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Volumn 951, Issue , 2013, Pages 131-144

Glycopeptide enrichment for MALDI-TOF mass spectrometry analysis by hydrophilic interaction liquid chromatography solid phase extraction (HILIC SPE)

Author keywords

Enrichment; Glycopeptides; HILIC; Ion pairing reagent; MALDI TOF MS; N glycosylation; SPE

Indexed keywords

GLYCOPEPTIDE; GLYCOPROTEIN; TRIFLUOROACETIC ACID; IMMUNOGLOBULIN G;

EID: 84878630101     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-146-2_10     Document Type: Article
Times cited : (37)

References (30)
  • 1
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3:97-130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 2
    • 0032763888 scopus 로고    scopus 로고
    • Evolutionary considerations in relating oligosaccharide diversity to biological function
    • Gagneux P, Varki A (1999) Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9:747-755
    • (1999) Glycobiology , vol.9 , pp. 747-755
    • Gagneux, P.1    Varki, A.2
  • 3
    • 0003091286 scopus 로고    scopus 로고
    • Biological roles of glycans
    • Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J (eds). Cold Spring Harbor Laboratory Press, Woodbury, NY
    • Varki A, Lowe JB (1999) Biological roles of glycans. In: Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J (eds) Essentials of glycobiology, 2nd edn. Cold Spring Harbor Laboratory Press, Woodbury, NY, pp 57-68
    • (1999) Essentials of Glycobiology, 2nd Edn , pp. 57-68
    • Varki, A.1    Lowe, J.B.2
  • 4
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro RG (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12:43R-56R
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 5
    • 76149084829 scopus 로고    scopus 로고
    • GlycoSpectrumScan: Fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA
    • Deshpande N, Jensen PH, Packer NH, Kolarich D (2009) GlycoSpectrumScan: fishing glycopeptides from MS spectra of protease digests of human colostrum sIgA. J Proteome Res 9:1063-1075
    • (2009) J Proteome Res , vol.9 , pp. 1063-1075
    • Deshpande, N.1    Jensen, P.H.2    Packer, N.H.3    Kolarich, D.4
  • 6
    • 14944367556 scopus 로고    scopus 로고
    • Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry
    • Larsen MR, Højrup P, Roepstorff P (2005) Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry. Mol Cell Proteomics 4:107-119
    • (2005) Mol Cell Proteomics , vol.4 , pp. 107-119
    • Larsen, M.R.1    Højrup, P.2    Roepstorff, P.3
  • 8
    • 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
    • Hägglund P, Bunkenborg J, Elortza F, Jensen ON, Roepstorff P (2004) 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 3:556-566
    • (2004) J Proteome Res , vol.3 , pp. 556-566
    • Hägglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 9
    • 0028816610 scopus 로고
    • Tandem mass spectrometry and structural elucidation of glycopeptides from a hydroxyproline-rich plant cell wall glycoprotein indicate that contiguous hydroxyproline residues are the major sites of hydroxyproline O-arabinosylation
    • Kieliszewski MJ, O'Neill M, Leykam J, Orlando R (1995) Tandem mass spectrometry and structural elucidation of glycopeptides from a hydroxyproline-rich plant cell wall glycoprotein indicate that contiguous hydroxyproline residues are the major sites of hydroxyproline O-arabinosylation. J Biol Chem 270:2541-2549
    • (1995) J Biol Chem , vol.270 , pp. 2541-2549
    • Kieliszewski, M.J.1    O'Neill, M.2    Leykam, J.3    Orlando, R.4
  • 10
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wi niewski JR (2004) Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics 4:454-465
    • (2004) Proteomics , vol.4 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Winiewski, J.R.4
  • 11
    • 5444254250 scopus 로고    scopus 로고
    • Lectin-based structural glycomics: Glycoproteomics and glycan profiling
    • Hirabayashi J (2004) Lectin-based structural glycomics: glycoproteomics and glycan profiling. Glycoconj J 21:35-40
