Comparative Analysis of Muscle Proteome from Porcine White and Red Muscles by Two-dimensional Electrophoresis

이차원전기영동법을 이용한 white muscle과 red muscle간의 단백질 발현양상의 비교분석

  • Kim, N.K. (Department of Applied Biochemistry) ;
  • Joh, J.H. (Department of Applied Biochemistry) ;
  • Chu, K.S. (Department of Applied Biochemistry) ;
  • Park, H.R. (Department of Applied Biochemistry) ;
  • Park, B.Y. (National Livestock Research Institute, R.D.A.) ;
  • Kim, O.H. (Department of Animal Science, College of Natural Science, Konkuk University) ;
  • Lee, C.S. (Department of Applied Biochemistry)
  • 김남국 (건국대학교 자연과학대학 응용생화학) ;
  • 조중호 (건국대학교 자연과학대학 응용생화학) ;
  • 추교선 (건국대학교 자연과학대학 응용생화학) ;
  • 박혜란 (건국대학교 자연과학대학 응용생화학) ;
  • 박범영 (농촌진흥청 축산기술연구소) ;
  • 김언현 (건국대학교 자연과학대학 축산학과) ;
  • 이창수 (건국대학교 자연과학대학 응용생화학)
  • Published : 2003.10.31


The technique known as proteomics is useful for characterizing the protein expression pattern of a particular tissue or cell type as well as quantitatively identifying differences in the levels of individual proteins. In present study, we carried out the comparative expression patterns of white and red muscles. We used the two-dimensional electrophoresis(2-DE) for analyzing the protein expression. Proteins isolated from porcine white and red muscles were separated by 12% poly-acrylamide gel and then were detected by coomassie blue and silver staining. More than 600 protein spots were detected on each 2-DE gel. By visual analysis of the stained gel, five proteins were identified to be differentially expressed in the white vs red muscle. By database searching based on the molecular weights and pI(isoelectric point) of the five proteins, three of them were found to be most close to troponin I, T and myoglobin. However, further researche is needed for identification and functional analysis of the unidentified proteins. In conclusion, we found five proteins, which are differentially expressed in the white vs red muscle. The functional analysis of the differentially expressed proteins will provide valuable information on biochemical characteristics of the muscle type.


White and red muscle;Two-dimensional electrophoresis


  1. Beecher, G. R., Kastenschmidt, L. L., Cassens, R. G., Hoekstra, W. G. and Briskey, E. J. 1968. A comparison of the light and dark portions of a striated muscle. J. Food Sci. 33:84.
  2. Cassens, R. G. and Cooper, C. C. 1971. Red and white muscle. Adv. Food Res. 19:1.
  3. Cornet, M. and Bousset, J. 1999. Free amino acids and dipeptides in procine muscles: differences between red and white muscles. Meat Sci. 51:215.
  4. Essen-Gustavsson, B., Karlstrom, K. and Lundstrom, K. 1992. Muscle fibre characteristics and metabolic response at slaughter in pigs of different halothane genotypes and their relation to meat quality. Meat Sci. 31:1.
  5. Fernandez, X., Lefaucheur, L. and Candek, M. 1995. Comparative study of two classifications of muscle fibres:consequences for the photometric determination of glycogen according to fibre type in red and white muscle of the pig. Meat Sci. 41:225.
  6. Henckel, P., Oksbjerg, N., Erlandsen, E., Barton-Gade, P. and Bejerholm, C. 1997. Histo- and biochemical characteristics of the longissimus dorsi muscle in pigs and their relationships to performance and meat quality. Meat Sci. 47:311.
  7. Karlsson, A., Enfalt, A. C., Essen-Gustavsson, B., Lundstrom, K., Rydhmer, L. and Stern, S. 1993. Muscle histochemical and biochemical properties in relation to meat quality during selection for increased lean tissue growth rate in pigs. J. Anim. Sci. 71:930.
  8. Karlsson, A. H., Klont, R. E. and Fernandez, X. 1999. Skeletal muscle fibres as factors for pork quality. Livest. Prod. Sci. 60:255.
  9. Klont, R. E., Brocks, L. and Eikelenboom. G. 1998. Muscle fibre type and meat quality. Meat Sci. 49:S219.
  10. Lawrie, R. A. 1950. Some observations on factors affecting myoglobin concentrations in muscle. J. Agr. Sci. 40:356.
  11. Lawrie, R. A. 1985. Meat science, 4th ed. Pergamon press, Headington Hill Hall, Oxford, U.K., p43.
  12. Maltin, C. A., Warkup, C. C., Matthews, K. R., Grant, C. M., Porter, A. D. and Delday, M. I. 1997. Pig muscle fibre characteristics as a source of variation in eating quality. Meat Sci. 47:237.
  13. Margreth, A. and Novello, F. 1964. Observations on the chemical determination and distribution of ribonucleic acid in several striated muscle. Exp. Cell Res. 35:38.
  14. Molloy, M. P., Herbert, B. R., Walsh, B. J., Tyler, M. I., Traini, M., Sanchez, J. C., Hochstrasser, D. F., Williams, K. L. and Gooley, A. A. 1998. Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis. Electrophoresis. 19:837.
  15. Neuhoff, V., Arold, N., Taube, D. and Ehrhardt, W. 1988. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using coomassie brilliant blue G-250 and R-250. Electrophoresis. 9:255.
  16. Ozawa, S., Mitsuhashi, T., Mitsumoto, M., Matsumoto, S., Ttoh, N., Itagaki, K., Kohno, Y. and Dohgo, T. 2000. The characteristics of muscle fiber types of longissimus thoracis muscle and their influences on the quantity and quality of meat from japanese black steers. Meat Sci. 54:65.
  17. Pandey, A. and Mann, M. 2000. Proteomics to study genes and genomes. Nature 405:837.
  18. Pette, D. and Staron, R. S. 1990. Cellular and molecular diversities of mammalian skeletal muscle fibres. Rev. Physiol. Biochem. Pharmacol. 116:1.
  19. Shevchenko, A., Wilm, M., Vorm, O. and Mann, M. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68:850.
  20. Soren, N. H., Michael, D. W. and Rainer Cramer. 2001. Proteomics-post-genomic cartography to understand gene function. Pharmacol. Sci. 22:376.
  21. Takasu, T. and Hunhes, B. P. 1966. Lactate dehydrogenase isoenzymes in developing human muscle. Nature 212:609.