메뉴 건너뛰기




Volumn 10, Issue 4, 2015, Pages

An optimized trichloroacetic acid/acetone precipitation method for two-dimensional gel electrophoresis analysis of Qinchuan cattle longissimus dorsi muscle containing high proportion of marbling

Author keywords

[No Author keywords available]

Indexed keywords

ACETONE; TRICHLOROACETIC ACID; LIPID; NUCLEIC ACID; PROTEIN; PROTEOME;

EID: 84929486098     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0124723     Document Type: Article
Times cited : (30)

References (54)
  • 1
    • 74049158318 scopus 로고    scopus 로고
    • Proteomics data mining
    • PMID: 19929606
    • Wilkins M. Proteomics data mining. Expert Rev Proteomics. 2009; 6: 599-603. doi: 10.1586/epr.09.81 PMID: 19929606
    • (2009) Expert Rev Proteomics , vol.6 , pp. 599-603
    • Wilkins, M.1
  • 2
  • 3
    • 10644223453 scopus 로고    scopus 로고
    • Quantitative protein profiling using antibody arrays
    • PMID: 15540209
    • Barry R, Soloviev M. Quantitative protein profiling using antibody arrays. Proteomics. 2004; 4: 3717-3726. PMID: 15540209
    • (2004) Proteomics , vol.4 , pp. 3717-3726
    • Barry, R.1    Soloviev, M.2
  • 4
    • 33748567134 scopus 로고    scopus 로고
    • Gel-free mass spectrometry-based high throughput proteomics: Tools for studying biological response of proteins and proteomes
    • PMID: 16888762
    • Roe MR, Griffin TJ. Gel-free mass spectrometry-based high throughput proteomics: tools for studying biological response of proteins and proteomes. Proteomics. 2006; 6: 4678-4687. PMID: 16888762
    • (2006) Proteomics , vol.6 , pp. 4678-4687
    • Roe, M.R.1    Griffin, T.J.2
  • 5
    • 0015968532 scopus 로고
    • The heterogeneity of mouse-chromatin nonhistone proteins as evidenced by two-dimensional polyacrylamide-gel electrophoresis and ion-exchange chromatography
    • PMID: 4816452
    • MacGillivray AJ, Rickwood D. The heterogeneity of mouse-chromatin nonhistone proteins as evidenced by two-dimensional polyacrylamide-gel electrophoresis and ion-exchange chromatography. Eur J Biochem. 1974; 41: 181-190. PMID: 4816452
    • (1974) Eur J Biochem , vol.41 , pp. 181-190
    • MacGillivray, A.J.1    Rickwood, D.2
  • 6
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • PMID: 236308
    • O'Farrell PH. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975; 250: 4007-4021. PMID: 236308
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 7
    • 77957220211 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: Past, present and future
    • PMID: 20685252
    • Rabilloud T, Chevallet M, Luche S, Lelong C. Two-dimensional gel electrophoresis in proteomics: Past, present and future. J Proteomics. 2010; 73: 2064-2077. doi: 10.1016/j.jprot.2010.05.016 PMID: 20685252
    • (2010) J Proteomics , vol.73 , pp. 2064-2077
    • Rabilloud, T.1    Chevallet, M.2    Luche, S.3    Lelong, C.4
  • 8
    • 84888604345 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in the light of new developments
    • Pomastowski P, Buszewski B. Two-dimensional gel electrophoresis in the light of new developments. TrAC Trends in Analytical Chemistry. 2014; 53: 167-177.
    • (2014) TrAC Trends in Analytical Chemistry , vol.53 , pp. 167-177
    • Pomastowski, P.1    Buszewski, B.2
  • 9
    • 80052024910 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: A tutorial
    • PMID: 21669304
    • Rabilloud T, Lelong C. Two-dimensional gel electrophoresis in proteomics: a tutorial. J Proteomics. 2011; 74: 1829-1841. doi: 10.1016/j.jprot.2011.05.040 PMID: 21669304
    • (2011) J Proteomics , vol.74 , pp. 1829-1841
    • Rabilloud, T.1    Lelong, C.2
  • 10
    • 84865411004 scopus 로고    scopus 로고
    • DMSO, an organic cleanup solvent for TCA/acetone-precipitated proteins, improves 2-DE protein analysis of rice roots
    • Song Y, Zhang H, Wang G, Shen Z. DMSO, an organic cleanup solvent for TCA/acetone-precipitated proteins, improves 2-DE protein analysis of rice roots. Plant Molecular Biology Reporter. 2012; 30: 1204-1209.
