메뉴 건너뛰기




Volumn 1476, Issue , 2016, Pages 1-8

Characterization of an immobilized enzyme reactor for on-line protein digestion

Author keywords

Digestion; IMER; Immobilized enzyme; Membrane proteins; Trypsin

Indexed keywords

BIOLOGICAL MEMBRANES; BIOREACTORS; ENZYMES; LIQUID CHROMATOGRAPHY; SLUDGE DIGESTION; YEAST;

EID: 84998693345     PISSN: 00219673     EISSN: 18733778     Source Type: Journal    
DOI: 10.1016/j.chroma.2016.11.021     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: new technologies, new concepts, and new words
    • [1] Anderson, N., Anderson, N., Proteome and proteomics: new technologies, new concepts, and new words. Electrophoresis 19 (1998), 1853–1861.
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.1    Anderson, N.2
  • 2
    • 77954512738 scopus 로고    scopus 로고
    • Proteomics retrenches
    • [2] Mitchell, P., Proteomics retrenches. Nat. Biotechnol. 28 (2010), 665–670.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 665-670
    • Mitchell, P.1
  • 6
    • 57649089547 scopus 로고    scopus 로고
    • Recent advances in immobilized enzymatic reactors and their applications in proteome analysis
    • [6] Ma, J., Zhang, L., Liang, Z., Zhang, W., Zhang, Y., Recent advances in immobilized enzymatic reactors and their applications in proteome analysis. Anal. Chim. Acta 632 (2009), 1–8.
    • (2009) Anal. Chim. Acta , vol.632 , pp. 1-8
    • Ma, J.1    Zhang, L.2    Liang, Z.3    Zhang, W.4    Zhang, Y.5
  • 7
    • 84913532579 scopus 로고    scopus 로고
    • Accelerating trypsin digestion: the immobilized enzyme reactor
    • [7] Regnier, F., Kim, J., Accelerating trypsin digestion: the immobilized enzyme reactor. Bioanalysis 6 (2014), 2685–2698.
    • (2014) Bioanalysis , vol.6 , pp. 2685-2698
    • Regnier, F.1    Kim, J.2
  • 8
    • 0035356224 scopus 로고    scopus 로고
    • Integrated microfluidic system enabling protein digestion, peptide separation, and protein identification
    • [8] Gao, J., Xu, J., Locascio, L., Lee, C., Integrated microfluidic system enabling protein digestion, peptide separation, and protein identification. Anal. Chem. 73 (2001), 2648–2655.
    • (2001) Anal. Chem. , vol.73 , pp. 2648-2655
    • Gao, J.1    Xu, J.2    Locascio, L.3    Lee, C.4
  • 9
    • 1942454733 scopus 로고    scopus 로고
    • Integrated and ultrasensitive gel protein identification
    • [9] Cooper, J., Lee, C., Integrated and ultrasensitive gel protein identification. Anal. Chem 76 (2004), 2196–2202.
    • (2004) Anal. Chem , vol.76 , pp. 2196-2202
    • Cooper, J.1    Lee, C.2
  • 10
    • 0037355581 scopus 로고    scopus 로고
    • Membrane-based nanoscale proteolytic reactor enabling protein digestion, peptide separation, and protein identification using mass spectrometry
    • [10] Cooper, J., Chen, J., Li, Y., Lee, C., Membrane-based nanoscale proteolytic reactor enabling protein digestion, peptide separation, and protein identification using mass spectrometry. Anal. Chem. 75 (2003), 1067–1074.
    • (2003) Anal. Chem. , vol.75 , pp. 1067-1074
    • Cooper, J.1    Chen, J.2    Li, Y.3    Lee, C.4
  • 12
    • 84922706932 scopus 로고    scopus 로고
    • Fabrication of an on-line enzyme micro-reactor coupled to liquid chromatography-tandem mass spectrometry for the digestion of recombinant human erythropoietin
    • [12] Foo, H., Smith, N., Stanley, S., Fabrication of an on-line enzyme micro-reactor coupled to liquid chromatography-tandem mass spectrometry for the digestion of recombinant human erythropoietin. Talanta 135 (2015), 18–22.
    • (2015) Talanta , vol.135 , pp. 18-22
    • Foo, H.1    Smith, N.2    Stanley, S.3
  • 13
    • 84907153239 scopus 로고    scopus 로고
    • Open tubular lab-on-column/mass spectrometry for targeted proteomics of nanogram sample amounts
    • [13] Hustoft, H., Vehus, T., Brandtzaeg, O., Krauss, S., Greibrokk, T., Wilson, S., Lundanes, E., Open tubular lab-on-column/mass spectrometry for targeted proteomics of nanogram sample amounts. PLoS One 9 (2014), 1–10.
