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Volumn 45, Issue 5, 2010, Pages 528-535

Fragmentation of negative ions from N-linked carbohydrates, Part 4. Fragmentation of complex glycans lacking substitution on the 6-antenna

Author keywords

Electrospray; Glycosylation disorder; MALDI; N Glycans; Negative ion fragmentation

Indexed keywords

CHITOBIOSE; ELECTROSPRAY; ELECTROSPRAYS; FRAGMENT IONS; GLYCANS; ISOMERIC COMPOUNDS; MASS SPECTRA; N-ACETYLGLUCOSAMINE; N-GLYCANS; N-LINKED; N-LINKED GLYCANS; PURE STATE; STRUCTURAL FEATURE;

EID: 77951727269     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1736     Document Type: Article
Times cited : (36)

References (21)
  • 1
    • 14344259450 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates: Part 1; Use of nitrate and other anionic adducts for the production of negative ion electrospray spectra from N-linked carbohydrates
    • D. J. Harvey. Fragmentation of negative ions from carbohydrates: Part 1; Use of nitrate and other anionic adducts for the production of negative ion electrospray spectra from N-linked carbohydrates. J. Am. Soc.Mass Spectrom. 2005, 16, 622.
    • (2005) J. Am. Soc.Mass Spectrom. , vol.16 , pp. 622
    • Harvey, D.J.1
  • 2
    • 18044364597 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates: Part 2, Fragmentation of high-mannose N-linked glycans
    • D. J. Harvey. Fragmentation of negative ions from carbohydrates: Part 2, Fragmentation of high-mannose N-linked glycans. J. Am. Soc. Mass Spectrom. 2005, 16, 631.
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 631
    • Harvey, D.J.1
  • 3
    • 14344254313 scopus 로고    scopus 로고
    • Fragmentation of negative ions from carbohydrates: Part 3, Fragmentation of hybrid and complex N-linked glycans
    • D. J. Harvey. Fragmentation of negative ions from carbohydrates: Part 3, Fragmentation of hybrid and complex N-linked glycans. J. Am. Soc. Mass Spectrom. 2005, 16, 647.
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 647
    • Harvey, D.J.1
  • 4
    • 41449103898 scopus 로고    scopus 로고
    • Structural and quantitative analysis of N-linked glycans by MALDI and negative ion nanospray mass spectrometry
    • D. J. Harvey, L. Royle, C. M. Radcliffe, P. M. Rudd, R. A. Dwek. Structural and quantitative analysis of N-linked glycans by MALDI and negative ion nanospray mass spectrometry. Anal. Biochem. 2008, 376, 44.
    • (2008) Anal. Biochem. , vol.376 , pp. 44
    • Harvey, D.J.1    Royle, L.2    Radcliffe, C.M.3    Rudd, P.M.4    Dwek, R.A.5
  • 8
    • 68549091059 scopus 로고    scopus 로고
    • Proposal for a standard system for drawing structural diagrams ofN-andO-linked carbohydratesandrelatedcompounds
    • D. J. Harvey, A.H.Merry, L. Royle, M. P. Campbell, R. A.Dwek, P. M. Rudd. Proposal for a standard system for drawing structural diagrams ofN-andO-linked carbohydratesandrelatedcompounds. Proteomics 2009, 9, 3796.
    • (2009) Proteomics , vol.9 , pp. 3796
    • Harvey, D.J.1    Merry, A.H.2    Royle, L.3    Campbell, M.P.4    Dwek, R.A.5    Rudd, P.M.6
  • 9
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N- And O-linked oligosaccharides from glycoproteins
    • T. Patel, J. Bruce, A. Merry, C. Bigge, M.Wormald, A. Jaques, R. Parekh. Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins. Biochemistry 1993, 32, 679.
    • (1993) Biochemistry , vol.32 , pp. 679
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4    Wormald, M.5    Jaques, A.6    Parekh, R.7
  • 10
    • 0027057617 scopus 로고
    • The use of large-scale hydrazinolysis in the preparation of N-linked oligosaccharide libraries: Application to brain tissue
    • D. R. Wing, M. C. Field, B. Schmitz, G. Thor, R. A. Dwek, M. S. Schachner, T. W. Rademacher. The use of large-scale hydrazinolysis in the preparation of N-linked oligosaccharide libraries: application to brain tissue. Glycoconj. J. 1992, 9, 293.
    • (1992) Glycoconj. J. , vol.9 , pp. 293
