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 …

Sialylated N-glycan isomers with α-2, 3 and α-2, 6 linkages play crucial and distinctive roles
in diverse physiological and pathological processes. Changes of α-2, 3-linked sialic acids in …

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 …

Isomeric N-glycans often vastly differ in their biological activities, hence the need for
methods that allow resolving and structurally characterizing them in biological material …

Sialylation can influence the stability, half-life, and immunogenicity of glycoproteins, but
sialylated N-glycans are known to be difficult to analyze. Human alpha1-acid glycoprotein …

Through direct coupling of capillary electrophoresis (CE) to mass spectrometry (MS) with a
sheathless interface, we have identified 77 potential N-glycan structures derived from …

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 …

Sialic acids have diverse biological roles, ranging from promoting up to preventing protein
and cellular recognition in health and disease. The various functions of these …

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

To characterize the structures of N-glycans derived from human serum, we report a strategy
that combines microchip electrophoresis, standard addition, enzymatic digestion, and matrix …