    • (2014) PLoS One , vol.9 , pp. 1-10
    • Hustoft, H.1    Vehus, T.2    Brandtzaeg, O.3    Krauss, S.4    Greibrokk, T.5    Wilson, S.6    Lundanes, E.7
  • 15
    • 0033868723 scopus 로고    scopus 로고
    • Integration of immobilized trypsin bead beds for protein digestion within a microfluidic chip incorporating capillary electrophoresis separations and an electrospray mass spectrometry interface
    • [15] Wang, C., Oleschuk, R., Ouchen, F., Li, J., Thibault, P., Harrison, D., Integration of immobilized trypsin bead beds for protein digestion within a microfluidic chip incorporating capillary electrophoresis separations and an electrospray mass spectrometry interface. Rapid Commun. Mass Spectrom. 14 (2000), 1377–1383.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1377-1383
    • Wang, C.1    Oleschuk, R.2    Ouchen, F.3    Li, J.4    Thibault, P.5    Harrison, D.6
  • 16
    • 0034650858 scopus 로고    scopus 로고
    • Integrated microanalytical technology enabling rapid and automated protein identification
    • [16] Ekstrom, S., Onnerfjord, P., Nilsson, J., Bengtsson, M., Laurell, T., Marko-Varga, G., Integrated microanalytical technology enabling rapid and automated protein identification. Anal. Chem. 72 (2000), 286–293.
    • (2000) Anal. Chem. , vol.72 , pp. 286-293
    • Ekstrom, S.1    Onnerfjord, P.2    Nilsson, J.3    Bengtsson, M.4    Laurell, T.5    Marko-Varga, G.6
  • 17
    • 15444373422 scopus 로고    scopus 로고
    • Monolithic bioreactor immobilizing trypsin for high-throughput analysis
    • [17] Kato, M., Inuzuka, K., Sakai-Kato, K., Toyo'oka, T., Monolithic bioreactor immobilizing trypsin for high-throughput analysis. Anal. Chem. 77 (2005), 1813–1818.
    • (2005) Anal. Chem. , vol.77 , pp. 1813-1818
    • Kato, M.1    Inuzuka, K.2    Sakai-Kato, K.3    Toyo'oka, T.4
  • 18
    • 7644236036 scopus 로고    scopus 로고
    • Stable microstructured network for protein patterning on a plastic microfluidic channel: strategy and characterization of on-chip enzyme microreactors
    • [18] Qu, H., Wang, H., Huang, Y., Zhong, W., Lu, H., Kong, J., Yang, P., Liu, B., Stable microstructured network for protein patterning on a plastic microfluidic channel: strategy and characterization of on-chip enzyme microreactors. Anal. Chem. 76 (2004), 6426–6433.
    • (2004) Anal. Chem. , vol.76 , pp. 6426-6433
    • Qu, H.1    Wang, H.2    Huang, Y.3    Zhong, W.4    Lu, H.5    Kong, J.6    Yang, P.7    Liu, B.8
  • 19
    • 69249125736 scopus 로고    scopus 로고
    • Overview on modern approaches to speed up protein identification workflows relying on enzymatic cleavage and mass spectrometry-based techniques
    • [19] Capelo, J., Carreira, R., Diniz, M., Fernandes, L., Galesio, M., Lodeiro, C., Santos, H., Vale, G., Overview on modern approaches to speed up protein identification workflows relying on enzymatic cleavage and mass spectrometry-based techniques. Anal. Chim. Acta 650 (2009), 151–159.
    • (2009) Anal. Chim. Acta , vol.650 , pp. 151-159
    • Capelo, J.1    Carreira, R.2    Diniz, M.3    Fernandes, L.4    Galesio, M.5    Lodeiro, C.6    Santos, H.7    Vale, G.8
  • 20
    • 31344455021 scopus 로고    scopus 로고
    • Rapid protein digestion and identification using monolithic enzymatic microreactor coupled with nano-liquid chromatography-electrospray ionization mass spectrometry
    • [20] Duan, J., Sun, L., Liang, Z., Zhang, J., Wang, H., Zhang, L., Zhang, W., Zhang, Y., Rapid protein digestion and identification using monolithic enzymatic microreactor coupled with nano-liquid chromatography-electrospray ionization mass spectrometry. J. Chrom. A 1106 (2006), 165–174.
