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Glutamine deamidation : differentiation of glutamic acid and gamma-Glutamic acid in peptides by electron capture dissociation
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Li, Xiaojuan, Lin, Cheng and O'Connor, Peter B. (2010) Glutamine deamidation : differentiation of glutamic acid and gamma-Glutamic acid in peptides by electron capture dissociation. Analytical Chemistry, Vol.82 (No.9). pp. 3606-3615. doi:10.1021/ac9028467 ISSN 0003-2700.
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Official URL: http://dx.doi.org/10.1021/ac9028467
Abstract
Due to its much slower deamidation rate compared to that of asparagine (Asn), studies on glutamine (Gin) deamidation have been scarce, especially on the differentiation of its isomeric deamidation products: alpha- and gamma-glutamic acid (Glu). It has been shown previously that electron capture dissociation (ECD) can be used to generate diagnostic ions for the deamidation products of Asn: aspartic acid (Asp) and isoaspartic acid (isoAsp). The current study explores the possibility of an extension of this ECD based method to the differentiation of the alpha- and gamma-Glu residues, using three human Crystallin peptides (alpha A (1-11), beta B2 (4-14), and gamma S (52-71)) and their potentially deamidated forms as model peptides. It was found that the z(center dot)-72 ions can be used to both identify the existence and locate the position of the gamma-Glu residues. When the peptide contains a charge carrier near its N-terminus, the c+57 and c+59 ions may also be generated at the gamma-Glu residue. It was unclear whether formation of these N-terminal diagnostic ions is specific to the Pro-gamma-Glu sequence. Unlike the Asp containing peptides, the Glu containing peptides generally do not produce diagnostic side chain loss ions, due to the instability of the resulting radical. The presence of Glu residue(s) may be inferred from the observation of a series of z(n)(center dot)-59 ions, although it was neither site specific nor without interference from the gamma-Glu residues. Finally, several interference peaks exist in the ECD spectra, which highlights the importance of the use of high performance mass spectrometers for confident identification of gamma-Glu residues.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
Library of Congress Subject Headings (LCSH): | Glutamine, Deamination, Tandem mass spectrometry, Glutamic acid, Peptides, Post-translational modification | ||||
Journal or Publication Title: | Analytical Chemistry | ||||
Publisher: | American Chemical Society | ||||
ISSN: | 0003-2700 | ||||
Official Date: | 1 May 2010 | ||||
Dates: |
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Volume: | Vol.82 | ||||
Number: | No.9 | ||||
Number of Pages: | 10 | ||||
Page Range: | pp. 3606-3615 | ||||
DOI: | 10.1021/ac9028467 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Funder: | National Institute of General Medical Sciences (U.S.) (NIGMS), National Heart, Lung, and Blood Institute (NHLBI), MDS Sciex, ACS Petroleum Research Fund, National Center for Research Resources (U.S.) (NCRR) | ||||
Grant number: | P41RR10888 (NCRR), N01HV28178 (NHLBI), R01GM078293 (NIGMS) |
Data sourced from Thomson Reuters' Web of Knowledge
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