As a post translational modification protein glycosylation plays a crucial role in protein
signaling, binding, kinetics and folding. In disease diagnosis and prognosis, monitoring …

Sialylation and sialic acid linkage in N-glycans are markers of disease but are analytically
challenging to quantify. A capillary electrophoresis method is reported that integrates a …

A thermally reversible nanogel is used in capillary electrophoresis to create discrete regions
for a galactosyltransferase reaction and separation. The β1–4 galactosyltransferase …

Glycosylated human IgG contains fucosylated biantennary N-glycans with different
modifications including N-acetylglucosamine, which bisects the mannose core. Although …

This chapter highlights recent developments in the analysis of proteins glycosylated of the
amino groups (N) of asparagine residues (ie, N-glycans) by capillary electrophoresis (CE) …

We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its
suitability for use in establishing a carbohydrate-mapping database that would enable a …

Linkage isomers (α-2, 3-or α-2, 6-linkage) of sialylated N-glycans are involved in the
emergence and progression of some diseases, so they are of great significance for …

This review summarizes our recent works concerned on the analysis of glycoprotein
glycans. Glycoprotein glycans are highly complicated and have variations that number into …

The study of N-linked glycans is among the most challenging bioanalytical tasks because of
their complexity and variety. The presence of glycoform families that differ only in branching …

Analysis of N‐glycan structures has been gaining attentions over the years due to their
critical importance to biopharma‐based applications and growing roles in biological …