    • (2004) Glycoconj J , vol.21 , pp. 35-40
    • Hirabayashi, J.1
  • 12
    • 0016219421 scopus 로고
    • Binding of boronic acids to chymotrypsin
    • Rawn JD, Lienhard GE (1974) Binding of boronic acids to chymotrypsin. Biochemistry 13:3124-3130
    • (1974) Biochemistry , vol.13 , pp. 3124-3130
    • Rawn, J.D.1    Lienhard, G.E.2
  • 13
    • 33645748520 scopus 로고    scopus 로고
    • Selective isolation of glycoproteins and glycopeptides for MALDITOF MS detection supported by magnetic particles
    • Sparbier K, Koch S, Kessler I, Wenzel T, Kostrzewa M (2005) Selective isolation of glycoproteins and glycopeptides for MALDITOF MS detection supported by magnetic particles. J Biomol Tech 16:407-413
    • (2005) J Biomol Tech , vol.16 , pp. 407-413
    • Sparbier, K.1    Koch, S.2    Kessler, I.3    Wenzel, T.4    Kostrzewa, M.5
  • 14
    • 60549101068 scopus 로고    scopus 로고
    • Use of activated graphitized carbon chips for liquid chromatography/mass spectrometric and tandem mass spectrometric analysis of tryptic glycopeptides
    • Alley WR, Mechref Y, Novotny MV (2009) Use of activated graphitized carbon chips for liquid chromatography/mass spectrometric and tandem mass spectrometric analysis of tryptic glycopeptides. Rapid Commun Mass Spectrom 23:495-505
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 495-505
    • Alley, W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 15
    • 35649011957 scopus 로고    scopus 로고
    • Exploring the sialiome using titanium dioxide chromatography and mass spectrometry
    • Larsen MR, Jensen SS, Jakobsen LA, Heegaard NHH (2007) Exploring the sialiome using titanium dioxide chromatography and mass spectrometry. Mol Cell Proteomics 6:1778-1787
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1778-1787
    • Larsen, M.R.1    Jensen, S.S.2    Jakobsen, L.A.3    Heegaard, N.H.H.4
  • 16
    • 48849109894 scopus 로고    scopus 로고
    • Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry
    • Calvano CD, Zambonin CG, Jensen ON (2008) Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry. J Proteomics 71:304-317
    • (2008) J Proteomics , vol.71 , pp. 304-317
    • Calvano, C.D.1    Zambonin, C.G.2    Jensen, O.N.3
  • 17
    • 70349995796 scopus 로고    scopus 로고
    • Glycopeptide profiling of beta-2-glycoprotein i by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome
    • Kondo A, Miyamoto T, Yonekawa O, Giessing AM, Østerlund EC, Jensen ON (2009) Glycopeptide profiling of beta-2-glycoprotein I by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome. J Proteomics 73:123-133
    • (2009) J Proteomics , vol.73 , pp. 123-133
    • Kondo, A.1    Miyamoto, T.2    Yonekawa, O.3    Giessing, A.M.4    Østerlund, E.C.5    Jensen, O.N.6
  • 18
    • 77950796589 scopus 로고    scopus 로고
    • Characterization of sialylated and fucosylated glycopeptides of 2-glycoprotein i by a combination of HILIC LC and MALDI MS/MS
    • Kondo A, Thaysen-Andersen M, Hjernø K, Jensen ON (2010) Characterization of sialylated and fucosylated glycopeptides of 2-glycoprotein I by a combination of HILIC LC and MALDI MS/MS. J Sep Sci 33:891-902
    • (2010) J Sep Sci , vol.33 , pp. 891-902
    • Kondo, A.1    Thaysen-Andersen, M.2    Hjernø, K.3    Jensen, O.N.4
  • 19
    • 66149118626 scopus 로고    scopus 로고
    • Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: Strong correlation between signal strength and glycoform quantities
    • Thaysen-Andersen M, Mysling S, Højrup P (2009) Site-specific glycoprofiling of N-linked glycopeptides using MALDI-TOF MS: strong correlation between signal strength and glycoform quantities. Anal Chem 81:3933-3943
    • (2009) Anal Chem , vol.81 , pp. 3933-3943
    • Thaysen-Andersen, M.1    Mysling, S.2    Højrup, P.3
  • 20
    • 77954203412 scopus 로고    scopus 로고
    • Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics
    • Mysling S, Palmisano G, Højrup P, Thaysen- Andersen M (2010) Utilizing ion-pairing hydrophilic interaction chromatography solid phase extraction for efficient glycopeptide enrichment in glycoproteomics. Anal Chem 82:5598-5609
    • (2010) Anal Chem , vol.82 , pp. 5598-5609
    • Mysling, S.1    Palmisano, G.2    Højrup, P.3    Thaysen- Andersen, M.4
  • 21
    • 10644268451 scopus 로고    scopus 로고
    • Zooming in: Fractionation strategies in proteomics
    • Stasyk T, Huber LA (2004) Zooming in: fractionation strategies in proteomics. Proteomics 4:3704-3716
    • (2004) Proteomics , vol.4 , pp. 3704-3716
    • Stasyk, T.1    Huber, L.A.2
  • 22
    • 77951830268 scopus 로고    scopus 로고
    • Challenges of determining O-glycopeptide heterogeneity: A fungal glucanase model system
    • Christiansen MN, Kolarich D, Nevalainen H, Packer NH, Jensen PH (2010) Challenges of determining O-glycopeptide heterogeneity: a fungal glucanase model system. Anal Chem 82:3500-3509
    • (2010) Anal Chem , vol.82 , pp. 3500-3509
    • Christiansen, M.N.1    Kolarich, D.2    Nevalainen, H.3    Packer, N.H.4    Jensen, P.H.5
  • 23
    • 34548186744 scopus 로고    scopus 로고
    • An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins
    • Hägglund P, Matthiesen R, Elortza F, Højrup P, Roepstorff P, Jensen ON, Bunkenborg J (2007) An enzymatic deglycosylation scheme enabling identification of core fucosylated N-glycans and O-glycosylation site mapping of human plasma proteins. J Proteome Res 6:3021-3031
    • (2007) J Proteome Res , vol.6 , pp. 3021-3031
    • Hägglund, P.1    Matthiesen, R.2    Elortza, F.3    Højrup, P.4    Roepstorff, P.5    Jensen, O.N.6    Bunkenborg, J.7
  • 24
    • 84877252765 scopus 로고    scopus 로고
    • Peptide mapping for protein characterization
    • Humana Press, Totawa, NJ, Walker JM (ed)
    • Højrup P (2009) Peptide mapping for protein characterization. In: Walker JM (ed) The protein protocols handbook, 3rd edn. Humana Press, Totawa, NJ, pp 965-983
    • (2009) The Protein Protocols Handbook, 3rd Edn , pp. 965-983
    • Højrup, P.1
  • 25
    • 0030587060 scopus 로고    scopus 로고
    • Analysis of acidic oligosaccharides and glycopeptides by matrixassisted laser desorption/ionization time-of-flight mass spectrometry
    • Papac DI, Wong A, Jones AJS (1996) Analysis of acidic oligosaccharides and glycopeptides by matrixassisted laser desorption/ionization time-of-flight mass spectrometry. Anal Chem 68:3215-3223
    • (1996) Anal Chem , vol.68 , pp. 3215-3223
    • Papac, D.I.1    Wong, A.2    Jones, A.J.S.3
  • 27
    • 0033218504 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
    • Harvey DJ (1999) Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates. Mass Spectrom Rev 18:349-450
    • (1999) Mass Spectrom Rev , vol.18 , pp. 349-450
    • Harvey, D.J.1
  • 28
    • 4444367291 scopus 로고    scopus 로고
    • Peptide separation by hydrophilic- interaction chromatography: A review
    • Yoshida T (2004) Peptide separation by hydrophilic- interaction chromatography: a review. J Biochem Biophys Methods 60:265-280
    • (2004) J Biochem Biophys Methods , vol.60 , pp. 265-280
    • Yoshida, T.1
  • 29
    • 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 (2009) Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies. Anal Biochem 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
  • 30
    • 51049095706 scopus 로고    scopus 로고
    • Mixedmode ion-exchangers and their comparative chromatographic characterization in reversed-phase and hydrophilic interaction chromatography elution modes
    • Lämmerhofer M, Richter M, Wu J, Nogueira R, Bicker W, Lindner W (2008) Mixedmode ion-exchangers and their comparative chromatographic characterization in reversed-phase and hydrophilic interaction chromatography elution modes. J Sep Sci 31:2572-2588
    • (2008) J Sep Sci , vol.31 , pp. 2572-2588
    • Lämmerhofer, M.1    Richter, M.2    Wu, J.3    Nogueira, R.4    Bicker, W.5    Lindner, W.6


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