메뉴 건너뛰기




Volumn 385, Issue 1, 2009, Pages 69-79

High-throughput immunoglobulin G N-glycan characterization using rapid resolution reverse-phase chromatography tandem mass spectrometry

Author keywords

Glycan profiling; N linked oligosaccharide; Reverse phase chromatography

Indexed keywords

DESORPTION; ELECTRODEPOSITION; ELECTROSPRAY IONIZATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NEGATIVE IONS;

EID: 57849115243     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.10.023     Document Type: Article
Times cited : (58)

References (31)
  • 1
    • 33947688082 scopus 로고    scopus 로고
    • Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion
    • Qian J., Liu T., Yang L., Daus A., Crowley R., and Zhou Q. Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion. Anal. Biochem. 364 (2007) 8-18
    • (2007) Anal. Biochem. , vol.364 , pp. 8-18
    • Qian, J.1    Liu, T.2    Yang, L.3    Daus, A.4    Crowley, R.5    Zhou, Q.6
  • 2
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • Jenkins N., Parekh R.B., and James D.C. Getting the glycosylation right: Implications for the biotechnology industry. Nat. Biotechnol. 14 (1996) 975-981
    • (1996) Nat. Biotechnol. , vol.14 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 8
    • 57849153690 scopus 로고    scopus 로고
    • European Medicines Agency, Guideline on Production and Quality Control of Monoclonal Antibodies and Related Substances [draft], 2007, available from: .
    • European Medicines Agency, Guideline on Production and Quality Control of Monoclonal Antibodies and Related Substances [draft], 2007, available from: .
  • 9
    • 0033218504 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates
    • Harvey D.J. Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates. Mass Spectrom. Rev. 18 (1999) 349-451
    • (1999) Mass Spectrom. Rev. , vol.18 , pp. 349-451
    • Harvey, D.J.1
  • 10
    • 0141482211 scopus 로고    scopus 로고
    • Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry
    • Mechref Y., and Novotny M.V. Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 75 (2003) 4895-4903
    • (2003) Anal. Chem. , vol.75 , pp. 4895-4903
    • Mechref, Y.1    Novotny, M.V.2
  • 11
    • 1942454436 scopus 로고    scopus 로고
    • Fragmentation characteristics of neutral N-linked glycans using a MALDI-TOF/TOF tandem mass spectrometer
    • Stephens E., Maslen S.L., Green L.G., and Williams D.H. Fragmentation characteristics of neutral N-linked glycans using a MALDI-TOF/TOF tandem mass spectrometer. Anal. Chem. 76 (2004) 2343-2354
    • (2004) Anal. Chem. , vol.76 , pp. 2343-2354
    • Stephens, E.1    Maslen, S.L.2    Green, L.G.3    Williams, D.H.4
  • 13
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins
    • Patel T., Bruce J., Merry A., Bigge C., Wormald M., Jaques A., and Parekh R. Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins. Biochemistry 32 (1993) 679-693
    • (1993) Biochemistry , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4    Wormald, M.5    Jaques, A.6    Parekh, R.7
  • 14
    • 0028261414 scopus 로고
    • Enzymatic deglycosylation of asparagines-linked glycans: Purification, Properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum
    • Tarentino A.L., and Plummer Jr. T.H. Enzymatic deglycosylation of asparagines-linked glycans: Purification, Properties, and specificity of oligosaccharide-cleaving enzymes from Flavobacterium meningosepticum. Methods Enzymol. 230 (1994) 44-57
    • (1994) Methods Enzymol. , vol.230 , pp. 44-57
    • Tarentino, A.L.1    Plummer Jr., T.H.2
  • 15
    • 33750632035 scopus 로고    scopus 로고
