메뉴 건너뛰기




Volumn 82, Issue , 2013, Pages 166-178

Optimized proteomic analysis of rat liver microsomes using dual enzyme digestion with 2D-LC-MS/MS

Author keywords

Dual enzyme digestion; Membrane proteins; Quadrupole time of flight (QqTOF); Rat liver microsomes; Solubilizing agents; Strong cation exchange

Indexed keywords

MEMBRANE PROTEIN; PEPSIN A; TRYPSIN;

EID: 84875764594     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.02.001     Document Type: Article
Times cited : (14)

References (54)
  • 3
    • 79960989340 scopus 로고    scopus 로고
    • Challenges and solutions for the identification of membrane proteins in non-model plants
    • Vertommen A., Panis B., Swennen R., Carpentier S.C. Challenges and solutions for the identification of membrane proteins in non-model plants. J Proteomics 2011, 74:1165-1181.
    • (2011) J Proteomics , vol.74 , pp. 1165-1181
    • Vertommen, A.1    Panis, B.2    Swennen, R.3    Carpentier, S.C.4
  • 4
    • 79961180436 scopus 로고    scopus 로고
    • Triton X-114 phase separation in the isolation and purification of mouse liver microsomal membrane proteins
    • Mathias R.A., Chen Y.-S., Kapp E.A., Greening D.W., Mathivanan S., Simpson R.J. Triton X-114 phase separation in the isolation and purification of mouse liver microsomal membrane proteins. Methods 2011, 54:396-406.
    • (2011) Methods , vol.54 , pp. 396-406
    • Mathias, R.A.1    Chen, Y.-S.2    Kapp, E.A.3    Greening, D.W.4    Mathivanan, S.5    Simpson, R.J.6
  • 5
    • 33749234216 scopus 로고    scopus 로고
    • Drugs, their targets and the nature and number of drug targets
    • Imming P., Sinning C., Meyer A. Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov 2006, 5:821-834.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 821-834
    • Imming, P.1    Sinning, C.2    Meyer, A.3
  • 6
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins - theory and application
    • Speers A.E., Wu C.C. Proteomics of integral membrane proteins - theory and application. Chem Rev 2007, 107:3687-3714.
    • (2007) Chem Rev , vol.107 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 7
    • 77957232334 scopus 로고    scopus 로고
    • Advances in shotgun proteomics and the analysis of membrane proteomes
    • Gilmore J.M., Washburn M.P. Advances in shotgun proteomics and the analysis of membrane proteomes. J Proteomics 2010, 73:2078-2091.
    • (2010) J Proteomics , vol.73 , pp. 2078-2091
    • Gilmore, J.M.1    Washburn, M.P.2
  • 9
    • 81055140642 scopus 로고    scopus 로고
    • Quantitative shot-gun proteomics and MS-based activity assay for revealing gender differences in enzyme contents for rat liver microsome
    • Huang H.-J., Tsai M.-L., Chen Y.-W., Chen S.-H. Quantitative shot-gun proteomics and MS-based activity assay for revealing gender differences in enzyme contents for rat liver microsome. J Proteomics 2011, 74:2734-2744.
    • (2011) J Proteomics , vol.74 , pp. 2734-2744
    • Huang, H.-J.1    Tsai, M.-L.2    Chen, Y.-W.3    Chen, S.-H.4
  • 10
    • 0035987523 scopus 로고    scopus 로고
    • Comparison of one-dimensional and two-dimensional gel electrophoresis as a separation tool for proteomic analysis of rat liver microsomes: cytochromes P450 and other membrane proteins
    • Galeva N., Altermann M. Comparison of one-dimensional and two-dimensional gel electrophoresis as a separation tool for proteomic analysis of rat liver microsomes: cytochromes P450 and other membrane proteins. Proteomics 2002, 2:713-722.
