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Volumn 101, Issue , 2014, Pages 17-30

Selective glycopeptide profiling by acetone enrichment and LC/MS

Author keywords

Acetone; Glycopeptide enrichment; LC MS

Indexed keywords

ACETONE; GLUCOSYLATED SERUM PROTEIN; GLYCOPEPTIDE; PLASMA PROTEIN;

EID: 84894544737     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.02.005     Document Type: Article
Times cited : (34)

References (36)
  • 1
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R., Hermjakob H., Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1999, 1473:4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 2
    • 0036816590 scopus 로고    scopus 로고
    • Regulation of signal transduction pathways in development by glycosylation
    • Haltiwanger R.S. Regulation of signal transduction pathways in development by glycosylation. Curr Opin Struct Biol 2002, 12:593-598.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 593-598
    • Haltiwanger, R.S.1
  • 3
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K., Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell 2006, 126:855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 4
    • 0038574979 scopus 로고    scopus 로고
    • Ion suppression in mass spectrometry
    • Annesley T.M. Ion suppression in mass spectrometry. Clin Chem 2003, 49:1041-1044.
    • (2003) Clin Chem , vol.49 , pp. 1041-1044
    • Annesley, T.M.1
  • 5
    • 80655131078 scopus 로고    scopus 로고
    • Characterization of the human submandibular/sublingual saliva glycoproteome using lectin affinity chromatography coupled to multidimensional protein identification technology
    • Gonzalez-Begne M., Lu B., Liao L., Xu T., Bedi G., Melvin J.E., et al. Characterization of the human submandibular/sublingual saliva glycoproteome using lectin affinity chromatography coupled to multidimensional protein identification technology. J Proteome Res 2011, 10:5031-5046.
    • (2011) J Proteome Res , vol.10 , pp. 5031-5046
    • Gonzalez-Begne, M.1    Lu, B.2    Liao, L.3    Xu, T.4    Bedi, G.5    Melvin, J.E.6
  • 6
    • 61849161703 scopus 로고    scopus 로고
    • Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography
    • Jung K., Cho W., Regnier F.E. Glycoproteomics of plasma based on narrow selectivity lectin affinity chromatography. J Proteome Res 2009, 8:643-650.
    • (2009) J Proteome Res , vol.8 , pp. 643-650
    • Jung, K.1    Cho, W.2    Regnier, F.E.3
  • 7
    • 75749150176 scopus 로고    scopus 로고
    • Automated platform for fractionation of human plasma glycoproteome in clinical proteomics
    • Kullolli M., Hancock W.S., Hincapie M. Automated platform for fractionation of human plasma glycoproteome in clinical proteomics. Anal Chem 2010, 82:115-120.
    • (2010) Anal Chem , vol.82 , pp. 115-120
    • Kullolli, M.1    Hancock, W.S.2    Hincapie, M.3
  • 8
    • 21644459777 scopus 로고    scopus 로고
    • Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides
    • Madera M., Mechref Y., Novotny M.V. Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides. Anal Chem 2005, 77:4081-4090.
    • (2005) Anal Chem , vol.77 , pp. 4081-4090
    • Madera, M.1    Mechref, Y.2    Novotny, M.V.3
  • 9
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column
    • Yang Z., Hancock W.S. Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column. J Chromatogr A 2004, 1053:79-88.
    • (2004) J Chromatogr A , vol.1053 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 10
    • 0037685263 scopus 로고    scopus 로고
    • Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins
    • Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., et al. Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins. Nat Biotechnol 2003, 21:667-672.
    • (2003) Nat Biotechnol , vol.21 , pp. 667-672
    • Kaji, H.1    Saito, H.2    Yamauchi, Y.3    Shinkawa, T.4    Taoka, M.5    Hirabayashi, J.6
  • 11
    • 34548836006 scopus 로고    scopus 로고
    • Mass spectrometric identification of N-linked glycopeptides using lectin-mediated affinity capture and glycosylation site-specific stable isotope tagging
    • Kaji H., Yamauchi Y., Takahashi N., Isobe T. Mass spectrometric identification of N-linked glycopeptides using lectin-mediated affinity capture and glycosylation site-specific stable isotope tagging. Nat Protoc 2006, 1:3019-3027.
    • (2006) Nat Protoc , vol.1 , pp. 3019-3027