    • (2012) Plant Molecular Biology Reporter , vol.30 , pp. 1204-1209
    • Song, Y.1    Zhang, H.2    Wang, G.3    Shen, Z.4
  • 11
    • 55749102260 scopus 로고    scopus 로고
    • Compatibility of plant protein extraction methods with mass spectrometry for proteome analysis
    • Sheoran IS, Ross ARS, Olson DJH, Sawhney VK. Compatibility of plant protein extraction methods with mass spectrometry for proteome analysis. Plant Science. 2009; 176: 99-104.
    • (2009) Plant Science , vol.176 , pp. 99-104
    • Sheoran, I.S.1    Ross, A.R.S.2    Olson, D.J.H.3    Sawhney, V.K.4
  • 12
    • 79957640312 scopus 로고    scopus 로고
    • Buffer optimization for bovine Longissimus muscle tissues: Proteome analysis of Korean native cattle using 2-dimensional gel electrophoresis
    • Lee H, Han J, Lee K, Kim E, Jin Y, Oh J, et al. Buffer optimization for bovine Longissimus muscle tissues: Proteome analysis of Korean native cattle using 2-dimensional gel electrophoresis. Food Sci. Biotechnol. 2010; 19: 1107-1112.
    • (2010) Food Sci. Biotechnol , vol.19 , pp. 1107-1112
    • Lee, H.1    Han, J.2    Lee, K.3    Kim, E.4    Jin, Y.5    Oh, J.6
  • 14
    • 70450227342 scopus 로고    scopus 로고
    • Optimized sample preparation for two-dimensional gel electrophoresis of soluble proteins from chicken bursa of Fabricius
    • Available PMID: 19814785
    • Wu Y, Zhou J, Zhang X, Zheng X, Jiang X, Shi L, et al. Optimized sample preparation for two-dimensional gel electrophoresis of soluble proteins from chicken bursa of Fabricius. Proteome Sci. 2009; 7: 38. Available: http://www.proteomesci.com/content/7/1/38. doi: 10.1186/1477-5956-7-38 PMID: 19814785
    • (2009) Proteome Sci , vol.7 , pp. 38
    • Wu, Y.1    Zhou, J.2    Zhang, X.3    Zheng, X.4    Jiang, X.5    Shi, L.6
  • 15
    • 34848899585 scopus 로고    scopus 로고
    • An optimized procedure for solubilization, reduction, and transfer of human breast cancer membrane-enriched fraction by 2-DE
    • PMID: 17722185
    • Ruan Y, Wan M. An optimized procedure for solubilization, reduction, and transfer of human breast cancer membrane-enriched fraction by 2-DE. Electrophoresis. 2007; 28: 3333-3340. PMID: 17722185
    • (2007) Electrophoresis , vol.28 , pp. 3333-3340
    • Ruan, Y.1    Wan, M.2
  • 16
    • 0042164911 scopus 로고    scopus 로고
    • Enhanced resolution of glycosylphosphatidylinositol-anchored and transmembrane proteins from the lipid-rich myelin membrane by two-dimensional gel electrophoresis
    • PMID: 12872231
    • Taylor CM, Pfeiffer SE. Enhanced resolution of glycosylphosphatidylinositol-anchored and transmembrane proteins from the lipid-rich myelin membrane by two-dimensional gel electrophoresis. Proteomics. 2003; 3: 1303-1312. PMID: 12872231
    • (2003) Proteomics , vol.3 , pp. 1303-1312
    • Taylor, C.M.1    Pfeiffer, S.E.2
  • 17
    • 0037274566 scopus 로고    scopus 로고
    • Solubilization of trichloroacetic acid (TCA) precipitated microbial proteins via naOH for two-dimensional electrophoresis
    • PMID: 12643547
    • Nandakumar MP, Shen J, Raman B, Marten MR. Solubilization of trichloroacetic acid (TCA) precipitated microbial proteins via naOH for two-dimensional electrophoresis. J Proteome Res. 2003; 2: 89-93. PMID: 12643547
    • (2003) J Proteome Res , vol.2 , pp. 89-93
    • Nandakumar, M.P.1    Shen, J.2    Raman, B.3    Marten, M.R.4
  • 18
