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Differentiation of Isomeric N-Glycan Structures by Normal-Phase Liquid Chromatography—MALDI-TOFI TOF Tandem Mass Spectrometry.

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Title: Differentiation of Isomeric N-Glycan Structures by Normal-Phase Liquid Chromatography—MALDI-TOFI TOF Tandem Mass Spectrometry.
Authors: Maslen, Sarah1, Sadowski, Pawel2, Adam, Alex3, Lilley, Kathryn2, Stephens, Elaine1 es287@cam.ac.uk.
Source: Analytical Chemistry. 12/15/2006, Vol. 78 Issue 24, p8491-8498. 8p. 1 Diagram, 7 Graphs.
Subjects: Glycosylation, Esterification, Spectrum analysis, Proteins, Nuclear isomers, Ionization (Atomic physics), Auger effect, Properties of matter, Phospholipases
Abstract: The detailed characterization of protein N-glycosylation is very demanding given the many different glycoforms and structural isomers that can exist on glycoproteins. Here we report a fast and sensitive method for the extensive structure elucidation of reducing-end labeled N-glycan mixtures using a combination of capillary normal-phase HPLC coupled off-line to matrix-assisted laser desorption! ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and TOP/TOP-MS/MS. Using this method, isobaric N-glycans released from honey bee phospholipase A2 and Arabidopsis thaliana glycoproteins were separated by normal-phase chromatography and subsequently identified by key fragment ions in the MALDI-TOF/TOF tandem mass spectra. In addition, linkage and branching information were provided by abundant cross-ring and "elimination" fragment ions in the MALDI-CID spectra that gave extensive structural information. Furthermore, the fragmentation characteristics of N-glycans reductively aminated with 2-aminobenzoic acid and 2-aminobenzamide were compared. The identification of N-glycans containing 3-linked core fucose was facilitated by distinctive ions present only in the MALDI-CID spectra of 2-aminobenzoic acid-labeled oligosaccharides. To our knowledge, this is the first MS/MS-based technique that allows confident identification of N-glycans containing 3-linked core fucose, which is a major allergenic determinant on insect and plant glycoproteins. [ABSTRACT FROM AUTHOR]
Copyright of Analytical Chemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Differentiation of Isomeric N-Glycan Structures by Normal-Phase Liquid Chromatography—MALDI-TOFI TOF Tandem Mass Spectrometry.
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  Data: <searchLink fieldCode="AR" term="%22Maslen%2C+Sarah%22">Maslen, Sarah</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Sadowski%2C+Pawel%22">Sadowski, Pawel</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Adam%2C+Alex%22">Adam, Alex</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Lilley%2C+Kathryn%22">Lilley, Kathryn</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Stephens%2C+Elaine%22">Stephens, Elaine</searchLink><relatesTo>1</relatesTo><i> es287@cam.ac.uk.</i>
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  Data: <searchLink fieldCode="JN" term="%22Analytical+Chemistry%22">Analytical Chemistry</searchLink>. 12/15/2006, Vol. 78 Issue 24, p8491-8498. 8p. 1 Diagram, 7 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Glycosylation%22">Glycosylation</searchLink><br /><searchLink fieldCode="DE" term="%22Esterification%22">Esterification</searchLink><br /><searchLink fieldCode="DE" term="%22Spectrum+analysis%22">Spectrum analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Nuclear+isomers%22">Nuclear isomers</searchLink><br /><searchLink fieldCode="DE" term="%22Ionization+%28Atomic+physics%29%22">Ionization (Atomic physics)</searchLink><br /><searchLink fieldCode="DE" term="%22Auger+effect%22">Auger effect</searchLink><br /><searchLink fieldCode="DE" term="%22Properties+of+matter%22">Properties of matter</searchLink><br /><searchLink fieldCode="DE" term="%22Phospholipases%22">Phospholipases</searchLink>
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  Data: The detailed characterization of protein N-glycosylation is very demanding given the many different glycoforms and structural isomers that can exist on glycoproteins. Here we report a fast and sensitive method for the extensive structure elucidation of reducing-end labeled N-glycan mixtures using a combination of capillary normal-phase HPLC coupled off-line to matrix-assisted laser desorption! ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and TOP/TOP-MS/MS. Using this method, isobaric N-glycans released from honey bee phospholipase A2 and Arabidopsis thaliana glycoproteins were separated by normal-phase chromatography and subsequently identified by key fragment ions in the MALDI-TOF/TOF tandem mass spectra. In addition, linkage and branching information were provided by abundant cross-ring and "elimination" fragment ions in the MALDI-CID spectra that gave extensive structural information. Furthermore, the fragmentation characteristics of N-glycans reductively aminated with 2-aminobenzoic acid and 2-aminobenzamide were compared. The identification of N-glycans containing 3-linked core fucose was facilitated by distinctive ions present only in the MALDI-CID spectra of 2-aminobenzoic acid-labeled oligosaccharides. To our knowledge, this is the first MS/MS-based technique that allows confident identification of N-glycans containing 3-linked core fucose, which is a major allergenic determinant on insect and plant glycoproteins. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
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  Data: <i>Copyright of Analytical Chemistry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1021/ac0614137
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        Text: English
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      – SubjectFull: Glycosylation
        Type: general
      – SubjectFull: Esterification
        Type: general
      – SubjectFull: Spectrum analysis
        Type: general
      – SubjectFull: Proteins
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      – SubjectFull: Nuclear isomers
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      – SubjectFull: Ionization (Atomic physics)
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      – SubjectFull: Auger effect
        Type: general
      – SubjectFull: Properties of matter
        Type: general
      – SubjectFull: Phospholipases
        Type: general
    Titles:
      – TitleFull: Differentiation of Isomeric N-Glycan Structures by Normal-Phase Liquid Chromatography—MALDI-TOFI TOF Tandem Mass Spectrometry.
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            NameFull: Maslen, Sarah
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            NameFull: Sadowski, Pawel
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            NameFull: Adam, Alex
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            NameFull: Lilley, Kathryn
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              Text: 12/15/2006
              Type: published
              Y: 2006
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              Value: 78
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              Value: 24
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            – TitleFull: Analytical Chemistry
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