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- W21546043 abstract "N-linked oligosaccharides are complex non-template-derived structures that are attached to the side chains of asparagine, via the nitrogen atom. Specific changes in the N-glycans of serum glycoproteins have been associated with the pathogenesis of many diseases. The oligosaccharides present on the C(H)2 domain of immunoglobulins are known to modulate the effector functions of the molecule. These glycans provoke various biological effects, necessitating the development of robust high-throughput technology in order to fully characterize the N-glycosylation profile. This chapter describes in detail four methods to release N-glycans from the glycoprotein of interest. Two of these protocols, referred to as the In-Gel Block and 1D sodium dodecyl sulfate-polyacrylamide gel electrophoresis methods, require immobilization of the glycoprotein prior to analysis. An automated method is also described, involving the purification of immunoglobulins directly from fermentation media, and, finally, an In-solution method is detailed, which directly releases the N-glycans into solution. HILIC and WAX-HPLC are used to analyze the N-glycan profile. Exoglycosidase enzymes digestion arrays, in combination with computer-assisted data analysis, are used to determine both the sequence and linkage of the N-glycans present." @default.
- W21546043 created "2016-06-24" @default.
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- W21546043 date "2012-01-01" @default.
- W21546043 modified "2023-09-25" @default.
- W21546043 title "High-Throughput Quantitative N-Glycan Analysis of Glycoproteins" @default.
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- W21546043 doi "https://doi.org/10.1007/978-1-61779-921-1_19" @default.
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