메뉴 건너뛰기




Volumn 88, Issue 2, 2010, Pages 593-598

Differential expression of liver proteins in Chianina and Holstein young bulls

Author keywords

Cattle breed; Liver; Proteome; Two dimensional electrophoresis

Indexed keywords

ANIMAL; ARTICLE; CATTLE; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIVER; MALE; MASS SPECTROMETRY; METABOLISM; PROTEIN SYNTHESIS; PROTEOMICS; TWO DIMENSIONAL GEL ELECTROPHORESIS;

EID: 75949088794     PISSN: 00218812     EISSN: 15253163     Source Type: Journal    
DOI: 10.2527/jas.2009-2193     Document Type: Article
Times cited : (8)

References (27)
  • 2
    • 18744411016 scopus 로고    scopus 로고
    • A missense mutation (Q279R) in the Fumarylacetoacetate hydrolase gene, responsible for hereditary tyrosemia, acts as a splicing mutation
    • Dreumont, N., J. A. Poudrier, A. Bergeron, H. L. Levy, F. Baklouti, and R. M. Tanguay. 2001. A missense mutation (Q279R) in the Fumarylacetoacetate hydrolase gene, responsible for hereditary tyrosemia, acts as a splicing mutation. BMC Genet. 2:9.
    • (2001) BMC Genet , vol.2 , pp. 9
    • Dreumont, N.1    Poudrier, J.A.2    Bergeron, A.3    Levy, H.L.4    Baklouti, F.5    Tanguay, R.M.6
  • 5
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Gorg, A., W. Weiss, and M. J. Dunn. 2004. Current two-dimensional electrophoresis technology for proteomics. Proteomics 4:3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 6
    • 33748888361 scopus 로고    scopus 로고
    • A proteomic analysis of the acute effects of high-intensity exercise on skeletal muscle proteins in fasted rats
    • Guelfi, K., T. Casey, J. Giles, P. Forunier, and P. Arthur. 2006. A proteomic analysis of the acute effects of high-intensity exercise on skeletal muscle proteins in fasted rats. Clin. Exp. Pharmacol. Physiol. 33:952-957.
    • (2006) Clin. Exp. Pharmacol. Physiol , vol.33 , pp. 952-957
    • Guelfi, K.1    Casey, T.2    Giles, J.3    Forunier, P.4    Arthur, P.5
  • 7
    • 0027550639 scopus 로고
    • Diurnal variation of rumen ammonia, serum urea and milk urea in dairy cows at high and low yields
    • Gustafsson, A. H., and D. L. Palmquist. 1993. Diurnal variation of rumen ammonia, serum urea and milk urea in dairy cows at high and low yields. J. Dairy Sci. 76:465-484.
    • (1993) J. Dairy Sci , vol.76 , pp. 465-484
    • Gustafsson, A.H.1    Palmquist, D.L.2
  • 9
    • 0242498430 scopus 로고    scopus 로고
    • Structure and function of enzymes of the Leloir pathway for galactose metabolism
    • Holden, H. M., I. Rayment, and J. B. Thoden. 2003. Structure and function of enzymes of the Leloir pathway for galactose metabolism. J. Biol. Chem. 278:43885-43888.
    • (2003) J. Biol. Chem , vol.278 , pp. 43885-43888
    • Holden, H.M.1    Rayment, I.2    Thoden, J.B.3
  • 10
    • 34250634816 scopus 로고    scopus 로고
    • Application of proteomics to understand the molecular mechanisms behind meat quality
    • Hollung, K., E. Veiseth, X. Jia, E. M. Fargestad, and K. I. Hildrum. 2007. Application of proteomics to understand the molecular mechanisms behind meat quality. Meat Sci. 77:97-104.
    • (2007) Meat Sci , vol.77 , pp. 97-104
    • Hollung, K.1    Veiseth, E.2    Jia, X.3    Fargestad, E.M.4    Hildrum, K.I.5
  • 11
    • 0003241502 scopus 로고    scopus 로고
    • Practical aspects of urea and ammonia metabolism in ruminants
    • Huntington, G. B., and S. L. Archibeque. 2000. Practical aspects of urea and ammonia metabolism in ruminants. J. Anim. Sci. 77:1-11.
    • (2000) J. Anim. Sci , vol.77 , pp. 1-11
    • Huntington, G.B.1    Archibeque, S.L.2
  • 13
    • 0242384896 scopus 로고    scopus 로고
    • Intron disruption of the annexin IV gene reveals novel transcripts
    • Li, B., J. R. Dedman, and M. A. Kaetzel. 2003. Intron disruption of the annexin IV gene reveals novel transcripts. J. Biol. Chem. 278:43276-43283.
    • (2003) J. Biol. Chem , vol.278 , pp. 43276-43283
    • Li, B.1    Dedman, J.R.2    Kaetzel, M.A.3
  • 14
    • 0034659898 scopus 로고    scopus 로고
    • Genomics, gene expression and DNA arrays
    • Lockhart, D. J., and E. A. Winzeler. 2000. Genomics, gene expression and DNA arrays. Nature 405:827-836.
    • (2000) Nature , vol.405 , pp. 827-836
    • Lockhart, D.J.1    Winzeler, E.A.2
  • 16
    • 33745713248 scopus 로고    scopus 로고
    • Understanding meat quality through the application of genomic and proteomic approaches
