Analytical performance of immobilized pronase for glycopeptide footprinting and implications for surpassing reductionist glycoproteomics.

ABSTRACT: A fully developed understanding of protein glycosylation requires characterization of the modifying oligosaccharides, elucidation of their covalent attachment sites, and determination of the glycan heterogeneity at specific sites. Considering the complexity inherent to protein glycosylation, establishing these features for even a single protein can present an imposing challenge. To meet the demands of glycoproteomics, the capability to screen far more complex systems of glycosylated proteins must be developed. Although the proteome wide examination of carbohydrate modification has become an area of keen interest, the intricacy of protein glycosylation has frustrated the progress of large-scale, systems oriented research on site-specific protein-glycan relationships. Indeed, the analytical

SUBMITTER: Dodds ED 

PROVIDER: S-EPMC2637306 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature