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Volumn 12, Issue 18, 2012, Pages 2879-2889

Myosin light chain isoforms retain their species-specific electrophoretic mobility after processing, which enables differentiation between six species: 2DE analysis of minced meat and meat products made from beef, pork and poultry

Author keywords

Animal proteomics; Meat products; Myosin light chains; Skeletal muscles; Species differentiation

Indexed keywords

MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN 1 FAST; MYOSIN LIGHT CHAIN 2 FAST; MYOSIN LIGHT CHAIN 3 FAST; UNCLASSIFIED DRUG;

EID: 84866146153     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201200043     Document Type: Article
Times cited : (41)

References (37)
  • 1
    • 0242523052 scopus 로고    scopus 로고
    • Postmortem proteome changes of porcine muscle related to tenderness
    • Lametsch, R., Karlsson, A., Rosenvold, K., Andersen, H. J. et al., Postmortem proteome changes of porcine muscle related to tenderness. J. Agric. Food Chem. 2003, 51, 6992-6997.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 6992-6997
    • Lametsch, R.1    Karlsson, A.2    Rosenvold, K.3    Andersen, H.J.4
  • 2
    • 1842584567 scopus 로고    scopus 로고
    • Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures
    • Morzel, M., Chambon, C., Hamelin, M., Sante-Lhoutellier, V. et al., Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures. Meat Sci. 2004, 67, 689-696.
    • (2004) Meat Sci , vol.67 , pp. 689-696
    • Morzel, M.1    Chambon, C.2    Hamelin, M.3    Sante-Lhoutellier, V.4
  • 3
    • 5744228466 scopus 로고    scopus 로고
    • Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus
    • Hwang, I. H., Park, B. Y., Kim, J. H., Cho, S. H. et al., Assessment of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus. Meat Sci. 2005, 69, 79-91.
    • (2005) Meat Sci , vol.69 , pp. 79-91
    • Hwang, I.H.1    Park, B.Y.2    Kim, J.H.3    Cho, S.H.4
  • 4
    • 32944454622 scopus 로고    scopus 로고
    • Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis
    • Jia, X., Hollung, K., Therkildsen, M., Hildrum, K. I. et al., Proteome analysis of early post-mortem changes in two bovine muscle types: M. longissimus dorsi and M. semitendinosis. Proteomics 2006, 6, 936-944.
    • (2006) Proteomics , vol.6 , pp. 936-944
    • Jia, X.1    Hollung, K.2    Therkildsen, M.3    Hildrum, K.I.4
  • 5
    • 72449156073 scopus 로고    scopus 로고
    • Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization
    • Laville, E., Sayd, T., Morzel, M., Blinet, S. et al., Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization. J. Agric. Food Chem. 2009, 57, 10755-10764.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 10755-10764
    • Laville, E.1    Sayd, T.2    Morzel, M.3    Blinet, S.4
  • 6
    • 0031287829 scopus 로고    scopus 로고
    • Proteolysis in dry fermented sausages: the effect of selected exogenous proteases
    • Díaz, O., Fernandez, M., De Fernando, G. D., de la Hoz, L. et al., Proteolysis in dry fermented sausages: the effect of selected exogenous proteases. Meat Sci. 1997, 46, 115-128.
    • (1997) Meat Sci , vol.46 , pp. 115-128
    • Díaz, O.1    Fernandez, M.2    De Fernando, G.D.3    de la Hoz, L.4
  • 7
    • 0030903775 scopus 로고    scopus 로고
    • The importance of meat enzymes in ripening and flavour generation in dry fermented sausages. First results of a European project
    • Molly, K., Demeyer, D., Johansson, G., Raemaekers, M. et al., The importance of meat enzymes in ripening and flavour generation in dry fermented sausages. First results of a European project. Food Chem. 1997, 59, 539-545.
    • (1997) Food Chem , vol.59 , pp. 539-545
    • Molly, K.1    Demeyer, D.2    Johansson, G.3    Raemaekers, M.4
  • 8
    • 0036823125 scopus 로고    scopus 로고
    • Characterization of proteolysis during the ripening of semi-dry fermented sausages
    • Hughes, M. C., Kerry, J. P., Arendt, E. K., Kenneally, P. M. et al., Characterization of proteolysis during the ripening of semi-dry fermented sausages. Meat Sci. 2002, 62, 205-216.
    • (2002) Meat Sci , vol.62 , pp. 205-216
    • Hughes, M.C.1    Kerry, J.P.2    Arendt, E.K.3    Kenneally, P.M.4
  • 9
    • 67349194036 scopus 로고    scopus 로고
    • Effect of starter culture on proteolytic changes during processing of fermented beef sausages
    • Candogan, K., Wardlaw, F. B., Acton, J. C., Effect of starter culture on proteolytic changes during processing of fermented beef sausages. Food Chem. 2009, 116, 731-737.
    • (2009) Food Chem , vol.116 , pp. 731-737
    • Candogan, K.1    Wardlaw, F.B.2    Acton, J.C.3
  • 10
    • 11444259281 scopus 로고    scopus 로고
    • Proteomic analysis of water soluble and myofibrillar protein changes occuring in dry-cured hams
    • Di Luccia, A., Picariello, G., Cacace, G., Scaloni, A. et al., Proteomic analysis of water soluble and myofibrillar protein changes occuring in dry-cured hams. Meat Sci. 2005, 69, 479-491.
    • (2005) Meat Sci. , vol.69 , pp. 479-491
    • Di Luccia, A.1    Picariello, G.2    Cacace, G.3    Scaloni, A.4
  • 12
    • 79955046274 scopus 로고    scopus 로고
    • Proteomic profile of dry-cured ham relative to PRKAG3 or CAST genotype, level of salt and pastiness
    • Šklerp, M., Čandek-Potokar, M., Mandelc, S., Javornik, B. et al., Proteomic profile of dry-cured ham relative to PRKAG3 or CAST genotype, level of salt and pastiness. Meat Sci. 2011, 88, 657-667.
    • (2011) Meat Sci , vol.88 , pp. 657-667
    • Šklerp, M.1    Čandek-Potokar, M.2    Mandelc, S.3    Javornik, B.4
  • 13
    • 65349114821 scopus 로고    scopus 로고
    • Naturally generated small peptides derived from myofibrillar proteins in Serrano dry-cured ham
    • Mora, L., Sentandreu, M. A., Koistinen, K. M., Fraser, P. D. et al., Naturally generated small peptides derived from myofibrillar proteins in Serrano dry-cured ham. J. Agric. Food Chem. 2009, 57, 3228-3234.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 3228-3234
    • Mora, L.1    Sentandreu, M.A.2    Koistinen, K.M.3    Fraser, P.D.4
  • 14
    • 79955018206 scopus 로고    scopus 로고
    • Intense degradation of myosin light chain isoforms in Spanish dry-cured ham
    • Mora, L., Sentandreu, M. A., Toldra, F., Intense degradation of myosin light chain isoforms in Spanish dry-cured ham. J. Agric. Food Chem. 2011, 59, 3884-3892.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 3884-3892
    • Mora, L.1    Sentandreu, M.A.2    Toldra, F.3
  • 15
    • 79959765265 scopus 로고    scopus 로고
    • Using 2-DE for the differentiation of local chicken breeds
    • Zanetti, E., Molette, C., Chambon, C., Pinguet, J. et al., Using 2-DE for the differentiation of local chicken breeds. Proteomics 2011, 11, 2613-2619.
    • (2011) Proteomics , vol.11 , pp. 2613-2619
    • Zanetti, E.1    Molette, C.2    Chambon, C.3    Pinguet, J.4
  • 16
    • 68849113107 scopus 로고    scopus 로고
    • Differential expression of the skeletal muscle proteome in grazed cattle
    • Shibata, M., Matsumoto, K., Oe, M., Ohnishi-Kameyama, M. et al., Differential expression of the skeletal muscle proteome in grazed cattle. J. Anim. Sci. 2009, 87, 2700-2708.
    • (2009) J. Anim. Sci. , vol.87 , pp. 2700-2708
    • Shibata, M.1    Matsumoto, K.2    Oe, M.3    Ohnishi-Kameyama, M.4
  • 17
    • 35648966498 scopus 로고    scopus 로고
    • Effect of fiber type on postmortem proteolysis in longissimus muscle of Landrace and Korean native black pigs
    • Park, B. Y., Kim, N. K., Lee, C. S., Hwang, I. H., Effect of fiber type on postmortem proteolysis in longissimus muscle of Landrace and Korean native black pigs. Meat Sci. 2007, 77, 482-491.
    • (2007) Meat Sci , vol.77 , pp. 482-491
    • Park, B.Y.1    Kim, N.K.2    Lee, C.S.3    Hwang, I.H.4
  • 18
    • 57149142755 scopus 로고    scopus 로고
    • Comparison of muscle proteome profiles in pure breeds of Norwegian Landrace and Duroc at three different ages
