- P-ISSN 2233-4203
- E-ISSN 2093-8950
- 권한신청
- P-ISSN2233-4203
- E-ISSN2093-8950
- ESCI, SCOPUS, KCI
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An Application of Electrostatic Repulsion Hydrophilic Interaction Chromatography in Phospho- and Glycoproteome Profiling of Epicardial Adipose Tissue in Obesity Mouse
Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2012, v.3 no.2, pp.39-42
https://doi.org/10.5478/MSL.2012.3.2.39
(Gachon University)
(Seoul National University)
(Gachon University)
(Seoul National University,)
(Gachon University)
(Seoul National University)
(Gachon University)
(Seoul National University,)
(Gachon University)
Tran,
T. H.,
Hwang,
I.,
Park,
J.,
Kim,
J. B.,
&
Lee,
H.
(2012). . Mass Spectrometry Letters, 3(2), 39-42, https://doi.org/10.5478/MSL.2012.3.2.39
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Abstract
Phosphorylation and glycosylation are two of the most important and widespread post-translational modifications(PTMs) in an organism. Proteomics analysis of the PTMs has been challenged by low stoichiometry of the modified proteins andsuppression effects by high abundance proteins, typically no-functional house-keeping proteins. In this study, a novel methodwas applied for not only isolating PTM peptides from intact peptides but also concurrently characterizing of glyco- and phosphoproteomeusing electrostatic repulsion hydrophilic interaction chromatography (ERLIC) packed with silica coated by crosslinkedpolyethyleneimine. For 2 mg tryptic digest of mouse proteome of epicardial adipose tissue with fat diet, 802 N-glycosylatedpeptides of 316 glycoproteins and 159 phosphorylated peptides of 75 phosphoproteins were identified using HPLC chip/quadrupole time-of-flight (Q-TOF) tandem mass spectrometer.
- keywords
- ERLIC, Phosphoproteome enrichment, Glycoproteome enrichment, Simultaneous enrichment, PTMs
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- 투고일Submission Date
- 2012-05-07
- 수정일Revised Date
- 2012-05-19
- 게재확정일Accepted Date
- 2020-05-20
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