    • Rapid removal of N-linked oligosaccharides using microwave assisted enzyme catalyzed deglycosylation
    • Sandoval W., Arellano F., Arnott D., Raab H., Vandlen R., and Lill J. Rapid removal of N-linked oligosaccharides using microwave assisted enzyme catalyzed deglycosylation. Int. J. Mass Spectrom. 259 (2007) 117-123
    • (2007) Int. J. Mass Spectrom. , vol.259 , pp. 117-123
    • Sandoval, W.1    Arellano, F.2    Arnott, D.3    Raab, H.4    Vandlen, R.5    Lill, J.6
  • 16
    • 32644474401 scopus 로고    scopus 로고
    • Advances in fluorescence derivatization methods for high-performance liquid chromatographic analysis of glycoprotein carbohydrates
    • Anumula K. Advances in fluorescence derivatization methods for high-performance liquid chromatographic analysis of glycoprotein carbohydrates. Anal. Biochem. 350 (2006) 1-23
    • (2006) Anal. Biochem. , vol.350 , pp. 1-23
    • Anumula, K.1
  • 17
    • 34548475063 scopus 로고    scopus 로고
    • Automated sample preparation facilitated by PhyNexus MEA purification system for oligosaccharide mapping of glycoproteins
    • Prater B.D., Anumula K.R., and Hutchins J.T. Automated sample preparation facilitated by PhyNexus MEA purification system for oligosaccharide mapping of glycoproteins. Anal. Biochem. 369 (2007) 202-209
    • (2007) Anal. Biochem. , vol.369 , pp. 202-209
    • Prater, B.D.1    Anumula, K.R.2    Hutchins, J.T.3
  • 18
    • 0031820069 scopus 로고    scopus 로고
    • High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid
    • Anumula K.R., and Dhume S.T. High resolution and high sensitivity methods for oligosaccharide mapping and characterization by normal phase high performance liquid chromatography following derivatization with highly fluorescent anthranilic acid. Glycobiology 8 (1998) 685-694
    • (1998) Glycobiology , vol.8 , pp. 685-694
    • Anumula, K.R.1    Dhume, S.T.2
  • 19
    • 0025006627 scopus 로고
    • High-performance anion-exchange chromatography for carbohydrate analysis
    • Lee Y.C. High-performance anion-exchange chromatography for carbohydrate analysis. Anal. Biochem. 189 (1990) 151-162
    • (1990) Anal. Biochem. , vol.189 , pp. 151-162
    • Lee, Y.C.1
  • 20
    • 0004248246 scopus 로고    scopus 로고
    • Lot-to-lot consistency of glycoproteins
    • Townsend R.R., and Hotchkiss Jr. A.T. (Eds), CRC Press, Boca Raton, FL
    • Kopp K., Schluter M., and Werner R.G. Lot-to-lot consistency of glycoproteins. In: Townsend R.R., and Hotchkiss Jr. A.T. (Eds). Techniques in Glycobiology (1997), CRC Press, Boca Raton, FL 475-489
    • (1997) Techniques in Glycobiology , pp. 475-489
    • Kopp, K.1    Schluter, M.2    Werner, R.G.3
  • 21
    • 0031792743 scopus 로고    scopus 로고
    • Profiling glycoprotein N-linked oligosaccharide by capillary electrophoresis
    • Chen F.T., and Evangalista R.A. Profiling glycoprotein N-linked oligosaccharide by capillary electrophoresis. Electrophoresis 19 (1998) 2639-2644
    • (1998) Electrophoresis , vol.19 , pp. 2639-2644
    • Chen, F.T.1    Evangalista, R.A.2
  • 22
    • 0025708306 scopus 로고
    • The use of polyacrylamide-gel electrophoresis for the high-resolution separation of reducing saccharides labelled with the fluorophore 8-aminonaphthalene-1, 3, 6-trisulphonic acid
    • Jackson P. The use of polyacrylamide-gel electrophoresis for the high-resolution separation of reducing saccharides labelled with the fluorophore 8-aminonaphthalene-1, 3, 6-trisulphonic acid. Biochem. J. 270 (1990) 705-713
    • (1990) Biochem. J. , vol.270 , pp. 705-713
    • Jackson, P.1
  • 23
    • 0034970558 scopus 로고    scopus 로고