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • PMID: 15543535
    • Gorg A, Weiss W, Dunn MJ. Current two-dimensional electrophoresis technology for proteomics. Proteomics. 2004; 4: 3665-3685. PMID: 15543535
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Gorg, A.1    Weiss, W.2    Dunn, M.J.3
  • 19
    • 51649124682 scopus 로고    scopus 로고
    • Evaluation of three different protocols of protein extraction for Arabidopsis thaliana leaf proteome analysis by two-dimensional electrophoresis
    • PMID: 18656559
    • Maldonado AM, Echevarria-Zomeno S, Jean-Baptiste S, Hernandez M, Jorrin-Novo JV. Evaluation of three different protocols of protein extraction for Arabidopsis thaliana leaf proteome analysis by two-dimensional electrophoresis. J Proteomics. 2008; 71: 461-472. doi: 10.1016/j.jprot.2008.06.012 PMID: 18656559
    • (2008) J Proteomics , vol.71 , pp. 461-472
    • Maldonado, A.M.1    Echevarria-Zomeno, S.2    Jean-Baptiste, S.3    Hernandez, M.4    Jorrin-Novo, J.V.5
  • 20
    • 0345550275 scopus 로고    scopus 로고
    • Comparison of protein precipitation methods for sample preparation prior to proteomic analysis
    • PMID: 14753699
    • Jiang L, He L, Fountoulakis M. Comparison of protein precipitation methods for sample preparation prior to proteomic analysis. Journal of Chromatography A. 2004; 1023: 317-320. PMID: 14753699
    • (2004) Journal of Chromatography A , vol.1023 , pp. 317-320
    • Jiang, L.1    He, L.2    Fountoulakis, M.3
  • 21
    • 22044456721 scopus 로고    scopus 로고
    • Preparation of protein extracts from recalcitrant plant tissues: An evaluation of different methods for two-dimensional gel electrophoresis analysis
    • PMID: 15912556
    • Carpentier SC, Witters E, Laukens K, Deckers P, Swennen R, Panis B. Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis. Proteomics. 2005; 5: 2497-2507. PMID: 15912556
    • (2005) Proteomics , vol.5 , pp. 2497-2507
    • Carpentier, S.C.1    Witters, E.2    Laukens, K.3    Deckers, P.4    Swennen, R.5    Panis, B.6
  • 22
    • 0037265724 scopus 로고    scopus 로고
    • Extraction of proteins from plant tissues for two-dimensional electrophoresis analysis
    • PMID: 12652593
    • Giavalisco P, Nordhoff E, Lehrach H, Gobom J, Klose J. Extraction of proteins from plant tissues for two-dimensional electrophoresis analysis. Electrophoresis. 2003; 24: 207-216. PMID: 12652593
    • (2003) Electrophoresis , vol.24 , pp. 207-216
    • Giavalisco, P.1    Nordhoff, E.2    Lehrach, H.3    Gobom, J.4    Klose, J.5
  • 23
    • 3042736601 scopus 로고    scopus 로고
    • Protein extraction from mature rice leaves for two-dimensional gel electrophoresis and its application in proteome analysis
    • PMID: 15221747
    • Islam N, Lonsdale M, Upadhyaya NM, Higgins TJ, Hirano H, Akhurst R. Protein extraction from mature rice leaves for two-dimensional gel electrophoresis and its application in proteome analysis. Proteomics. 2004; 4: 1903-1908. PMID: 15221747
    • (2004) Proteomics , vol.4 , pp. 1903-1908
    • Islam, N.1    Lonsdale, M.2    Upadhyaya, N.M.3    Higgins, T.J.4    Hirano, H.5    Akhurst, R.6
  • 24
    • 4444237731 scopus 로고    scopus 로고
    • A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues
    • PMID: 15352226
    • Saravanan RS, Rose JK. A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues. Proteomics. 2004; 4: 2522-2532. PMID: 15352226
