An Application of Electrostatic Repulsion Hydrophilic Interaction Chromatography in Phospho- and Glycoproteome Profiling of Epicardial Adipose Tissue in Obesity Mouse

• Published in: Mass spectrometry letters Vol. 3; no. 2; pp. 39 - 42
• Main Authors: Trang Huyentran, Injae Hwang, Jong-moon Park, Jae Bum Kim, Hookeun Lee
• Format: Journal Article
• Language: English
• Published: 한국질량분석학회 01.06.2012; 사단법인 한국질량분석학회
• Subjects: 화학; Glycoproteome enrichment; ERLIC; Phosphoproteome enrichment; Simultaneous enrichment; PTMs
• ISSN: 2233-4203; 2093-8950
• DOI: 10.5478/MSL.2012.3.2.39

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. KCI Citation Count: 2