DICP OpenIR
Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides
Cao, Liwei; Yu, Long; Guo, Zhimou; Li, Xiuling; Xue, Xinya; Liang, Xinmiao
KeywordSax Erlic Glycopeptides Enrichment Mass Spectrometry
Source PublicationJOURNAL OF CHROMATOGRAPHY A
2013-07-19
DOI10.1016/j.chroma.2013.05.037
Volume1299Pages:18-24
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS KeywordN-LINKED GLYCOPROTEINS ; TANDEM MASS-SPECTROMETRY ; SOLID-PHASE EXTRACTION ; GLYCOSYLATION HETEROGENEITY ; BIOMARKER DISCOVERY ; AFFINITY CAPTURE ; FACILE SYNTHESIS ; IDENTIFICATION ; SEPARATION ; DATABASE
AbstractGlycoproteins are involved in various cellular activities, including inter- and extracellular signaling. However, glycopeptide signals are significantly suppressed by coeluting non-glycosylated peptides in mass spectrometry-based analysis. For detailed elucidation of the biological functions of glycoproteins, selective enrichment of glycopeptides from non-glycosylated peptides is crucial. In the present study, a SAX material, XCharge SAX, was used in a column in the ERLIC mode with the aim of specifically enriching glycopeptides. Enrichment conditions were initially optimized, and selectivity, glycosylation heterogeneity coverage and detection sensitivity of XCharge SAX were subsequently assessed. In the selectivity assessment, glycopeptides were effectively isolated from a peptide mixture (human serum immunoglobulin G (IgG) and human serum albumin digests) and a tryptic digest of human serum using XCharge SAX. In the evaluation of glycosylation heterogeneity coverage, five glycosites and eleven glyco peptides from horseradish peroxidase were identified after enrichment with XCharge SAX. In detection sensitivity assessment, glycopeptides within four orders of magnitude were identified after enrichment with XCharge SAX. In addition, volatile solvents were used in the loading and eluting buffers so that desalting was not necessary for ERLIC fractions. Our results collectively support the utility of XCharge SAX as a suitable chromatographic material for global glycosylation site analysis. (C) 2013 Elsevier B.V. All rights reserved.
Language英语
WOS IDWOS:000321424000003
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/137932
Collection中国科学院大连化学物理研究所
AffiliationChinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
Recommended Citation
GB/T 7714
Cao, Liwei,Yu, Long,Guo, Zhimou,et al. Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides[J]. JOURNAL OF CHROMATOGRAPHY A,2013,1299:18-24.
APA Cao, Liwei,Yu, Long,Guo, Zhimou,Li, Xiuling,Xue, Xinya,&Liang, Xinmiao.(2013).Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides.JOURNAL OF CHROMATOGRAPHY A,1299,18-24.
MLA Cao, Liwei,et al."Application of a strong anion exchange material in electrostatic repulsion-hydrophilic interaction chromatography for selective enrichment of glycopeptides".JOURNAL OF CHROMATOGRAPHY A 1299(2013):18-24.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Cao, Liwei]'s Articles
[Yu, Long]'s Articles
[Guo, Zhimou]'s Articles
Baidu academic
Similar articles in Baidu academic
[Cao, Liwei]'s Articles
[Yu, Long]'s Articles
[Guo, Zhimou]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Cao, Liwei]'s Articles
[Yu, Long]'s Articles
[Guo, Zhimou]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.