Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/80217
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dc.contributor.authorNg, Justin Tze-Yangen
dc.contributor.authorHao, Piliangen
dc.contributor.authorSze, Siu Kwanen
dc.date.accessioned2015-12-02T04:17:40Zen
dc.date.accessioned2019-12-06T13:45:07Z-
dc.date.available2015-12-02T04:17:40Zen
dc.date.available2019-12-06T13:45:07Z-
dc.date.issued2014en
dc.identifier.citationNg, J. T.-Y., Hao, P., & Sze, S. K. (2014). The Use of Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) for Proteomics Research. Mass Spectrometry Letters, 5(4), 95-103.en
dc.identifier.issn2233-4203en
dc.identifier.urihttps://hdl.handle.net/10356/80217-
dc.description.abstractCharacterization and studies of proteome are challenging because biological samples are complex, with a wide dynamic range of abundance. At present the proteins are identified by digestion into peptides, with subsequent identification of the peptides by mass spectrometry (MS). MS is a powerful technique for the purpose, but it cannot identify every peptide in such complex mixtures simultaneously. For accurate analysis and quantification it is important to separate the peptides first by chromatography into fractions of a size that MS can handle. With these less complex fractions, the probability is increased of identifying peptides of low abundance that would otherwise experience ion suppression effects due to the presence of peptides of high abundance. Enrichment for peptides with certain post-translational modifications helps to increase their detection rates as well. Electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) is a mixed-mode chromatographic technique which combines the use of electrostatic repulsion and hydrophilic interaction. This review provides an overview of ERLIC and its various proteomics applications. ERLIC has been demonstrated to have good orthogonality to reverse phase liquid chromatography (RPLC), making it useful as a first dimension in multidimensional liquid chromatography (MDLC) and fractionation of digests in general. Peptides elute in order of their isoelectric points and polarity. ERLIC has also been successfully utilized for the enrichment for phosphopeptides and glycopeptides, facilitating their identification. In addition, it is promising for the study of peptide deamidation. ERLIC performs comparably well or better than established methods for these various applications, and serves as a viable and efficient workflow alternative.en
dc.description.sponsorshipNMRC (Natl Medical Research Council, S’pore)en
dc.format.extent9 p.en
dc.language.isoenen
dc.relation.ispartofseriesMass Spectrometry Lettersen
dc.rightsAll MS Letters content is Open Access, meaning it is accessible online to everyone, without fee and authors’ permission. All MS Letters content is published and distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org /licenses/by/3.0/). Under this license, authors reserve the copyright for their content; however, they permit anyone to unrestrictedly use, distribute, and reproduce the content in any medium as far as the original authors and source are cited. For any reuse, redistribution, or reproduction of a work, users must clarify the license terms under which the work was produced.en
dc.subjectGlycosylationen
dc.subjectDeamidationen
dc.subjectMass spectrometryen
dc.subjectERLICen
dc.subjectMDLCen
dc.subjectPhosphorylationen
dc.titleThe Use of Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) for Proteomics Researchen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.5478/MSL.2014.5.4.95en
dc.description.versionPublished versionen
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