In-depth analysis of site-specific N-glycosylated alpha 1 acid glycoprotein and vitronectin from human plasma

摘要

Glycoproteins is one of the most common posttranslational modifications and related to protein folding, quality control, sorting and secretion. In glycosylation, glycan are attached to proteins that are related to the stability of the polypeptide folding structure, cell-cell adhesion and signal transduction. Therefore, the characterization of site-specific microheterogeneity in glycoprotein is N-glycoproteins is very important for understanding cell biology and disease process. In this study, the intact N-glycopeptides of alpha 1 acid glycoprotein(AGP) and vitronectin which are proteins well known to be related to disease in human blood sample were site-specifically analyzed by tandem mass spectrometry combined with hydrophilic interaction liquid chromatography (HILIC) enrichment.