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Direct structural assignment of neutral and sialylated N-glycans of glycopeptides using collision-induced dissociation MSⁿ spectral matching.

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タイトル: Direct structural assignment of neutral and sialylated N-glycans of glycopeptides using collision-induced dissociation MSⁿ spectral matching.
著者: Ito, Hiroki 著作を一覧する
Takegawa, Yasuhiro 著作を一覧する
Deguchi, Kisaburo 著作を一覧する
Nagai, Shinji 著作を一覧する
Nakagawa, Hiroaki 著作を一覧する
Shinohara, Yasuro 著作を一覧する
Nishimura, Shin-Ichiro 著作を一覧する
発行日: 2006年
誌名: Rapid Communications in Mass Spectrometry
巻: 20
号: 23
開始ページ: 3557
終了ページ: 3565
出版社 DOI: 10.1002/rcm.2761
抄録: Mass spectrometric analyses of various N-glycans binding to proteins and peptides are highly desirable for elucidating their biological roles. An approach based on collision-induced dissociation (CID) MSⁿ spectra acquired by electrospray ionization linear ion trap time-of-flight mass spectrometry (ESI-LIT-TOFMS) in the positive- and negative-ion modes has been proposed as a direct method of assigning N-glycans without releasing them from N-glycopeptides. In the positive-ion mode of this approach, the MS² spectrum of N-glycopeptide was acquired so that a glycoside-bond cleavage occurs in the chitobiose residue (i.e., GlcNAcβ1-4GlcNAc, GlcNAc: N-acetylglucosamine) attached to asparagine (N), and two charges on the [M+H+Na]²+ precursor ion are shared with both of the resulting fragments. These fragments are sodiated Bn-type fragment ions of oligosaccharide (N-glycan) and a protonated peptide ion retaining one GlcNAc residue on the asparagine (N) residue. The structure of N-glycan was assigned by comparing MS³ spectra derived from both the sodiated Bn-type fragment ions of N-glycopeptide and the PA (2-aminopyridine) N-glycan standard (i.e., MSⁿ spectral matching). In a similar manner, the structural assignment of sialylated N-glycan was performed by employing the negative-ion CID MSⁿ spectra of deprotonated Bn-type fragment ions of N-glycopeptide and the PA N-glycan standard. The efficacy of this approach was tested with chicken egg yolk glycopeptides with a neutral and a sialylated N-glycan, and human serum IgG glycopeptides with neutral N-glycan isomers. These results suggest that the approach based on MSⁿ spectral matching is useful for the direct and simple structural assignment of neutral and sialylated N-glycans of glycopeptides. Copyright © 2006 John Wiley & Sons, Ltd.
Rights: Copyright © 2006 John Wiley & Sons, Inc., Rapid Communications in Mass Spectrometry, 20(23)3557-3565
Relation (URI): http://www.interscience.wiley.com/
http://www3.interscience.wiley.com/cgi-bin/jhome/4849
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/17086
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 出口 喜三郎

 

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