    • Kaji, H.1    Yamauchi, Y.2    Takahashi, N.3    Isobe, T.4
  • 12
    • 18144419694 scopus 로고    scopus 로고
    • Use of multidimensional lectin affinity chromatography in differential glycoproteomics
    • Qui R., Regnier F.E. Use of multidimensional lectin affinity chromatography in differential glycoproteomics. Anal Chem 2005, 77:2802-2809.
    • (2005) Anal Chem , vol.77 , pp. 2802-2809
    • Qui, R.1    Regnier, F.E.2
  • 13
    • 36048977494 scopus 로고    scopus 로고
    • Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection
    • Sparbier K., Asperger A., Resemann A., Kessler I., Koch S., Wenzel T., et al. Analysis of glycoproteins in human serum by means of glycospecific magnetic bead separation and LC-MALDI-TOF/TOF analysis with automated glycopeptide detection. J Biomol Tech 2007, 18:252-258.
    • (2007) J Biomol Tech , vol.18 , pp. 252-258
    • Sparbier, K.1    Asperger, A.2    Resemann, A.3    Kessler, I.4    Koch, S.5    Wenzel, T.6
  • 14
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska D.F., Gnad F., Wiśniewski J.R., Mann M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 2010, 141:897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 15
    • 34047164035 scopus 로고    scopus 로고
    • Glycoproteomics based on tandem mass spectrometry of glycopeptides
    • Wuhrer M., Catalina M.I., Deelder M., Hokke C.H. Glycoproteomics based on tandem mass spectrometry of glycopeptides. J Chromatogr B 2007, 849:115-128.
    • (2007) J Chromatogr B , vol.849 , pp. 115-128
    • Wuhrer, M.1    Catalina, M.I.2    Deelder, M.3    Hokke, C.H.4
  • 16
    • 33947581026 scopus 로고    scopus 로고
    • N-linked glycosylation profiling of pancreatic cancer serum using capillary liquid phase separation coupled with mass spectrometric analysis
    • Zhao J., Qiu W., Simeone D.M., Lubman D.M. N-linked glycosylation profiling of pancreatic cancer serum using capillary liquid phase separation coupled with mass spectrometric analysis. J Proteome Res 2007, 6:1126-1138.
    • (2007) J Proteome Res , vol.6 , pp. 1126-1138
    • Zhao, J.1    Qiu, W.2    Simeone, D.M.3    Lubman, D.M.4
  • 17
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wiśniewski J.R. Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics 2004, 4:454-465.
    • (2004) Proteomics , vol.4 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wiśniewski, J.R.4
  • 18
    • 4143072608 scopus 로고    scopus 로고
    • A method for proteomic identification of membrane-bound proteins containing Asn-linked oligosaccharides
    • Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J. A method for proteomic identification of membrane-bound proteins containing Asn-linked oligosaccharides. Anal Biochem 2004, 332:178-186.
    • (2004) Anal Biochem , vol.332 , pp. 178-186
    • Fan, X.1    She, Y.-M.2    Bagshaw, R.D.3    Callahan, J.W.4    Schachter, H.5    Mahuran, D.J.6
  • 19
    • 0020368287 scopus 로고
    • Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography
    • Cummings R.D., Kornfeld S. Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography. J Biol Chem 1982, 257:11235-11240.
    • (1982) J Biol Chem , vol.257 , pp. 11235-11240
    • Cummings, R.D.1    Kornfeld, S.2
  • 20
    • 48849109894 scopus 로고    scopus 로고
    • Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry
    • Calvano C.D., Zambonin C.G., Jensen O.N. Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry. J Proteomics 2008, 71:304-317.
    • (2008) J Proteomics , vol.71 , pp. 304-317
    • Calvano, C.D.1    Zambonin, C.G.2    Jensen, O.N.3
  • 21
    • 71049170514 scopus 로고    scopus 로고
    • Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry
    • Ding W., Norhaft H., Szymanski C.M., Kelly J. Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry. Mol Cell Proteomics 2009, 8:2170-2185.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2170-2185
    • Ding, W.1    Norhaft, H.2    Szymanski, C.M.3    Kelly, J.4
  • 22
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J Proteome Res 2004, 3:556-566.
    • (2004) J Proteome Res , vol.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 23
    • 79955840214 scopus 로고    scopus 로고
    • Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides
    • Neue K., Mormann M., Peter-Katalinic J., Pohlentz G. Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides. J Proteome Res 2011, 10:2248-2260.
    • (2011) J Proteome Res , vol.10 , pp. 2248-2260
