| Download | - View supplementary information part 1: Iodination on tyrosine residues during oxidation with sodium periodate in solid phase extraction of N-linked glycopeptides (XLS, 54 KiB)
- View supplementary information part 2: Iodination on tyrosine residues during oxidation with sodium periodate in solid phase extraction of N-linked glycopeptides (XLS, 58 KiB)
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| DOI | Resolve DOI: https://doi.org/10.1007/s13361-011-0262-1 |
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| Author | Search for: Cohen, Alejandro M.1; Search for: Kostyleva, Ripsik1; Search for: Chisholm, Kenneth A.1; Search for: Pinto, Devanand M.1ORCID identifier: https://orcid.org/0000-0002-0665-7041 |
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| Affiliation | - National Research Council of Canada. NRC Institute for Marine Biosciences
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| Format | Text, Article |
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| Subject | glycoproteomics; iodination; N-linked glycoproteins; hydrazide modified solid phase extraction; oxidation; sodium periodate |
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| Abstract | Solid-phase extraction of N-linked glycopeptides (SPEG) using hydrazide-modified supports has become a common sample preparation procedure in glycoproteomic experiments. We demonstrate that iodination of tyrosine residues occur in SPEG as a side reaction during an oxidation step with sodium periodate. MS/MS analysis of oxidized bovine serum albumin and carbonic anhydrase digests revealed a characteristic shift of m/z 125.9 on all y and b fragment ions containing the modified tyrosine residues. Selected reaction monitoring (SRM) measurements showed that the peak intensity from of the iodinated peptides increased during the course of oxidation. After an hour of oxidation, SRM analysis revealed that the strongest signal from an iodinated peptide was approximately one-tenth of the intensity of the corresponding unmodified peptide. Iodinated tyrosine residues were also identified in serum samples subjected to SPEG and analyzed by LC-ESI-MS/MS. We recommend assessing this side reaction by including iodotyrosine as a variable modification when performing database searches on SPEG experiments. For SRM-based acquisitions, we encourage the avoidance of tyrosine-containing glycopeptides or, if this is not practical, monitoring transitions that contain the potential modified iodinated tyrosine residue to monitor the presence of the iodinated form of the glycopeptide. |
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| Publication date | 2011-10-18 |
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| Publisher | American Chemical Society
Springer |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | NRC-IMB-7828 |
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| NPARC number | 21268626 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 0dcf4b3e-f490-4c73-9cfc-b3438a967f67 |
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| Record created | 2013-10-31 |
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| Record modified | 2024-06-28 |
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