    • (2006) J. Chrom. A , vol.1106 , pp. 165-174
    • Duan, J.1    Sun, L.2    Liang, Z.3    Zhang, J.4    Wang, H.5    Zhang, L.6    Zhang, W.7    Zhang, Y.8
  • 21
    • 32344448186 scopus 로고    scopus 로고
    • Coupling the immobilized trypsin microreactor of monolithic capillary with μRPLC–MS/MS for shotgun proteome analysis
    • [21] Feng, S., Ye, M., Jiang, X., Jin, W., Zou, H., Coupling the immobilized trypsin microreactor of monolithic capillary with μRPLC–MS/MS for shotgun proteome analysis. J. Proteome Res. 5 (2006), 422–428.
    • (2006) J. Proteome Res. , vol.5 , pp. 422-428
    • Feng, S.1    Ye, M.2    Jiang, X.3    Jin, W.4    Zou, H.5
  • 22
    • 84867858439 scopus 로고    scopus 로고
    • Protein analysis using a combination of an on-line monolithic trypsin immobilized enzyme reactor and collisionally-activated dissociation/electron transfer dissociation dual tandem mass spectrometry
    • [22] Hwang, H., Cho, K., Kim, J., Kim, Y., Oh, H., Protein analysis using a combination of an on-line monolithic trypsin immobilized enzyme reactor and collisionally-activated dissociation/electron transfer dissociation dual tandem mass spectrometry. Bull. Kor. Chem. Soc. 33 (2012), 3233–3240.
    • (2012) Bull. Kor. Chem. Soc. , vol.33 , pp. 3233-3240
    • Hwang, H.1    Cho, K.2    Kim, J.3    Kim, Y.4    Oh, H.5
  • 23
    • 64749088652 scopus 로고    scopus 로고
    • Highly efficient enzyme reactors containing trypsin and endoproteinase LysC immobilized on porous polymer monolith coupled to MS suitable for analysis of antibodies
    • [23] Krenkova, J., Lacher, N., Svec, F., Highly efficient enzyme reactors containing trypsin and endoproteinase LysC immobilized on porous polymer monolith coupled to MS suitable for analysis of antibodies. Anal. Chem. 81 (2009), 2004–2012.
    • (2009) Anal. Chem. , vol.81 , pp. 2004-2012
    • Krenkova, J.1    Lacher, N.2    Svec, F.3
  • 24
    • 84902549172 scopus 로고    scopus 로고
    • Capillary electrophoresis-based immobilized enzyme reactor using particle-packing technique
    • [24] Liu, L., Zhang, B., Zhang, Q., Shi, Y., Guo, L., Yang, L., Capillary electrophoresis-based immobilized enzyme reactor using particle-packing technique. J. Chromatogr. A 1352 (2014), 80–86.
    • (2014) J. Chromatogr. A , vol.1352 , pp. 80-86
    • Liu, L.1    Zhang, B.2    Zhang, Q.3    Shi, Y.4    Guo, L.5    Yang, L.6
  • 25
    • 33747202736 scopus 로고    scopus 로고
    • Detection and identification of sub-nanogram levels of protein in a nanoLC-trypsin-MS system
    • [25] Slysz, G., Lewis, D., Schriemer, D., Detection and identification of sub-nanogram levels of protein in a nanoLC-trypsin-MS system. J. Proteome Res. 5 (2006), 1959–1966.
    • (2006) J. Proteome Res. , vol.5 , pp. 1959-1966
    • Slysz, G.1    Lewis, D.2    Schriemer, D.3
  • 26
    • 84864153271 scopus 로고    scopus 로고
    • Nano-flow multidimensional liquid chromatography platform integrated with combination of protein and peptide separation for proteome analysis
    • [26] Xia, S., Tao, D., Yuan, H., Zhou, Y., Liang, Z., Zhang, L., Zhang, Y., Nano-flow multidimensional liquid chromatography platform integrated with combination of protein and peptide separation for proteome analysis. J. Sep. Sci. 35 (2012), 1764–1770.
    • (2012) J. Sep. Sci. , vol.35 , pp. 1764-1770
    • Xia, S.1    Tao, D.2    Yuan, H.3    Zhou, Y.4    Liang, Z.5    Zhang, L.6    Zhang, Y.7
  • 27
    • 0017222264 scopus 로고
    • Immobilized-enzyme reactors
    • Elsevier Science & Technology: On-line
    • [27] Lilly, M., Dunnill, P., Immobilized-enzyme reactors. Methods in Enzymology, Vol. 44, 1976, Elsevier Science & Technology: On-line, 717–738.
