ArticleAnalytical chemistry2020
Quantification of the α2-6 Sialic Acid Linkage in Branched N-Glycan Structures with Capillary Nanogel Electrophoresis.
Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 23 citations in OpenAlex.
- Hairpin aptamer and ROS-sensitive microcapsule-mediated glycoprotein determination for the prognosis of colorectal cancer.Mikrochimica acta · 2024Article
- Fluorescent parallel electrophoresis assay of enzyme inhibition.Analytica chimica acta · 2024Article
- Microscale Quantification of the Inhibition of Neuraminidase Using Capillary Nanogel Electrophoresis.Analytical chemistry · 2022Article
- Capillary Nanogel Electrophoresis for the Determination of the β1-4 Galactosyltransferase Michaelis-Menten Constant and Real-Time Addition of Galactose Residues toAnalytical chemistry · 2021Article
- Isomer-Specific Monitoring of SialylatedFrontiers in molecular biosciences · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
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 unique combination of enzymes and lectins to modify sialylated N-glycans in real time in the capillary so that N-glycan structures containing α2-6-linked sialic acid are easily separated, detected, and quantified. In this study, N-glycans were sequentially cleaved by enzymes at the head of the separation capillary so that the presence of α2-6-linked sialic acids corresponded to a shift in the analyte migration time in a manner that enabled interpretation of the N-glycan structure. Following injection, only afucosylated N-glycan structures were passed through enzyme zones that contained α2-3 sialidase, followed by β1-3,4 galactosidase, which cleaved any terminal α2-3-linked sialic acid and underlying galactose yielding a terminal N-acetyl glucosamine. With this treatment complete, a third zone of α2-3,6,8 sialidase converted the remaining α2-6-linked sialic acid to terminal galactose. With these enzyme processing steps the α2-6-linked sialic acid residues on an N-glycan correlated directly to the number of terminal galactose residues that remained. The number of terminal galactose residues could be interpreted as a stepwise decrease in the migration time. Complex N-glycans from α-1-acid glycoprotein were analyzed using this approach, revealing that a limited number of α2-6-linked sialic acids were present with biantennary, triantennary, and tetraantennary N-glycans of α-1-acid glycoprotein generally containing 0 or 1 α2-6-linked sialic acid.
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Registered trials
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