    • Wing, D.R.1    Field, M.C.2    Schmitz, B.3    Thor, G.4    Dwek, R.A.5    Schachner, M.S.6    Rademacher, T.W.7
  • 11
    • 0031571138 scopus 로고    scopus 로고
    • Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high performance liquid chromatography
    • B. Küster, S. F.Wheeler, A. P. Hunter, R. A. Dwek, D. J. Harvey. Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high performance liquid chromatography. Anal. Biochem. 1997, 250, 82.
    • (1997) Anal. Biochem. , vol.250 , pp. 82
    • Küster, B.1    Wheeler, S.F.2    Hunter, A.P.3    Dwek, R.A.4    Harvey, D.J.5
  • 12
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • B. Domon, C. E. Costello. A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconj. J. 1988, 5, 397.
    • (1988) Glycoconj. J. , vol.5 , pp. 397
    • Domon, B.1    Costello, C.E.2
  • 13
    • 10844287190 scopus 로고    scopus 로고
    • Fragmentation of N-linked glycans with a MALDI-ion trap time-of-flight mass spectrometer
    • D. J. Harvey, R. L. Martin, K. A. Jackson, C. W. Sutton. Fragmentation of N-linked glycans with a MALDI-ion trap time-of-flight mass spectrometer. Rapid Commun.Mass Spectrom. 2004, 18, 2997.
    • (2004) Rapid Commun.Mass Spectrom. , vol.18 , pp. 2997
    • Harvey, D.J.1    Martin, R.L.2    Jackson, K.A.3    Sutton, C.W.4
  • 14
    • 0031037943 scopus 로고    scopus 로고
    • High-energy collision-induced fragmentation of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry
    • D. J. Harvey, R. H. Bateman, M. R. Green. High-energy collision-induced fragmentation of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 1997, 32, 167.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 167
    • Harvey, D.J.1    Bateman, R.H.2    Green, M.R.3
  • 15
    • 41549130879 scopus 로고    scopus 로고
    • Differentiation between isomeric triantennary N-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose attached to the bisecting (ß1-4-GlcNAc) residue in N-glycans from IgG
    • D. J.Harvey,M. Crispin,C. Scanlan,B. B. Singer,L. Lucka,V. T. Chang, C. M. Radcliffe, S. Thobhani, C.-T. Yuen, P. M. Rudd. Differentiation between isomeric triantennary N-linked glycans by negative ion tandem mass spectrometry and confirmation of glycans containing galactose attached to the bisecting (ß1-4-GlcNAc) residue in N-glycans from IgG. Rapid Commun.Mass Spectrom. 2008, 22, 1047.
    • (2008) Rapid Commun.Mass Spectrom. , vol.22 , pp. 1047
    • Harvey, D.J.1    Crispin, M.2    Scanlan, C.3    Singer, B.B.4    Lucka, L.5    Chang, V.T.6    Radcliffe, C.M.7    Thobhani, S.8    Yuen, C.-T.9    Rudd, P.M.10
  • 16
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • R. Kornfeld, S. Kornfeld. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 1985, 54, 631.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631
    • Kornfeld, R.1    Kornfeld, S.2
  • 18
    • 0032789158 scopus 로고    scopus 로고
    • Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain- type" neutral N-glycans
    • S. Zamze, D. J. Harvey, P. Pesheva, T. S. Mattu, M. Schachner, R. A. Dwek, D. R. Wing. Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain-type" neutral N-glycans. Glycobiology 1999, 9, 823.
    • (1999) Glycobiology , vol.9 , pp. 823
    • Zamze, S.1    Harvey, D.J.2    Pesheva, P.3    Mattu, T.S.4    Schachner, M.5    Dwek, R.A.6    Wing, D.R.7
  • 19
    • 16644364860 scopus 로고    scopus 로고
    • Abnormal biantennary sugar chains are expressed in human chorionic gonadotropin produced in the choriocarcinoma cell line, JEG-3
    • S. Takamatsu, T. Katsumata, N. Inoue, T. Watanabe, Y. Fujibayashi, M. Takeuchi. Abnormal biantennary sugar chains are expressed in human chorionic gonadotropin produced in the choriocarcinoma cell line, JEG-3. Glycoconj. J. 2004, 20, 473.
    • (2004) Glycoconj. J. , vol.20 , pp. 473
    • Takamatsu, S.1    Katsumata, T.2    Inoue, N.3    Watanabe, T.4    Fujibayashi, Y.5    Takeuchi, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.