An Application of Electrostatic Repulsion Hydrophilic Interaction Chromatography in Phospho- and Glycoproteome Profiling of Epicardial Adipose Tissue in Obesity Mouse
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-func...
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Published in | Mass spectrometry letters Vol. 3; no. 2; pp. 39 - 42 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
한국질량분석학회
01.06.2012
사단법인 한국질량분석학회 |
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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. KCI Citation Count: 2 |
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AbstractList | 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 |
Author | Injae Hwang Jae Bum Kim Hookeun Lee Trang Huyentran Jong-moon Park |
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Title | An Application of Electrostatic Repulsion Hydrophilic Interaction Chromatography in Phospho- and Glycoproteome Profiling of Epicardial Adipose Tissue in Obesity Mouse |
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