    • (2004) Proteomics , vol.4 , pp. 2522-2532
    • Saravanan, R.S.1    Rose, J.K.2
  • 25
    • 84896694811 scopus 로고    scopus 로고
    • Proteomic sample preparation for blast wound characterization
    • Available PMID: 24529238
    • Chromy BA, Eldridge A, Forsberg JA, Brown TS, Kirkup BC, Elster E, et al. Proteomic sample preparation for blast wound characterization. Proteome Sci. 2014; 12: 10. Available: http://www.proteomesci.com/content/12/1/10. doi: 10.1186/1477-5956-12-10 PMID: 24529238
    • (2014) Proteome Sci , vol.12 , pp. 10
    • Chromy, B.A.1    Eldridge, A.2    Forsberg, J.A.3    Brown, T.S.4    Kirkup, B.C.5    Elster, E.6
  • 26
    • 84869838929 scopus 로고    scopus 로고
    • Sequential extraction results in improved proteome profiling of medicinal plant Pinellia ternata tubers, which contain large amounts of high-abundance proteins
    • PMID: 23185632
    • Wu X, Xiong E, An S, Gong F, Wang W. Sequential extraction results in improved proteome profiling of medicinal plant Pinellia ternata tubers, which contain large amounts of high-abundance proteins. PLoS One. 2012; 7: e50497. doi: 10.1371/journal.pone.0050497 PMID: 23185632
    • (2012) PLoS One , vol.7 , pp. e50497
    • Wu, X.1    Xiong, E.2    An, S.3    Gong, F.4    Wang, W.5
  • 27
    • 77953637963 scopus 로고    scopus 로고
    • Proteome changes in bovine longissimus thoracis muscle during the first 48 h postmortem: Shifts in energy status and myofibrillar stability
    • PMID: 20515034
    • Bjarnadottir SG, Hollung K, Faergestad EM, Veiseth-Kent E. Proteome changes in bovine longissimus thoracis muscle during the first 48 h postmortem: shifts in energy status and myofibrillar stability. J Agric Food Chem. 2010; 58: 7408-7414. doi: 10.1021/jf100697h PMID: 20515034
    • (2010) J Agric Food Chem , vol.58 , pp. 7408-7414
    • Bjarnadottir, S.G.1    Hollung, K.2    Faergestad, E.M.3    Veiseth-Kent, E.4
  • 28
    • 84878811149 scopus 로고    scopus 로고
    • Proteolytic pattern of myofibrillar protein and meat tenderness as affected by breed and aging time
    • PMID: 23743033
    • Marino R, Albenzio M, Della Malva A, Santillo A, Loizzo P, Sevi A. Proteolytic pattern of myofibrillar protein and meat tenderness as affected by breed and aging time. Meat Sci. 2013; 95: 281-287. doi: 10.1016/j.meatsci.2013.04.009 PMID: 23743033
    • (2013) Meat Sci , vol.95 , pp. 281-287
    • Marino, R.1    Albenzio, M.2    Della Malva, A.3    Santillo, A.4    Loizzo, P.5    Sevi, A.6
  • 29
    • 84755161198 scopus 로고    scopus 로고
    • Differentially expressed proteins during fat accumulation in bovine skeletal muscle
    • PMID: 20667664
    • Zhang Q, Lee HG, Han JA, Kim EB, Kang SK, Yin J, et al. Differentially expressed proteins during fat accumulation in bovine skeletal muscle. Meat Sci. 2010; 86: 814-820. doi: 10.1016/j.meatsci.2010.07.002 PMID: 20667664
    • (2010) Meat Sci , vol.86 , pp. 814-820
    • Zhang, Q.1    Lee, H.G.2    Han, J.A.3    Kim, E.B.4    Kang, S.K.5    Yin, J.6
  • 30
    • 0348206867 scopus 로고
    • Technical improvements in two-dimensional electrophoresis increase the level of genetic variation detected in wheat-seedling proteins
    • Damerval C, De Vienne D, Zivy M, Thiellement H. Technical improvements in two-dimensional electrophoresis increase the level of genetic variation detected in wheat-seedling proteins. Electrophoresis. 1986; 7: 52-54.