    • Mullen, A. M., P. C. Stapleton, D. Corcoran, R. M. Hamill, and A. White. 2006. Understanding meat quality through the application of genomic and proteomic approaches. Meat Sci. 74:3-16.
    • (2006) Meat Sci , vol.74 , pp. 3-16
    • Mullen, A.M.1    Stapleton, P.C.2    Corcoran, D.3    Hamill, R.M.4    White, A.5
  • 17
    • 2542517819 scopus 로고    scopus 로고
    • Activities of the enzymes of hepatic gluconeogenesis in periparturient dairy cows with induced fatty liver
    • Murondoti, A., R. Jorritsma, A. C. Beynen, T. Wensing, and M. J. Geelen. 2004. Activities of the enzymes of hepatic gluconeogenesis in periparturient dairy cows with induced fatty liver. J. Dairy Res. 71:129-134.
    • (2004) J. Dairy Res , vol.71 , pp. 129-134
    • Murondoti, A.1    Jorritsma, R.2    Beynen, A.C.3    Wensing, T.4    Geelen, M.J.5
  • 18
    • 33947127015 scopus 로고    scopus 로고
    • Carbohydrate and lipid metabolism in farm animals
    • Nafikov, R. A., and D. C. Beitz. 2007. Carbohydrate and lipid metabolism in farm animals. J. Nutr. 7:702-705.
    • (2007) J. Nutr , vol.7 , pp. 702-705
    • Nafikov, R.A.1    Beitz, D.C.2
  • 19
    • 0023931883 scopus 로고
    • 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
    • Neuhoff, V., N. Arold, D. Taube, and W. Ehrhardt. 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 9:255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 20
    • 0029098696 scopus 로고
    • Retinoids stimulate fibrinogen production both in vitro (hepatocytes) and in vivo induction requires activation of the retinoid x receptor
    • Nicodeme, E., M. Nicaud, and M. Issandou. 1995. Retinoids stimulate fibrinogen production both in vitro (hepatocytes) and in vivo induction requires activation of the retinoid x receptor. Arterioscler. Thromb. Vasc. Biol. 15:1660-1667.
    • (1995) Arterioscler. Thromb. Vasc. Biol , vol.15 , pp. 1660-1667
    • Nicodeme, E.1    Nicaud, M.2    Issandou, M.3
  • 21
    • 33947325566 scopus 로고    scopus 로고
    • Proteomic comparison between Japanese Black and Holstein cattle by two dimensional gel electrophoresis and identification of proteins
    • Ohsaki, H., M. Okada, S. Sasazaki, T. Hinenoya, T. Sawa, S. Iwanaga, H. Tsuruta, F. Mukai, and H. Mannen. 2007. Proteomic comparison between Japanese Black and Holstein cattle by two dimensional gel electrophoresis and identification of proteins. Asian-Aust. J. Anim. Sci. 20:638-644.
    • (2007) Asian-Aust J. Anim. Sci , vol.20 , pp. 638-644
    • Ohsaki, H.1    Okada, M.2    Sasazaki, S.3    Hinenoya, T.4    Sawa, T.5    Iwanaga, S.6    Tsuruta, H.7    Mukai, F.8    Mannen, H.9
  • 22
    • 0021173140 scopus 로고
    • Whole body and tissue fractional protein synthesis in the ovine foetus in utero
    • Schaefer, A. L., and C. R. Krishnamurti. 1984. Whole body and tissue fractional protein synthesis in the ovine foetus in utero. Br. J. Nutr. 52:359-369.
    • (1984) Br. J. Nutr , vol.52 , pp. 359-369
    • Schaefer, A.L.1    Krishnamurti, C.R.2
  • 25
    • 0037387168 scopus 로고    scopus 로고
    • Proteins from bovine tissue and biological fluids: Defining a reference electrophoresis map of liver, kidney, muscle, plasma and red blood cells
    • Talamo, F., C. D'Ambrosio, S. Arena, P. Del Vecchio, L. Ledda, G. Zehender, L. Ferrara, and A. Scaloni. 2003. Proteins from bovine tissue and biological fluids: Defining a reference electrophoresis map of liver, kidney, muscle, plasma and red blood cells. Proteomics 3:440-460.
    • (2003) Proteomics , vol.3 , pp. 440-460
    • Talamo, F.1    D'Ambrosio, C.2    Arena, S.3    del Vecchio, P.4    Ledda, L.5    Zehender, G.6    Ferrara, L.7    Scaloni, A.8
  • 26
    • 0033200322 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a carbon-carbon bond hydrolase
    • Timm, D. E., H. A. Mueller, P. Bhanumoorthy, J. M. Harp, and G. J. Bunick. 1999. Crystal structure and mechanism of a carbon-carbon bond hydrolase. Structure 7:1023-1033.
    • (1999) Structure , vol.7 , pp. 1023-1033
    • Timm, D.E.1    Mueller, H.A.2    Bhanumoorthy, P.3    Harp, J.M.4    Bunick, G.J.5
  • 27
    • 38649086403 scopus 로고    scopus 로고
    • Comparative proteomic analysis of livers from ketotic cows
    • Xu, C., and Z. Wang. 2008. Comparative proteomic analysis of livers from ketotic cows. Vet. Res. Commun. 32:263-273.
    • (2008) Vet. Res. Commun , vol.32 , pp. 263-273
    • Xu, C.1    Wang, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.