    • Investigation of different combinations of derivatization, separation methods, and electrospray ionization mass spectrometry for standard oligosaccharides and glycans from ovalbumin
    • Saba J.A., Shen X., Jamieson J.C., and Perreault H. Investigation of different combinations of derivatization, separation methods, and electrospray ionization mass spectrometry for standard oligosaccharides and glycans from ovalbumin. J. Mass Spectrom. 36 (2001) 563-574
    • (2001) J. Mass Spectrom. , vol.36 , pp. 563-574
    • Saba, J.A.1    Shen, X.2    Jamieson, J.C.3    Perreault, H.4
  • 24
    • 16244381432 scopus 로고    scopus 로고
    • Simultaneous analysis of 2-aminopyridine-derivatized neutral and sialylated oligosaccharides from human serum in the negative-ion mode by sonic spray ionization ion trap mass spectrometry
    • Takegawa Y., Deguchi K., Ito S., Yoshioka S., Nakagawa H., and Nishimura S. Simultaneous analysis of 2-aminopyridine-derivatized neutral and sialylated oligosaccharides from human serum in the negative-ion mode by sonic spray ionization ion trap mass spectrometry. Anal. Chem. 77 (2005) 2097-2106
    • (2005) Anal. Chem. , vol.77 , pp. 2097-2106
    • Takegawa, Y.1    Deguchi, K.2    Ito, S.3    Yoshioka, S.4    Nakagawa, H.5    Nishimura, S.6
  • 25
    • 34748837881 scopus 로고    scopus 로고
    • Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry
    • Chen X., and Flynn G.C. Analysis of N-glycans from recombinant immunoglobulin G by on-line reversed-phase high-performance liquid chromatography/mass spectrometry. Anal. Biochem. 370 (2007) 147-161
    • (2007) Anal. Biochem. , vol.370 , pp. 147-161
    • Chen, X.1    Flynn, G.C.2
  • 26
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: A tool for the computer assisted annotation of mass spectra of glycans
    • Ceroni A., Maass K., Geyer H., Geyer R., Dell A., and Haslam S.M. GlycoWorkbench: A tool for the computer assisted annotation of mass spectra of glycans. J. Proteome Res. 7 (2008) 1650-1659
    • (2008) J. Proteome Res. , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5    Haslam, S.M.6
  • 27
    • 0034661933 scopus 로고    scopus 로고
    • High-sensitivity and high-resolution methods for glycoprotein analysis
    • Anumula K.R. High-sensitivity and high-resolution methods for glycoprotein analysis. Anal. Biochem. 283 (2000) 17-26
    • (2000) Anal. Biochem. , vol.283 , pp. 17-26
    • Anumula, K.R.1
  • 28
    • 34547909916 scopus 로고    scopus 로고
    • Distinguishing isomeric pyridylaminated high-mannose (Man7) oligosaccharides based on energy-resolved mass spectra
    • Kurimoto A., and Kanie O. Distinguishing isomeric pyridylaminated high-mannose (Man7) oligosaccharides based on energy-resolved mass spectra. Rapid Commun. Mass Spectrom. 21 (2007) 2770-2778
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 2770-2778
    • Kurimoto, A.1    Kanie, O.2
  • 31
    • 38649143213 scopus 로고    scopus 로고
    • Double knockdown of α1,6-fucosyltransferase (FUT8) and GDP-mannose 4, 6-dehydratase (GMD) in antibody-producing cells: A new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC
    • Imai-Nishiya H., Mori K., Inoue M., Wakitani M., Iida S., Shitara K., and Satoh M. Double knockdown of α1,6-fucosyltransferase (FUT8) and GDP-mannose 4, 6-dehydratase (GMD) in antibody-producing cells: A new strategy for generating fully non-fucosylated therapeutic antibodies with enhanced ADCC. BMC Biotechnol. 7 (2007) 84-97
    • (2007) BMC Biotechnol. , vol.7 , pp. 84-97
    • Imai-Nishiya, H.1    Mori, K.2    Inoue, M.3    Wakitani, M.4    Iida, S.5    Shitara, K.6    Satoh, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.