    • (1986) Electrophoresis. , vol.7 , pp. 52-54
    • Damerval, C.1    De Vienne, D.2    Zivy, M.3    Thiellement, H.4
  • 31
    • 0031837579 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of proteins in an immobilized pH 4-12 gradient
    • PMID: 9694305
    • Gorg A, Boguth G, Obermaier C, Weiss W. Two-dimensional electrophoresis of proteins in an immobilized pH 4-12 gradient. Electrophoresis. 1998; 19: 1516-1519. PMID: 9694305
    • (1998) Electrophoresis , vol.19 , pp. 1516-1519
    • Gorg, A.1    Boguth, G.2    Obermaier, C.3    Weiss, W.4
  • 32
    • 84904344736 scopus 로고    scopus 로고
    • A proteomics sample preparation method for mature, recalcitrant leaves of perennial plants
    • PMID: 25028960
    • Gang D, Xinyue Z, Na Z, Chengying L, BoW, Dingxiang P, et al. A proteomics sample preparation method for mature, recalcitrant leaves of perennial plants. PLoS One. 2014; 9: e102175. doi: 10.1371/journal.pone.0102175 PMID: 25028960
    • (2014) PLoS One , vol.9 , pp. e102175
    • Gang, D.1    Xinyue, Z.2    Na, Z.3    Chengying, L.4    Bo, W.5    Dingxiang, P.6
  • 33
    • 0348011459 scopus 로고    scopus 로고
    • An optimized protocol for isolation of soluble proteins from microalgae for two-dimensional gel electrophoresis analysis
    • Wang S-B, Hu Q, Sommerfeld M, Chen F. An optimized protocol for isolation of soluble proteins from microalgae for two-dimensional gel electrophoresis analysis. Journal of applied phycology. 2003; 15: 485-496.
    • (2003) Journal of Applied Phycology , vol.15 , pp. 485-496
    • Wang, S.-B.1    Hu, Q.2    Sommerfeld, M.3    Chen, F.4
  • 34
    • 66149121925 scopus 로고    scopus 로고
    • Differentially-expressed genes in pig Longissimus muscles with contrasting levels of fat, as identified by combined transcriptomic, reverse transcription PCR, and proteomic analyses
    • PMID: 19296579
    • Liu J, Damon M, Guitton N, Guisle I, Ecolan P, Vincent A, et al. Differentially-expressed genes in pig Longissimus muscles with contrasting levels of fat, as identified by combined transcriptomic, reverse transcription PCR, and proteomic analyses. J Agric Food Chem. 2009; 57: 3808-3817. doi: 10.1021/jf8033144 PMID: 19296579
    • (2009) J Agric Food Chem , vol.57 , pp. 3808-3817
    • Liu, J.1    Damon, M.2    Guitton, N.3    Guisle, I.4    Ecolan, P.5    Vincent, A.6
  • 35
    • 2942529230 scopus 로고    scopus 로고
    • Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • PMID: 15174147
    • Bouley J, Chambon C, Picard B. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics. 2004; 4: 1811-1824. PMID: 15174147
    • (2004) Proteomics , vol.4 , pp. 1811-1824
    • Bouley, J.1    Chambon, C.2    Picard, B.3
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • PMID: 942051
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72: 248-254. PMID: 942051
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 0024119482 scopus 로고
    • Two-dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): Method, reproducibility and genetic aspects
    • PMID: 3250872
    • Gorg A, Postel W, Domscheit A, Gunther S. Two-dimensional electrophoresis with immobilized pH gradients of leaf proteins from barley (Hordeum vulgare): method, reproducibility and genetic aspects. Electrophoresis. 1988; 9: 681-692. PMID: 3250872
    • (1988) Electrophoresis , vol.9 , pp. 681-692
    • Gorg, A.1    Postel, W.2    Domscheit, A.3    Gunther, S.4
  • 38
    • 0031861787 scopus 로고    scopus 로고
    • Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent
    • PMID: 9629925
