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

다국어 초록 (Multilingual 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.

참고문헌 (Reference)

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