    • (2002) Proteomics , vol.2 , pp. 713-722
    • Galeva, N.1    Altermann, M.2
  • 11
    • 0037377939 scopus 로고    scopus 로고
    • Direct identification of cytochrome P450 isozymes by matrix-assisted laser desorption/ionization time of flight-based proteomic approach
    • Galeva N., Yakovlev D., Koen Y., Duzhak T., Alterman M. Direct identification of cytochrome P450 isozymes by matrix-assisted laser desorption/ionization time of flight-based proteomic approach. Drug Metab Dispos 2003, 31:351-355.
    • (2003) Drug Metab Dispos , vol.31 , pp. 351-355
    • Galeva, N.1    Yakovlev, D.2    Koen, Y.3    Duzhak, T.4    Alterman, M.5
  • 12
    • 4444368605 scopus 로고    scopus 로고
    • Fast proteolytic digestion coupled with organelle enrichment for proteomic analysis of rat liver
    • Arnold R.J., Hrncirova P., Annaiah K., Novotny M.V. Fast proteolytic digestion coupled with organelle enrichment for proteomic analysis of rat liver. J Proteome Res 2004, 3:653-657.
    • (2004) J Proteome Res , vol.3 , pp. 653-657
    • Arnold, R.J.1    Hrncirova, P.2    Annaiah, K.3    Novotny, M.V.4
  • 13
    • 1842536853 scopus 로고    scopus 로고
    • A proteomic approach to the identification of cytochrome P450 isoforms in male and female rat liver by nanoscale liquid chromatography-electrospray ionization-tandem mass spectrometry
    • Nisar S., Lane C.S., Wilderspin A.F., Welham K.J., Griffiths W.J., Patterson L.H. A proteomic approach to the identification of cytochrome P450 isoforms in male and female rat liver by nanoscale liquid chromatography-electrospray ionization-tandem mass spectrometry. Drug Metab Dispos 2004, 32:382-386.
    • (2004) Drug Metab Dispos , vol.32 , pp. 382-386
    • Nisar, S.1    Lane, C.S.2    Wilderspin, A.F.3    Welham, K.J.4    Griffiths, W.J.5    Patterson, L.H.6
  • 16
    • 84874744352 scopus 로고    scopus 로고
    • Proteomic and bioinformatics analyses of mouse liver microsomes
    • Peng F., Zhan X., Li M.-Y., Fang F., Li G., Li C., et al. Proteomic and bioinformatics analyses of mouse liver microsomes. Int J Proteomics 2012, 2012:832569.
    • (2012) Int J Proteomics , vol.2012 , pp. 832569
    • Peng, F.1    Zhan, X.2    Li, M.-Y.3    Fang, F.4    Li, G.5    Li, C.6
  • 17
    • 65249099037 scopus 로고    scopus 로고
    • Multiple-approaches to the identification and quantification of cytochromes P450 in human liver tissue by mass spectrometry
    • Seibert C., Davidson B.R., Fuller B.J., Patterson L.H., Griffiths W.J., Wang Y. Multiple-approaches to the identification and quantification of cytochromes P450 in human liver tissue by mass spectrometry. J Proteome Res 2009, 8:1672-1681.
    • (2009) J Proteome Res , vol.8 , pp. 1672-1681
    • Seibert, C.1    Davidson, B.R.2    Fuller, B.J.3    Patterson, L.H.4    Griffiths, W.J.5    Wang, Y.6
  • 19
    • 84862154112 scopus 로고    scopus 로고
    • Glutathione S-transferase pi trapping method for generation and characterization of drug-protein adducts in human liver microsomes using liquid chromatography-tandem mass spectrometry
    • Yukinaga H., Iwabuchi H., Okazaki O., Izumi T. Glutathione S-transferase pi trapping method for generation and characterization of drug-protein adducts in human liver microsomes using liquid chromatography-tandem mass spectrometry. J Pharm Biomed Anal 2012, 67-68:186-192.
