Abstract
Analysis of protein post-translational modifications (PTM) is one of major objectives of proteomics, because status and their changes of PTM may suggest significance of the modification for particular protein function, and could not presumed by genomic or transcriptomic analyses. Thus, we focused protein glycosylation and developed a method for LC/MS-based large-scale identification of N-glycosylated proteins. This method composed of (1) lectin column-mediated affinity capture of glycopeptides from protease digest of sample protein mixtures; (2) peptide-N-glycanase-catalyzed incorporation of a stable isotope tag, 18 O, at N-glycosylation site; and (3) identification of the labeled peptides by LC/MS. We applied this method to the characterization of N-glycoproteins from crude extracts of C.elegans and mouse tissues using multiple lectin columns with distinct binding specificity.
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