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Article: Fully automatable two-dimensional hydrophilic interaction liquid chromatography-reversed phase liquid chromatography with online tandem mass spectrometry for shotgun proteomics

TitleFully automatable two-dimensional hydrophilic interaction liquid chromatography-reversed phase liquid chromatography with online tandem mass spectrometry for shotgun proteomics
Authors
KeywordsHilic-Rp
Orthogonality
Proteomics
Two-Dimensional Liquid Chromatography
Issue Date2012
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/jss
Citation
Journal Of Separation Science, 2012, v. 35 n. 14, p. 1755-1763 How to Cite?
AbstractWe have developed a fully automatable two-dimensional liquid chromatography platform for shotgun proteomics analyses based on the online coupling of hydrophilic interaction liquid chromatography (HILIC) - using a nonionic type of TSKgel Amide 80 at either pH 6.8 (neutral) or 2.7 (acidic) - with conventional low-pH reversed-phase chromatography. Online coupling of the neutral-pH HILIC and reversed phase chromatography systems outperformed the acidic HILIC-reversed phase chromatography combination, resulting in 18.4% (1914 versus 1617 nonredundant proteins) and 41.6% (12,989 versus 9172 unique peptides) increases in the number of identified peptides and proteins from duplicate analyses of Rat pheochromocytoma lysates. Armed with this optimized HILIC-reversed phase liquid chromatography platform, we identified 2554 nonredundant proteins from duplicate analyses of a Saccharomyces cerevisiae lysate, with the detected protein abundances spanning from approximately 41 to 10 6 copies per cell, which contained up to approximately 2092 different validated protein species with a dynamic range of concentrations of up to approximately 10 4. This present study establishes a fully automated platform as a promising methodology to enable online coupling of different hydrophilic HILIC and reversed phase chromatography systems, thereby expanding the repertoire of multidimensional liquid chromatography for shotgun proteomics. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Persistent Identifierhttp://hdl.handle.net/10722/168658
ISSN
2015 Impact Factor: 2.741
2015 SCImago Journal Rankings: 1.041
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhao, Yen_US
dc.contributor.authorKong, RPWen_US
dc.contributor.authorLi, Gen_US
dc.contributor.authorLam, MPYen_US
dc.contributor.authorLaw, CHen_US
dc.contributor.authorLee, SMYen_US
dc.contributor.authorLam, HCen_US
dc.contributor.authorChu, IKen_US
dc.date.accessioned2012-10-08T03:24:05Z-
dc.date.available2012-10-08T03:24:05Z-
dc.date.issued2012en_US
dc.identifier.citationJournal Of Separation Science, 2012, v. 35 n. 14, p. 1755-1763en_US
dc.identifier.issn1615-9306en_US
dc.identifier.urihttp://hdl.handle.net/10722/168658-
dc.description.abstractWe have developed a fully automatable two-dimensional liquid chromatography platform for shotgun proteomics analyses based on the online coupling of hydrophilic interaction liquid chromatography (HILIC) - using a nonionic type of TSKgel Amide 80 at either pH 6.8 (neutral) or 2.7 (acidic) - with conventional low-pH reversed-phase chromatography. Online coupling of the neutral-pH HILIC and reversed phase chromatography systems outperformed the acidic HILIC-reversed phase chromatography combination, resulting in 18.4% (1914 versus 1617 nonredundant proteins) and 41.6% (12,989 versus 9172 unique peptides) increases in the number of identified peptides and proteins from duplicate analyses of Rat pheochromocytoma lysates. Armed with this optimized HILIC-reversed phase liquid chromatography platform, we identified 2554 nonredundant proteins from duplicate analyses of a Saccharomyces cerevisiae lysate, with the detected protein abundances spanning from approximately 41 to 10 6 copies per cell, which contained up to approximately 2092 different validated protein species with a dynamic range of concentrations of up to approximately 10 4. This present study establishes a fully automated platform as a promising methodology to enable online coupling of different hydrophilic HILIC and reversed phase chromatography systems, thereby expanding the repertoire of multidimensional liquid chromatography for shotgun proteomics. © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.en_US
dc.languageengen_US
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/jssen_US
dc.relation.ispartofJournal of Separation Scienceen_US
dc.subjectHilic-Rpen_US
dc.subjectOrthogonalityen_US
dc.subjectProteomicsen_US
dc.subjectTwo-Dimensional Liquid Chromatographyen_US
dc.titleFully automatable two-dimensional hydrophilic interaction liquid chromatography-reversed phase liquid chromatography with online tandem mass spectrometry for shotgun proteomicsen_US
dc.typeArticleen_US
dc.identifier.emailChu, IK:ivankchu@hku.hken_US
dc.identifier.authorityChu, IK=rp00683en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/jssc.201200054en_US
dc.identifier.pmid22807358-
dc.identifier.scopuseid_2-s2.0-84864128566en_US
dc.identifier.hkuros211430-
dc.identifier.hkuros208684-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84864128566&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume35en_US
dc.identifier.issue14en_US
dc.identifier.spage1755en_US
dc.identifier.epage1763en_US
dc.identifier.isiWOS:000306493700008-
dc.publisher.placeGermanyen_US
dc.identifier.scopusauthoridZhao, Y=55319071700en_US
dc.identifier.scopusauthoridKong, RPW=35217869000en_US
dc.identifier.scopusauthoridLi, G=55319115500en_US
dc.identifier.scopusauthoridLam, MPY=35302594800en_US
dc.identifier.scopusauthoridLaw, CH=54922894500en_US
dc.identifier.scopusauthoridLee, SMY=54947119900en_US
dc.identifier.scopusauthoridLam, HC=55319109600en_US
dc.identifier.scopusauthoridChu, IK=7103327484en_US

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