    • (2012) J Pharm Biomed Anal , pp. 186-192
    • Yukinaga, H.1    Iwabuchi, H.2    Okazaki, O.3    Izumi, T.4
  • 20
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 21
    • 17244383269 scopus 로고    scopus 로고
    • 2D-LC/MS techniques for the identification of proteins in highly complex mixtures
    • Nägele E., Vollmer M., Hörth P., Vad C. 2D-LC/MS techniques for the identification of proteins in highly complex mixtures. Expert Rev Proteomics 2004, 1:37-46.
    • (2004) Expert Rev Proteomics , vol.1 , pp. 37-46
    • Nägele, E.1    Vollmer, M.2    Hörth, P.3    Vad, C.4
  • 23
    • 77955876447 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in cell biology
    • Walther T.C., Mann M. Mass spectrometry-based proteomics in cell biology. J Cell Biol 2010, 190:491-500.
    • (2010) J Cell Biol , vol.190 , pp. 491-500
    • Walther, T.C.1    Mann, M.2
  • 24
    • 84863863406 scopus 로고    scopus 로고
    • Time-of-flight mass spectrometry versus orbitrap-based mass spectrometry for the screening and identification of drugs and metabolites: is there a winner?
    • Eichhorn P., Pérez S., Barceló D. Time-of-flight mass spectrometry versus orbitrap-based mass spectrometry for the screening and identification of drugs and metabolites: is there a winner?. Compr Anal Chem 2012, 58:217-272.
    • (2012) Compr Anal Chem , vol.58 , pp. 217-272
    • Eichhorn, P.1    Pérez, S.2    Barceló, D.3
  • 25
    • 79953192195 scopus 로고    scopus 로고
    • Overcoming key technological challenges in using mass spectrometry for mapping cell surfaces in tissues
    • [R110.000935]
    • Griffin N.M., Schnitzer J.E. Overcoming key technological challenges in using mass spectrometry for mapping cell surfaces in tissues. Mol Cell Proteomics 2011, 10. [R110.000935].
    • (2011) Mol Cell Proteomics , vol.10
    • Griffin, N.M.1    Schnitzer, J.E.2
  • 26
    • 79551524680 scopus 로고    scopus 로고
    • High-performance liquid chromatography separation and intact mass analysis of detergent-solubilized integral membrane proteins
    • Berridge G., Chalk R., D'Avanzo N., Dong L., Doyle D., Kim J.-I., et al. High-performance liquid chromatography separation and intact mass analysis of detergent-solubilized integral membrane proteins. Anal Biochem 2011, 410:272-280.
    • (2011) Anal Biochem , vol.410 , pp. 272-280
    • Berridge, G.1    Chalk, R.2    D'Avanzo, N.3    Dong, L.4    Doyle, D.5    Kim, J.-I.6
  • 27
    • 34547232157 scopus 로고    scopus 로고
    • Optimization of mass spectrometry-compatible surfactants for shotgun proteomics
    • Chen E.I., Cociorva D., Norris J.L., Yates J.R. Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. J Proteome Res 2007, 6:2529-2538.
    • (2007) J Proteome Res , vol.6 , pp. 2529-2538
    • Chen, E.I.1    Cociorva, D.2    Norris, J.L.3    Yates, J.R.4
  • 28
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • Le Maire M., Champeil P., Moller J.V. Interaction of membrane proteins and lipids with solubilizing detergents. Biochim Biophys Acta 2000, 1508:86-111.
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 29
    • 0242291099 scopus 로고    scopus 로고
    • Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins
    • Yu Y., Gilar M., Lee P.J., Bouvier E.S.P., Gebler J.C. Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Anal Chem 2003, 75:6023-6028.
    • (2003) Anal Chem , vol.75 , pp. 6023-6028
    • Yu, Y.1    Gilar, M.2    Lee, P.J.3    Bouvier, E.S.P.4    Gebler, J.C.5
  • 31
    • 4444320836 scopus 로고    scopus 로고
    • Proteolysis and mass spectrometric analysis of an integral membrane: aquaporin 0
    • Han J., Schey K.L. Proteolysis and mass spectrometric analysis of an integral membrane: aquaporin 0. J Proteome Res 2004, 3:807-812.
