Abstract
Glycosylation is the most common protein modification post translation and sugar chains play important roles in a variety of physiological functions, e.g., recognition of proteins and cells, tumor invasion and metastasis, etc. The current study used multiple lectin chromatography in tandem to sequentially extract serum sub-glycoproteome of N-linked high-mannose and sialic acid type, and O-linked type, respectively. One-dimensional and two-dimensional SDS-PAGE showed distinct maps of each serum sub-glycoproteome. For N-linked sialic acid glycoproteome, we identified a total of 14 glycoproteins from 12 differential protein spots by ESI-MS/MS. In conclusion, sequential extraction of multiple serum glycoproteome by lectins in tandem can effectively decrease complexity and dynamic range of serum proteome, which leads to improvement of biomarker discovery for disease diagnosis and monitoring with clinical relevance.
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