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an improved protocol for n-glycosylation analysis of gel-separated sialylated glycoproteins by maldi-toftof一种改进的协议n-glycosylation分析gel-separated sialylated maldi-toftof糖蛋白
An Improved Protocol for N-Glycosylation Analysis of
Gel-Separated Sialylated Glycoproteins by MALDI-TOF/
TOF
1 1 2
Piliang Hao *, Yan Ren , Yongming Xie
1 Beijing institute of Genomics, Chinese Academy of Science, Beijing, China, 2 Applied Biosystems Inc. (China), Shanghai, China
Abstract
Different glycoforms of some proteins have been identified as differential spots for certain diseases in 2-DE, indicating
disease-related glycosylation changes. It is routine to determine the site-specific glycosylation of nonsialylated N-
glycoproteins from a single gel spot, but some obstacles still exist in analyzing sialylated glycoproteins due to the lability
and higher detection limit of acid glycans in MALDI-TOF/TOF analysis. Thus, we present an improved protocol here. Tryptic
glycopeptides were separated and subjected to MALDI-TOF/TOF analysis, resulting in the identification of site-specific
glycosylation of high-intensity glycopeptides. Sequential deglycosylation and desialylation were used to improve the
identification of glycosylation sites and desialylated glycans. The site-specific glycosylation of large glycopeptides and low-
intensity glycopeptides was deduced based on the masses of glycopeptides, deglycosylated peptides and desialylated
glycans. By applying it to 2-DE separated human serum, the difference of N-glycosylation was successfully determined for
a1-antitrypsin between different gel spots.
Citation: Hao P, Ren Y, Xie Y (2010) An Improved Protocol for N-Glycosylation Analysis of Gel-Separated Sialylated Glycoproteins by MALDI-TOF/TOF. PLoS
ONE 5(11): e15096. doi:10.1371/journal.pone.0015096
Editor: Vladimir N. Uversky, University of South Florida College of Medicine, United States of America
Received A
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