    • (1976) Methods in Enzymology , vol.44 , pp. 717-738
    • Lilly, M.1    Dunnill, P.2
  • 28
    • 70350648825 scopus 로고    scopus 로고
    • Integrated platform for proteome analysis with combination of protein and peptide separation via on-line digestion
    • [28] Yuan, H., Zhang, L., Hou, C., Zhu, G., Tao, D., Liang, Z., Zhang, Y., Integrated platform for proteome analysis with combination of protein and peptide separation via on-line digestion. Anal. Chem. 81 (2009), 8708–8714.
    • (2009) Anal. Chem. , vol.81 , pp. 8708-8714
    • Yuan, H.1    Zhang, L.2    Hou, C.3    Zhu, G.4    Tao, D.5    Liang, Z.6    Zhang, Y.7
  • 30
    • 76849103926 scopus 로고    scopus 로고
    • A capillary monolithic trypsin reactor for efficient protein digestion in on-line and offline coupling to ESI and MALDI mass spectrometry
    • [30] Spross, J., Sinz, A., A capillary monolithic trypsin reactor for efficient protein digestion in on-line and offline coupling to ESI and MALDI mass spectrometry. Anal. Chem. 82 (2010), 1434–1443.
    • (2010) Anal. Chem. , vol.82 , pp. 1434-1443
    • Spross, J.1    Sinz, A.2
  • 31
    • 84904863832 scopus 로고    scopus 로고
    • Novel regenerative large-volume immobilized enzyme reactor: preparation, characterization and application
    • [31] Ruan, G., Wei, M., Chen, Z., Su, R., Du, F., Zheng, Y., Novel regenerative large-volume immobilized enzyme reactor: preparation, characterization and application. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 967 (2014), 13–20.
    • (2014) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.967 , pp. 13-20
    • Ruan, G.1    Wei, M.2    Chen, Z.3    Su, R.4    Du, F.5    Zheng, Y.6
  • 32
    • 84865506560 scopus 로고    scopus 로고
    • Native protein proteolysis in an immobilized enzyme reactor as a function of temperature
    • [32] Rivera-Burgos, D., Regnier, F., Native protein proteolysis in an immobilized enzyme reactor as a function of temperature. Anal. Chem. 84 (2012), 7021–7028.
    • (2012) Anal. Chem. , vol.84 , pp. 7021-7028
    • Rivera-Burgos, D.1    Regnier, F.2
  • 33
    • 67649713420 scopus 로고    scopus 로고
    • Proteomic analysis of lipid-protein complexes
    • [33] Vaisar, T., Proteomic analysis of lipid-protein complexes. J. Lipid Res. 50 (2009), 781–786.
    • (2009) J. Lipid Res. , vol.50 , pp. 781-786
    • Vaisar, T.1
  • 34
    • 77952836190 scopus 로고    scopus 로고
    • Recent advances in on-line multidimensional liquid chromatography
    • [34] Malerod, H., Lundanes, E., Greibrokk, T., Recent advances in on-line multidimensional liquid chromatography. Anal. Methods 2 (2010), 110–122.
    • (2010) Anal. Methods , vol.2 , pp. 110-122
    • Malerod, H.1    Lundanes, E.2    Greibrokk, T.3
  • 35
    • 84873359716 scopus 로고    scopus 로고
    • Prefractionation of intact proteins by reversed-phase and anion-exchange chromatography for the differential proteomic analysis of Saccharomyces cerevisiae
    • [35] Stobaugh, J., Fague, K., Jorgenson, J., Prefractionation of intact proteins by reversed-phase and anion-exchange chromatography for the differential proteomic analysis of Saccharomyces cerevisiae. J. Proteome Res. 12 (2013), 626–636.
    • (2013) J. Proteome Res. , vol.12 , pp. 626-636
    • Stobaugh, J.1    Fague, K.2    Jorgenson, J.3
  • 36
    • 84920175281 scopus 로고    scopus 로고
    • Liquid phase based separation systems for depletion, prefractionation, and enrichment of proteins in biological fluids and matrices for in-depth proteomics analysis − an update covering the period 2011–2014
    • [36] Puangpila, C., Mayadunne, E., El Rassi, Z., Liquid phase based separation systems for depletion, prefractionation, and enrichment of proteins in biological fluids and matrices for in-depth proteomics analysis − an update covering the period 2011–2014. Electrophoresis 36 (2015), 238–252.