    • Neue, K.1    Mormann, M.2    Peter-Katalinic, J.3    Pohlentz, G.4
  • 24
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada Y., Tajiri M. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics. Anal Chem 2004, 76(22):6560-6565.
    • (2004) Anal Chem , vol.76 , Issue.22 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2
  • 25
    • 84861844024 scopus 로고    scopus 로고
    • Centrifugation assisted microreactor enables facile integration of trypsin digestion, hydrophilic interaction chromatography enrichment, and on-column deglycosylation for rapid and sensitive N-glycoproteome analysis
    • Zhu J., Wang F., Chen R., Cheng K., Xu B., Guo Z., et al. Centrifugation assisted microreactor enables facile integration of trypsin digestion, hydrophilic interaction chromatography enrichment, and on-column deglycosylation for rapid and sensitive N-glycoproteome analysis. Anal Chem 2012, 84:5146-5153.
    • (2012) Anal Chem , vol.84 , pp. 5146-5153
    • Zhu, J.1    Wang, F.2    Chen, R.3    Cheng, K.4    Xu, B.5    Guo, Z.6
  • 26
    • 70349784960 scopus 로고    scopus 로고
    • Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies
    • Wohlgemuth J., Karas M., Eichhorn T., Hendriks R., Andrecht S. Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies. Anal Biochem 2009, 395:178-188.
    • (2009) Anal Biochem , vol.395 , pp. 178-188
    • Wohlgemuth, J.1    Karas, M.2    Eichhorn, T.3    Hendriks, R.4    Andrecht, S.5
  • 27
    • 0035895786 scopus 로고    scopus 로고
    • Shielding of protein-boronate interactions during boronate chromatography of neoglycoproteins
    • Li Y., Larsson E.L., Jungvid H., Galaev I.Y., Mattiasson B. Shielding of protein-boronate interactions during boronate chromatography of neoglycoproteins. J Chromatogr A 2001, 909:137-145.
    • (2001) J Chromatogr A , vol.909 , pp. 137-145
    • Li, Y.1    Larsson, E.L.2    Jungvid, H.3    Galaev, I.Y.4    Mattiasson, B.5
  • 28
    • 0016219421 scopus 로고
    • The binding of boronic acids to chymotrypsin
    • Rawn J.D., Lienhard C.E. The binding of boronic acids to chymotrypsin. Biochemistry 1974, 13:3124-3130.
    • (1974) Biochemistry , vol.13 , pp. 3124-3130
    • Rawn, J.D.1    Lienhard, C.E.2
  • 29
    • 33644841035 scopus 로고    scopus 로고
    • Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites
    • Alvarez-Manilla G., Atwood J., Guo Y., Warren N.L., Orlando R., Pierce M. Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites. J Proteome Res 2003, 5:701-708.
    • (2003) J Proteome Res , vol.5 , pp. 701-708
    • Alvarez-Manilla, G.1    Atwood, J.2    Guo, Y.3    Warren, N.L.4    Orlando, R.5    Pierce, M.6
  • 30
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H., Li X.-j., Martin D.B., Aebersold R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 2003, 21(6):660-666.
    • (2003) Nat Biotechnol , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aebersold, R.4
  • 31
    • 32044455761 scopus 로고    scopus 로고
    • Characterization of N-glycans of recombinant human thyrotropin using mass spectrometry
    • Morelle W., Donadio S., Ronin C., Michalski J.C. Characterization of N-glycans of recombinant human thyrotropin using mass spectrometry. Rapid Commun Mass Spectrom 2006, 20(3):331-345.
    • (2006) Rapid Commun Mass Spectrom , vol.20 , Issue.3 , pp. 331-345
    • Morelle, W.1    Donadio, S.2    Ronin, C.3    Michalski, J.C.4
  • 33
    • 0023390753 scopus 로고
    • Structure and expression of the genes coding for human α1- acid glycoprotein
    • Dente L., Pizza M.G., Metspalu A., Cortese R. Structure and expression of the genes coding for human α1- acid glycoprotein. EMBO J 1987, 6(8):2289-2296.
    • (1987) EMBO J , vol.6 , Issue.8 , pp. 2289-2296
    • Dente, L.1    Pizza, M.G.2    Metspalu, A.3    Cortese, R.4
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982, 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 44749083346 scopus 로고    scopus 로고
    • Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry
    • Harazono A., Kawasaki N., Itoh S., Hashii N., Matsuishi-Nakajima Y., Kawanishi T., et al. Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry. J Chromatogr B 2008, 869:20-30.
    • (2008) J Chromatogr B , vol.869 , pp. 20-30
    • Harazono, A.1    Kawasaki, N.2    Itoh, S.3    Hashii, N.4    Matsuishi-Nakajima, Y.5    Kawanishi, T.6


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