
    • 0035294573 scopus 로고    scopus 로고
    • Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Yan, J. X., Harry, R. A., Wait, R., Welson, S. Y., Emery, P. W., Preedy, V. R., et al. (2001). Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics, 1(3), 424-434.
    • (2001) Proteomics , vol.1 , Issue.3 , pp. 424-434
    • Yan, J.X.1    Harry, R.A.2    Wait, R.3    Welson, S.Y.4    Emery, P.W.5    Preedy, V.R.6


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