    • Hollung, K., Grove, H., Færgestad, E. M., Sidhu, M. S. et al., Comparison of muscle proteome profiles in pure breeds of Norwegian Landrace and Duroc at three different ages. Meat Sci. 2009, 83, 487-492.
    • (2009) Meat Sci , vol.83 , pp. 487-492
    • Hollung, K.1    Grove, H.2    Færgestad, E.M.3    Sidhu, M.S.4
  • 19
    • 68849087671 scopus 로고    scopus 로고
    • Differential proteome analysis of porcine skeletal muscles between Meishan and Large White
    • Xu, Y. J., Jin, M. L., Wang, L. J., Zhang, A. D. et al., Differential proteome analysis of porcine skeletal muscles between Meishan and Large White. J. Anim. Sci. 2009, 87, 2519-2527.
    • (2009) J. Anim. Sci. , vol.87 , pp. 2519-2527
    • Xu, Y.J.1    Jin, M.L.2    Wang, L.J.3    Zhang, A.D.4
  • 20
    • 78650745355 scopus 로고    scopus 로고
    • Authenticity determination of meat and meat products on the protein and DNA basis
    • Montowska, M., Pospiech, E., Authenticity determination of meat and meat products on the protein and DNA basis. Food Rev. Int. 2011, 27, 84-100.
    • (2011) Food Rev. Int , vol.27 , pp. 84-100
    • Montowska, M.1    Pospiech, E.2
  • 21
    • 84862105406 scopus 로고    scopus 로고
    • Is authentication of regional and traditional food made of meat possible?
    • Montowska, M., Pospiech, E., Is authentication of regional and traditional food made of meat possible? Crit. Rev. Food Sci. Nutr. 2012, 52, 475-487.
    • (2012) Crit. Rev. Food Sci. Nutr. , vol.52 , pp. 475-487
    • Montowska, M.1    Pospiech, E.2
  • 22
    • 80052615687 scopus 로고    scopus 로고
    • Differences in two-dimensional gel electrophoresis patterns of skeletal muscle myosin light chain isoforms between Bos taurus, Sus scrofa and selected poultry species
    • Montowska, M., Pospiech, E., Differences in two-dimensional gel electrophoresis patterns of skeletal muscle myosin light chain isoforms between Bos taurus, Sus scrofa and selected poultry species. J. Sci. Food Agric. 2011, 91, 2449-2456.
    • (2011) J. Sci. Food Agric , vol.91 , pp. 2449-2456
    • Montowska, M.1    Pospiech, E.2
  • 23
    • 0026114381 scopus 로고
    • Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses
    • Koohmaraie, M., Whipple, G., Kretchmar, D. H., Crouse, J. D. et al., Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. J. Anim. Sci. 1991, 69, 617-624.
    • (1991) J. Anim. Sci. , vol.69 , pp. 617-624
    • Koohmaraie, M.1    Whipple, G.2    Kretchmar, D.H.3    Crouse, J.D.4
  • 24
    • 0002434049 scopus 로고
    • Lawrie, R. (Eds.), Elsevier Applied Science, London
    • Monin, G., Ouali, A., in: Lawrie, R. (Eds.), Developments in Meat Science, Elsevier Applied Science, London 1992, pp. 89-157.
    • (1992) Developments in Meat Science , pp. 89-157
    • Monin, G.1    Ouali, A.2
  • 25
    • 0030305246 scopus 로고    scopus 로고
    • Structural weaking of skeletalmuscle tissue during postmortem ageing of meat: the non-enzymatic mechanism of meat tenderization
    • Takahashi, K., Structural weaking of skeletalmuscle tissue during postmortem ageing of meat: the non-enzymatic mechanism of meat tenderization. Meat Sci. 1996, 43, S67-S80.
    • (1996) Meat Sci , vol.43
    • Takahashi, K.1
  • 26
    • 79956220810 scopus 로고    scopus 로고
    • Post mortem development of meat quality as related to changes in cytoskeletal proteins of chicken muscles
    • Tomaszewska-Gras, J., Scherurs, F. J. G. I, Kijowski, J., Post mortem development of meat quality as related to changes in cytoskeletal proteins of chicken muscles. British Poultry Sci. 2011, 52, 189-201.
    • (2011) British Poultry Sci , vol.52 , pp. 189-201
    • Tomaszewska-Gras, J.1    Scherurs, F.J.G.I.2    Kijowski, J.3
  • 27
    • 79951575655 scopus 로고    scopus 로고
    • Impact of polymorphysm of the regulatory subunit of the μ-calpain (CAPN1S) on the proteolysis process and meat tenderness of young cattle
    • Iwanowska, A., Grześ, B., Mikołajczak, B., Iwańska, E. et al., Impact of polymorphysm of the regulatory subunit of the μ-calpain (CAPN1S) on the proteolysis process and meat tenderness of young cattle. Mol. Biol. Rep. 2011, 38, 1295-1300.
