The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Selective Zirconium Dioxide-Based Enrichment of Phosphorylated Peptides for Mass Spectrometric Analysis
Abstract
Due to the dynamic nature and low stoichiometry of protein phosphorylation, enrichment of phosphorylated peptides from proteolytic mixtures is often necessary prior to their characterization by mass spectrometry. Several phosphopeptide isolation strategies have been presented in the literature, including immobilized metal ion affinity chromatography. However, that technique suffers from poor selectivity and reproducibility. Recently, titanium dioxide-based columns have been successfully employed for phosphopeptide enrichment by several research groups. Here, we present, to our knowledge, the first demonstration of the utility of zirconium dioxide microtips for phosphopeptide isolation prior to mass spectrometric analysis. These microtips display similar overall performance as TiO2 microtips. However, more selective isolation of singly phosphorylated peptides was observed with ZrO2 compared to TiO2 whereas TiO2 preferentially enriched multiply phosphorylated peptides. Thus, these two chromatographic materials possess complementary properties. For alpha- and beta-casein, Glu-C digestion provided no evident advantage compared to trypsin digestion when combined with TiO2 or ZrO2 phosphopeptide enrichment.
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Cited by
Protein Analysis by Shotgun/Bottom-up Proteomics
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Catch me if you can: Mass spectrometry‐based phosphoproteomics and quantification strategies
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Metadata
- Authors
- Kweon, H. K., & Håkansson, K.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-02-07
- Volume
- 78
- Issue
- 6
- Pages
- 1743-1749
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2108136469
- Cited by
- 489
- References
- 23
- FWCI
- 22.19
- Type
- journal article
- Language
- en
- Open access
- closed
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