    • (2004) J Proteome Res , vol.3 , pp. 807-812
    • Han, J.1    Schey, K.L.2
  • 32
    • 84855877960 scopus 로고    scopus 로고
    • Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics
    • Burkhart J.M., Schumbrutzki C., Wortelkamp S., Sickmann A., Zahedi R.P. Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics. J Proteomics 2012, 75:1454-1462.
    • (2012) J Proteomics , vol.75 , pp. 1454-1462
    • Burkhart, J.M.1    Schumbrutzki, C.2    Wortelkamp, S.3    Sickmann, A.4    Zahedi, R.P.5
  • 33
    • 33646557331 scopus 로고    scopus 로고
    • Protein cleavage strategies for an improved analysis of the membrane proteome
    • Fischer F., Poetsch A. Protein cleavage strategies for an improved analysis of the membrane proteome. Proteome Sci 2006, 4:2.
    • (2006) Proteome Sci , vol.4 , pp. 2
    • Fischer, F.1    Poetsch, A.2
  • 34
    • 0034908275 scopus 로고    scopus 로고
    • Botulinum neurotoxin types B and E: purification, limited proteolysis by endoproteinase Glu-C and pepsin, and comparison of their identified cleaved sites relative to the three-dimensional structure of type A neurotoxin
    • Prabakaran S., Tepp W., Dasgupta B.R. Botulinum neurotoxin types B and E: purification, limited proteolysis by endoproteinase Glu-C and pepsin, and comparison of their identified cleaved sites relative to the three-dimensional structure of type A neurotoxin. Toxicon 2001, 39:1515-1531.
    • (2001) Toxicon , vol.39 , pp. 1515-1531
    • Prabakaran, S.1    Tepp, W.2    Dasgupta, B.R.3
  • 35
    • 33747177566 scopus 로고    scopus 로고
    • A targeted proteomic approach for the analysis of rat liver mitochondrial outer membrane proteins with extensive sequence coverage
    • Distler A.M., Kerner J., Peterman S.M., Hoppel C.L. A targeted proteomic approach for the analysis of rat liver mitochondrial outer membrane proteins with extensive sequence coverage. Anal Biochem 2006, 356:18-29.
    • (2006) Anal Biochem , vol.356 , pp. 18-29
    • Distler, A.M.1    Kerner, J.2    Peterman, S.M.3    Hoppel, C.L.4
  • 36
    • 1842833112 scopus 로고    scopus 로고
    • Mapping of protein phosphorylation by dual enzyme digestion and matrix-assisted laser desorption ionization-quadrupole orthogonal time-of-flight mass spectrometry
    • Han J., Pope M., Borchers C., Graves L.M. Mapping of protein phosphorylation by dual enzyme digestion and matrix-assisted laser desorption ionization-quadrupole orthogonal time-of-flight mass spectrometry. Anal Biochem 2002, 310:215-218.
    • (2002) Anal Biochem , vol.310 , pp. 215-218
    • Han, J.1    Pope, M.2    Borchers, C.3    Graves, L.M.4
  • 37
    • 0037056021 scopus 로고    scopus 로고
    • Combined in-gel tryptic digestion and CNBr cleavage for the generation of peptide maps of an integral membrane protein with MALDI-TOF mass spectrometry
    • Van Montfort B.A., Doeven M.K., Canas B., Veenhoff L.M., Poolman B., Robillard G.T. Combined in-gel tryptic digestion and CNBr cleavage for the generation of peptide maps of an integral membrane protein with MALDI-TOF mass spectrometry. Biochim Biophys Acta 2002, 1555:111-115.
