Retention Order Reversal of Phosphorylated and Unphosphorylated Peptides in Reversed-Phase LC/MS
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- OGATA Kosuke
- Graduate School of Pharmaceutical Sciences, Kyoto University
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- KROKHIN Oleg V.
- Manitoba Centre for Proteomics and Systems Biology and Department of Internal Medicine, University of Manitoba
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- ISHIHAMA Yasushi
- Graduate School of Pharmaceutical Sciences, Kyoto University
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<p>Protein phosphorylation is one of the most ubiquitous post-translational modifications in humans, and trypsin-digested phosphorylated peptides have been analyzed by reversed phase LC/MS using C18-silica columns under acidic conditions to profile human phosphoproteomes. Here, we report that phosphopeptides generally exhibit stronger retention than their unphosphorylated counterparts when C18-silica columns are used with acetic acid or formic acid as an ion-pairing reagent, whereas the retention order is reversed when less hydrophobic stationary phases such as C4-silica columns are employed. Similarly the retention reversal is observed when more hydrophobic ion-pairing reagents such as trifluoroacetic acid are used with C18-silica columns. These phenomena could be explained by the smaller S-values of phosphopeptides in linear solvation strength theory, based on the reduced net charge caused by intramolecular interaction between phosphate and basic groups.</p>
収録刊行物
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- Analytical Sciences
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Analytical Sciences 34 (9), 1037-1041, 2018-09-10
社団法人 日本分析化学会
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詳細情報 詳細情報について
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- CRID
- 1390845712998256128
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- NII論文ID
- 130007474696
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- NII書誌ID
- AA10500785
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- ISSN
- 13482246
- 09106340
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- HANDLE
- 2433/244860
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- NDL書誌ID
- 029215269
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- PubMed
- 30058604
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- Web Site
- http://id.ndl.go.jp/bib/029215269
- https://ndlsearch.ndl.go.jp/books/R000000004-I029215269
- https://link.springer.com/content/pdf/10.2116/analsci.18SCP11.pdf
- https://link.springer.com/article/10.2116/analsci.18SCP11/fulltext.html
- https://www.jstage.jst.go.jp/article/analsci/34/9/34_18SCP11/_pdf
- https://search.jamas.or.jp/link/ui/2019147704
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- en
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