    • Herbert BR, Molloy MP, Gooley AA, Walsh BJ, Bryson WG, Williams KL. Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent. Electrophoresis. 1998; 19: 845-851. PMID: 9629925
    • (1998) Electrophoresis , vol.19 , pp. 845-851
    • Herbert, B.R.1    Molloy, M.P.2    Gooley, A.A.3    Walsh, B.J.4    Bryson, W.G.5    Williams, K.L.6
  • 40
    • 0034769635 scopus 로고    scopus 로고
    • Proteome analysis applied to meat science: Characterizing postmortem changes in porcine muscle
    • PMID: 11599984
    • Lametsch R, Bendixen E. Proteome analysis applied to meat science: characterizing postmortem changes in porcine muscle. J Agric Food Chem. 2001; 49: 4531-4537. PMID: 11599984
    • (2001) J Agric Food Chem , vol.49 , pp. 4531-4537
    • Lametsch, R.1    Bendixen, E.2
  • 41
    • 45849085174 scopus 로고    scopus 로고
    • In vivo proteome dynamics during early bovine myogenesis
    • PMID: 18924180
    • Chaze T, Meunier B, Chambon C, Jurie C, Picard B. In vivo proteome dynamics during early bovine myogenesis. Proteomics. 2008; 8: 4236-4248. doi: 10.1002/pmic.200701101 PMID: 18924180
    • (2008) Proteomics , vol.8 , pp. 4236-4248
    • Chaze, T.1    Meunier, B.2    Chambon, C.3    Jurie, C.4    Picard, B.5
  • 43
    • 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
    • PMID: 19860418
    • Laville E, Sayd T, Morzel M, Blinet S, Chambon C, Lepetit J, 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. doi: 10.1021/jf901949r PMID: 19860418
    • (2009) J Agric Food Chem , vol.57 , pp. 10755-10764
    • Laville, E.1    Sayd, T.2    Morzel, M.3    Blinet, S.4    Chambon, C.5    Lepetit, J.6
  • 44
    • 84873321291 scopus 로고    scopus 로고
    • Comparison of the longissimus muscle proteome between obese and lean pigs at 180 days
    • PMID: 23160730
    • Li A, Mo D, Zhao X, Jiang W, Cong P, He Z, et al. Comparison of the longissimus muscle proteome between obese and lean pigs at 180 days. Mamm Genome. 2013; 24: 72-79. doi: 10.1007/s00335-012-9440-0 PMID: 23160730
    • (2013) Mamm Genome , vol.24 , pp. 72-79
    • Li, A.1    Mo, D.2    Zhao, X.3    Jiang, W.4    Cong, P.5    He, Z.6
  • 45
    • 0037021624 scopus 로고    scopus 로고
    • Protein extraction from heat-stabilized defatted rice bran.1. Physical processing and enzyme treatments
    • PMID: 12452673
    • Tang S, Hettiarachchy NS, Shellhammer TH. Protein extraction from heat-stabilized defatted rice bran.1. Physical processing and enzyme treatments. J Agric Food Chem. 2002; 50: 7444-7448. PMID: 12452673
    • (2002) J Agric Food Chem , vol.50 , pp. 7444-7448
    • Tang, S.1    Hettiarachchy, N.S.2    Shellhammer, T.H.3
  • 46
    • 34248578524 scopus 로고    scopus 로고
    • Sample preparation for serum/plasma profiling and biomarker identification by mass spectrometry
    • PMID: 17166507
    • Luque-Garcia JL, Neubert TA. Sample preparation for serum/plasma profiling and biomarker identification by mass spectrometry. J Chromatogr A. 2007; 1153: 259-276. PMID: 17166507
    • (2007) J Chromatogr A , vol.1153 , pp. 259-276
    • Luque-Garcia, J.L.1    Neubert, T.A.2
  • 47
    • 34248598796 scopus 로고    scopus 로고
    • Trends in sample preparation for classical and second generation proteomics
    • PMID: 17276441
    • Canas B, Pineiro C, Calvo E, Lopez-Ferrer D, Gallardo JM. Trends in sample preparation for classical and second generation proteomics. J Chromatogr A. 2007; 1153: 235-258. PMID: 17276441
    • (2007) J Chromatogr A , vol.1153 , pp. 235-258
    • Canas, B.1    Pineiro, C.2    Calvo, E.3    Lopez-Ferrer, D.4    Gallardo, J.M.5
  • 48
    • 0000608625 scopus 로고