    • (2002) Biochim Biophys Acta , vol.1555 , pp. 111-115
    • Van Montfort, B.A.1    Doeven, M.K.2    Canas, B.3    Veenhoff, L.M.4    Poolman, B.5    Robillard, G.T.6
  • 38
    • 34347234182 scopus 로고    scopus 로고
    • Shotgun analysis of integral membrane proteins facilitated by elevated temperature
    • Speers A.E., Blackler A.R., Wu C.C. Shotgun analysis of integral membrane proteins facilitated by elevated temperature. Anal Chem 2007, 79:4613-4620.
    • (2007) Anal Chem , vol.79 , pp. 4613-4620
    • Speers, A.E.1    Blackler, A.R.2    Wu, C.C.3
  • 39
    • 33644854651 scopus 로고    scopus 로고
    • Selenium bioaccessibility assessment in selenized yeast after "in vitro" gastrointestinal digestion using two-dimensional chromatography and mass spectrometry
    • Reyes L.H., Encinar J.R., Marchante-Gayón J.M., Alonso J.I.G., Sanz-Medel A. Selenium bioaccessibility assessment in selenized yeast after "in vitro" gastrointestinal digestion using two-dimensional chromatography and mass spectrometry. J Chromatogr A 2006, 1110:108-116.
    • (2006) J Chromatogr A , vol.1110 , pp. 108-116
    • Reyes, L.H.1    Encinar, J.R.2    Marchante-Gayón, J.M.3    Alonso, J.I.G.4    Sanz-Medel, A.5
  • 40
    • 79951764344 scopus 로고    scopus 로고
    • Investigation of solubilization and digestion methods for microsomal membrane proteome analysis using data-independent LC-MSE
    • Mbeunkui F., Goshe M.B. Investigation of solubilization and digestion methods for microsomal membrane proteome analysis using data-independent LC-MSE. Proteomics 2011, 11:898-911.
    • (2011) Proteomics , vol.11 , pp. 898-911
    • Mbeunkui, F.1    Goshe, M.B.2
  • 41
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov I.V., Seymour S.L., Patel A.A., Loboda A., Tang W.H., Keating S.P., et al. The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol Cell Proteomics 2007, 6:1638-1655.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6
  • 42
    • 55249121202 scopus 로고    scopus 로고
    • Nonlinear fitting method for determining local false discovery rates from decoy database searches
    • Tang W.H., Shilov I.V., Seymour S.L. Nonlinear fitting method for determining local false discovery rates from decoy database searches. J Proteome Res 2008, 7:3661-3667.
    • (2008) J Proteome Res , vol.7 , pp. 3661-3667
    • Tang, W.H.1    Shilov, I.V.2    Seymour, S.L.3
  • 44
    • 0037249501 scopus 로고    scopus 로고
    • PANTHER: a browsable database of gene products organized by biological function, using curated protein family and subfamily classification
    • Thomas P.D., Kejariwal A., Campbell M.J., Mi H., Diemer K., Guo N., et al. PANTHER: a browsable database of gene products organized by biological function, using curated protein family and subfamily classification. Nucleic Acids Res 2003, 31:334-341.
    • (2003) Nucleic Acids Res , vol.31 , pp. 334-341
    • Thomas, P.D.1    Kejariwal, A.2    Campbell, M.J.3    Mi, H.4    Diemer, K.5    Guo, N.6
  • 45
    • 51049113607 scopus 로고    scopus 로고
    • InnateDB: facilitating systems-level analyses of the mammalian innate immune response
    • Lynn D.J., Winsor G.L., Chan C., Richard N., Laird M.R., Barsky A., et al. InnateDB: facilitating systems-level analyses of the mammalian innate immune response. Mol Syst Biol 2008, 4:218.
    • (2008) Mol Syst Biol , vol.4 , pp. 218
    • Lynn, D.J.1    Winsor, G.L.2    Chan, C.3    Richard, N.4    Laird, M.R.5    Barsky, A.6
  • 46
    • 34249751614 scopus 로고    scopus 로고
    • Cerebral: a Cytoscape plugin for layout of and interaction with biological networks using subcellular localization annotation
    • Barsky A., Gardy J.L., Hancock R.E.W., Munzner T. Cerebral: a Cytoscape plugin for layout of and interaction with biological networks using subcellular localization annotation. Bioinformatics 2007, 23:1040-1042.