    • (2011) Mol. Biol. Rep. , vol.38 , pp. 1295-1300
    • Iwanowska, A.1    Grześ, B.2    Mikołajczak, B.3    Iwańska, E.4
  • 28
    • 0036571319 scopus 로고    scopus 로고
    • Silver staining of proteins on electroblotting membranes and intensification of silver staining of proteins separated by polyacrylamide gel electrophoresis
    • Sørensen, B. K., Højrup, P., Østergård, E., Jørgensen, C. S. et al., Silver staining of proteins on electroblotting membranes and intensification of silver staining of proteins separated by polyacrylamide gel electrophoresis. Anal. Biochem. 2002, 304, 33-41.
    • (2002) Anal. Biochem. , vol.304 , pp. 33-41
    • Sørensen, B.K.1    Højrup, P.2    Østergård, E.3    Jørgensen, C.S.4
  • 30
    • 0001119134 scopus 로고
    • The association of protein solubility with physical properties in a fermented sausage
    • Klement, J. T., Cassens, R. G., Fennema, O. W., The association of protein solubility with physical properties in a fermented sausage. J. Food Sci. 1973, 38, 1128-1131.
    • (1973) J. Food Sci. , vol.38 , pp. 1128-1131
    • Klement, J.T.1    Cassens, R.G.2    Fennema, O.W.3
  • 31
    • 0026579299 scopus 로고
    • Activities of pork muscle proteases in model cured meat systems
    • Toldra, F., Rico, E., Flores, M., Activities of pork muscle proteases in model cured meat systems. Biochimie 1992, 74, 291-296.
    • (1992) Biochimie , vol.74 , pp. 291-296
    • Toldra, F.1    Rico, E.2    Flores, M.3
  • 33
    • 20244368177 scopus 로고    scopus 로고
    • Species identification of cooked fish by urea isoelectric focusing and sodium dodecylsulfate polyacrylamide gel electrophoresis: a collaborative study
    • Rehbein, H., Kundiger, R., Yman, I. M., Ferm, M. et al., Species identification of cooked fish by urea isoelectric focusing and sodium dodecylsulfate polyacrylamide gel electrophoresis: a collaborative study. Food Chem. 1999, 67, 333-339.
    • (1999) Food Chem. , vol.67 , pp. 333-339
    • Rehbein, H.1    Kundiger, R.2    Yman, I.M.3    Ferm, M.4
  • 34
    • 1242339585 scopus 로고    scopus 로고
    • Application of proteome analysis to seafood authentication
    • Martinez, I., Friis, T. J., Application of proteome analysis to seafood authentication. Proteomics 2004, 4, 347-354.
    • (2004) Proteomics , vol.4 , pp. 347-354
    • Martinez, I.1    Friis, T.J.2
  • 35
    • 33947301122 scopus 로고    scopus 로고
    • High resolution two-dimensional electrophoresis as a tool to differentiate wild from farmed cod (Gadus morhua) and to assess the protein composition of klipfish
    • Martinez, I., Slizyte, R., Daukas, E., High resolution two-dimensional electrophoresis as a tool to differentiate wild from farmed cod (Gadus morhua) and to assess the protein composition of klipfish. Food Chem. 2007, 102, 504-510.
    • (2007) Food Chem , vol.102 , pp. 504-510
    • Martinez, I.1    Slizyte, R.2    Daukas, E.3
  • 36
    • 21144470425 scopus 로고
    • Differentiation of animal species by meat proteins. I. Detection of beef mixed with pork meat by isoelectric focusing of the A2 myosin light chain
    • Di Luccia, A., Santoro, A., Anastasio, A., Sarli, T. et al., Differentiation of animal species by meat proteins. I. Detection of beef mixed with pork meat by isoelectric focusing of the A2 myosin light chain. Ital. J. Food Sci. 1992, 3, 195-204.
    • (1992) Ital. J. Food Sci. , vol.3 , pp. 195-204
    • Di Luccia, A.1    Santoro, A.2    Anastasio, A.3    Sarli, T.4
  • 37
    • 77954374037 scopus 로고    scopus 로고
    • A proteomic-based approach for detection of chicken in meat mixes
    • Sentandreu, M. A., Fraser, P. D., Halket, J., Patel, R. et al., A proteomic-based approach for detection of chicken in meat mixes. J. Proteome Res. 2010, 9, 3374-3383.
    • (2010) J. Proteome Res. , vol.9 , pp. 3374-3383
    • Sentandreu, M.A.1    Fraser, P.D.2    Halket, J.3    Patel, R.4


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