    • Analysis of Leaf Proteins by Two-Dimensional Gel Electrophoresis: Protease Action as Exemplified by Ribulose Bisphosphate Carboxylase/ Oxygenase Degradation and Procedure to Avoid Proteolysis during Extraction
    • PMID: 16664194
    • Francs CC, Thiellement H, Vienne D. Analysis of Leaf Proteins by Two-Dimensional Gel Electrophoresis: Protease Action as Exemplified by Ribulose Bisphosphate Carboxylase/ Oxygenase Degradation and Procedure to Avoid Proteolysis during Extraction. Plant Physiol. 1985; 78: 178-182. PMID: 16664194
    • (1985) Plant Physiol , vol.78 , pp. 178-182
    • Francs, C.C.1    Thiellement, H.2    Vienne, D.3
  • 49
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: An updated protocol and implications for a functional analysis of the genome
    • PMID: 7498127
    • Klose J, Kobalz U. Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome. Electrophoresis. 1995; 16: 1034-1059. PMID: 7498127
    • (1995) Electrophoresis , vol.16 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 50
    • 0030957650 scopus 로고    scopus 로고
    • Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients
    • Rabilloud T, Adessi C, Giraudel A, Lunardi J. Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis. 2007; 18: 307-316.
    • (2007) Electrophoresis. , vol.18 , pp. 307-316
    • Rabilloud, T.1    Adessi, C.2    Giraudel, A.3    Lunardi, J.4
  • 51
    • 41149084897 scopus 로고    scopus 로고
    • Stain efficiency and MALDI-TOF MS compatibility of seven visible staining procedures
    • PMID: 18283439
    • Lin JF, Chen QX, Tian HY, Gao X, Yu ML, Xu G, et al. Stain efficiency and MALDI-TOF MS compatibility of seven visible staining procedures. Anal Bioanal Chem. 2008; 390: 1765-1773. doi: 10.1007/s00216-008-1910-6 PMID: 18283439
    • (2008) Anal Bioanal Chem , vol.390 , pp. 1765-1773
    • Lin, J.F.1    Chen, Q.X.2    Tian, H.Y.3    Gao, X.4    Yu, M.L.5    Xu, G.6
  • 52
    • 84856106493 scopus 로고    scopus 로고
    • Polar electrophoresis: Shape of two-dimensional maps is as important as size
    • PMID: 22292075
    • Millioni R, Polati R, Menini M, Puricelli L, Miuzzo M, Tessari P, et al. Polar electrophoresis: shape of two-dimensional maps is as important as size. PLoS One. 2012; 7: e30911. doi: 10.1371/journal.pone.0030911 PMID: 22292075
    • (2012) PLoS One , vol.7 , pp. e30911
    • Millioni, R.1    Polati, R.2    Menini, M.3    Puricelli, L.4    Miuzzo, M.5    Tessari, P.6
  • 53
    • 83755192039 scopus 로고    scopus 로고
    • Skeletal muscle proteomics: Current approaches, technical challenges and emerging techniques
    • Available PMID: 21798084
    • Ohlendieck K. Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques. Skelet Muscle. 2011; 1: 6. Available: http://www.skeletalmusclejournal.com/content/1/1/6. doi: 10.1186/2044-5040-1-6 PMID: 21798084
    • (2011) Skelet Muscle , vol.1 , pp. 6
    • Ohlendieck, K.1
  • 54
    • 34047161584 scopus 로고    scopus 로고
    • Improvements in the search for potential biomarkers by proteomics: Application of principal component and discriminant analyses for two-dimensional maps evaluation
    • PMID: 17071145
    • Rodriguez-Pineiro AM, Rodriguez-Berrocal FJ, Paez de la Cadena M. Improvements in the search for potential biomarkers by proteomics: application of principal component and discriminant analyses for two-dimensional maps evaluation. J Chromatogr B Analyt Technol Biomed Life Sci. 2007; 849: 251-260. PMID: 17071145
    • (2007) J Chromatogr B Analyt Technol Biomed Life Sci , vol.849 , pp. 251-260
    • Rodriguez-Pineiro, A.M.1    Rodriguez-Berrocal, F.J.2    Paez De La Cadena, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.