    • (2007) Bioinformatics , vol.23 , pp. 1040-1042
    • Barsky, A.1    Gardy, J.L.2    Hancock, R.E.W.3    Munzner, T.4
  • 47
    • 0036846006 scopus 로고    scopus 로고
    • Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases
    • Del Vecchio P., Graziano G., Granata V., Barone G., Mandrich L., Rossi M., et al. Denaturing action of urea and guanidine hydrochloride towards two thermophilic esterases. Biochem J 2002, 367:857-863.
    • (2002) Biochem J , vol.367 , pp. 857-863
    • Del Vecchio, P.1    Graziano, G.2    Granata, V.3    Barone, G.4    Mandrich, L.5    Rossi, M.6
  • 48
    • 0942276251 scopus 로고    scopus 로고
    • A detergent- and cyanogen bromide-free method for integral membrane proteomics: application to Halobacterium purple membranes and the human epidermal membrane proteome
    • Blonder J., Conrads T.P., Yu L.-R., Terunuma A., Janini G.M., Issaq H.J., et al. A detergent- and cyanogen bromide-free method for integral membrane proteomics: application to Halobacterium purple membranes and the human epidermal membrane proteome. Proteomics 2004, 4:31-45.
    • (2004) Proteomics , vol.4 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.-R.3    Terunuma, A.4    Janini, G.M.5    Issaq, H.J.6
  • 49
    • 70349991237 scopus 로고    scopus 로고
    • Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS/MS
    • Ye X., Johann D.J., Hakami R.M., Xiao Z., Meng Z., Ulrich R.G., et al. Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS/MS. J Proteomics 2009, 73:112-122.
    • (2009) J Proteomics , vol.73 , pp. 112-122
    • Ye, X.1    Johann, D.J.2    Hakami, R.M.3    Xiao, Z.4    Meng, Z.5    Ulrich, R.G.6
  • 50
    • 34547584314 scopus 로고    scopus 로고
    • Advantages of combined transmembrane topology and signal peptide prediction - the Phobius web server
    • Krogh A., Sonnhammer E.L.L., Käll L. Advantages of combined transmembrane topology and signal peptide prediction - the Phobius web server. Nucleic Acids Res 2007, 35:429-432.
    • (2007) Nucleic Acids Res , vol.35 , pp. 429-432
    • Krogh, A.1    Sonnhammer, E.L.L.2    Käll, L.3
  • 51
    • 84864560730 scopus 로고    scopus 로고
    • A guideline to proteome-wide α-helical membrane protein topology predictions
    • Tsirigos K.D., Hennerdal A., Käll L., Elofsson A. A guideline to proteome-wide α-helical membrane protein topology predictions. Proteomics 2012, 12:2282-2294.
    • (2012) Proteomics , vol.12 , pp. 2282-2294
    • Tsirigos, K.D.1    Hennerdal, A.2    Käll, L.3    Elofsson, A.4
  • 52
    • 84924149446 scopus 로고    scopus 로고
    • Cambridge University Press, New York, USA
    • Xiong J. Essential Bioinformatics 2006, Cambridge University Press, New York, USA.
    • (2006) Essential Bioinformatics
    • Xiong, J.1
  • 54
    • 41149161152 scopus 로고    scopus 로고
    • Gel-eluted liquid fraction entrapment electrophoresis: an electrophoretic method for broad molecular weight range proteome separation
    • Tran J.C., Doucette A.A. Gel-eluted liquid fraction entrapment electrophoresis: an electrophoretic method for broad molecular weight range proteome separation. Anal Chem 2008, 80:1568-1573.
    • (2008) Anal Chem , vol.80 , pp. 1568-1573
    • Tran, J.C.1    Doucette, A.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.