A Method for Large-Scale Analysis for N-linked Glycoproteins by the Glycosylation Site-Specific Stable Isotope-Labeling and LC/MS Shotgun Technology
Genome information constitutes a catalog of genes and proteins of an organism and allows genome-wide expression profiling of the transcriptome and proteome. A large body of evidence, however, suggests that many biological events are regulated not only by gene expression but also by post-translational modifications of proteins, such as glycosylation. Thus, the analysis of protein glycosylation is one of the most important issues of current proteomics research. We introduce here our strategy for large-scale “glycoproteome” analysis based on liquid chromatography-coupled mass spectrometry (LC/MS) shotgun technology.
KeywordsWheat Germ Agglutinin Protein Mixture Protein Glycosylation Hydrophilic Interaction Chromatography Complex Peptide Mixture
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- Kaji H, Kamiie J, Kawakami H, Kido K, Yamauchi Y, Shinkawa T, Taoka M, Takahashi N, Isobe T (2007) Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins. Mol Cell Proteomics 6:2100–2109PubMedCrossRefGoogle Scholar