This paper reports studies comparing the relative degree of sialylation among human serum
glycoproteins carrying complex biantennary N-linked, hybrid, and high-mannose …

A novel approach for the determination of N-glycans in glycoproteins has been developed
based on a combination of deglycosylation, chemoenzymatic labeling, and high …

The reducing oligosaccharides released from α1-acid glycoprotein (AGP) by conventional
hydrazinolysis have been analyzed by two different mapping techniques, using high-pH …

Fidelity of glycan structures is a key requirement for biotherapeutics, with carbohydrates
playing an important role for therapeutic efficacy. Comprehensive glycan profiling …

The structural characterization and quantification of the glycome of cells and glycoproteins is
necessary for the understanding of glycan functions in Biology, the development of …

We describe a simple and sensitive two-dimensional sugar-mapping technique of 8-amine-
1, 3, 6-naphthalene trisulfonic acid derivatives (ANTS derivatives) of neutral and …

Protein sialylation participates many biological processes in a linkage-specific manner, and
aberrant sialylation has been associated with many malignant diseases. Mass spectrometry …

In contrast to the conventional combination of physical, chemical and enzymatic methods
used for a structural analysis of glycans in glycoproteins, alternative methods involve affinity …

Profiling specific glycans in histopathological samples is hampered by the lack of selective
and sensitive tools for their detection. Here, we report on the development of …

Glycosylation is one of the most common protein modifications. Each glycoprotein can be
glycosylated at multiple glycosites, and each glycosites can be modified by different glycans …