    • (2015) Electrophoresis , vol.36 , pp. 238-252
    • Puangpila, C.1    Mayadunne, E.2    El Rassi, Z.3
  • 37
    • 20544442274 scopus 로고    scopus 로고
    • Comparison of protein and peptide prefractionation methods for the shotgun proteomic analysis of Synechocystis sp. PCC 6803
    • [37] Gan, C., Reardon, K., Wright, P., Comparison of protein and peptide prefractionation methods for the shotgun proteomic analysis of Synechocystis sp. PCC 6803. Proteomics 5 (2005), 2468–2478.
    • (2005) Proteomics , vol.5 , pp. 2468-2478
    • Gan, C.1    Reardon, K.2    Wright, P.3
  • 38
    • 77958559051 scopus 로고    scopus 로고
    • New method for prefractionation of plasma for proteomic analysis
    • [38] Fitzgerald, A., Walsh, B., New method for prefractionation of plasma for proteomic analysis. Electrophoresis 31 (2010), 3580–3585.
    • (2010) Electrophoresis , vol.31 , pp. 3580-3585
    • Fitzgerald, A.1    Walsh, B.2
  • 39
    • 84865511222 scopus 로고    scopus 로고
    • Pepsin immobilized on high-strength hybrid particles for continuous flow on-line digestion at 10,000 psi
    • [39] Ahn, J., Jung, M., Wyndham, K., Yu, Y., Engen, J., Pepsin immobilized on high-strength hybrid particles for continuous flow on-line digestion at 10,000 psi. Anal. Chem. 84 (2012), 7256–7262.
    • (2012) Anal. Chem. , vol.84 , pp. 7256-7262
    • Ahn, J.1    Jung, M.2    Wyndham, K.3    Yu, Y.4    Engen, J.5
  • 42
    • 84999023284 scopus 로고    scopus 로고
    • Multidimensional Separations with Ultrahigh Pressure Liquid Chromatography-Mass Spectrometry for the Proteomics Analysis of Saccharomyces Cerevisiae
    • The University of North Carolina at Chapel Hill Doctoral Dissertation
    • [42] Fague, K., Multidimensional Separations with Ultrahigh Pressure Liquid Chromatography-Mass Spectrometry for the Proteomics Analysis of Saccharomyces Cerevisiae. 2014, The University of North Carolina at Chapel Hill Doctoral Dissertation.
    • (2014)
    • Fague, K.1
  • 43
    • 63049084861 scopus 로고    scopus 로고
    • The detection, correlation, and comparison of peptide precursor and product ions from data independent LC–MS with data dependant LC–MS/MS
    • [43] Geromanos, S., Vissers, J., Silva, J., Dorschel, C., Li, G., Gorenstein, M., Bateman, R., Langridge, J., The detection, correlation, and comparison of peptide precursor and product ions from data independent LC–MS with data dependant LC–MS/MS. Proteomics 9 (2009), 1683–1695.
    • (2009) Proteomics , vol.9 , pp. 1683-1695
    • Geromanos, S.1    Vissers, J.2    Silva, J.3    Dorschel, C.4    Li, G.5    Gorenstein, M.6    Bateman, R.7    Langridge, J.8
  • 44
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • [44] Bradford, M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976), 248–254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 45
    • 84883486565 scopus 로고    scopus 로고
    • Integrated sample preparation methodology for proteomics: analysis of native proteins
    • [45] Kim, J., Inerowicz, D., Hedrick, V., Regnier, F., Integrated sample preparation methodology for proteomics: analysis of native proteins. Anal. Chem. 85 (2013), 8039–8045.
    • (2013) Anal. Chem. , vol.85 , pp. 8039-8045
    • Kim, J.1    Inerowicz, D.2    Hedrick, V.3    Regnier, F.4
  • 46
    • 84940036458 scopus 로고    scopus 로고
    • A one-step preparation method of monolithic enzyme reactor for highly efficient sample preparation coupled to mass spectrometry-based proteomics studies
    • [46] Jiang, S., Zhang, Z., Li, L., A one-step preparation method of monolithic enzyme reactor for highly efficient sample preparation coupled to mass spectrometry-based proteomics studies. J. Chromatogr. A 1412 (2015), 75–81.
    • (2015) J. Chromatogr. A , vol.1412 , pp. 75-81
    • Jiang, S.1    Zhang, Z.2    Li, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.