We are analyzing https://link.springer.com/article/10.1007/s10875-010-9409-2.

Title:
Analytical and Functional Aspects of Antibody Sialylation | Journal of Clinical Immunology
Description:
Materials and methods This review focuses on the role of antibody sialylation and methods for its quantitation. The recent attribution of the anti-inflammatory activity of IgG to the sialylation of its glycans in the Fc region has raised interest in the fine structure and analysis of the glycans. The anti-inflammatory fraction of intravenous IgG could be isolated with the Sambucus nigra lectin. Experimental strategies for the assessment of antibody sialylation are discussed. Results Thorough analysis of the lectin-binding fraction revealed that the antibody Fc region only binds to S. nigra lectin when two sialic acids are present, whereas for other glycoprotein ligands, one sialic acid appears sufficient.
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Keywords {🔍}

igg, glycans, article, google, scholar, cas, pubmed, glycosylation, sialylation, antibody, sialic, analysis, fab, nglycans, antiinflammatory, sna, fraction, ivig, found, mass, methods, region, acid, table, human, sialylated, study, access, stadlmann, pabst, lectin, glycoforms, fragments, binding, data, open, altmann, structure, acids, antibodies, hplc, information, activity, neutral, glycopeptides, lcesims, glycan, obtained, monosialylated, disialylated,

Topics {✒️}

normal-phase hplc gave martin pabst & friedrich altmann entire anti-inflammatory activity anti-inflammatory activity depended ivig anti-inflammatory activity improve antibody-based therapeutics article download pdf mass + retention time = structure postlabeling purification method lectin-affinity fraction holds contrasting glycosylation profiles n-linked oligosaccharide structures sialylated antibody n-glycans related subjects anti-inflammatory potency analyzing oligosaccharide profiles lc-esi-ms work sialic acid–binding lectin anti-inflammatory activity normal-phase hplc igg-update n-glycans anti-inflammatory efficacy anti-inflammatory effect [22] anti-inflammatory power anti-inflammatory fraction n-linked oligosaccharides released carbon lc-esi-ms liquid chromatography combined privacy choices/manage cookies enormous resolution powers unusually high degree sialylated n-glycans found dissolved-state charge lectin-binding fraction revealed article stadlmann glycosylation profiling sialic acid loss sialic acid residue add sialic acid full access highly interesting features applied life sciences open access human platelet antigens soc mass spectrom inter-laboratory study quantifying n-glycosylation n-glycosylation sites regulated glycosylation patterns sialic acid occur

Questions {❓}

Considering the spatial constraints in the Fc glycosylation pocket [2], a most interesting question to raise is “what is the impact of a high degree of sialylation of Fc glycans on protein structure?

Schema {🗺️}

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         description:This review focuses on the role of antibody sialylation and methods for its quantitation. The recent attribution of the anti-inflammatory activity of IgG to the sialylation of its glycans in the Fc region has raised interest in the fine structure and analysis of the glycans. The anti-inflammatory fraction of intravenous IgG could be isolated with the Sambucus nigra lectin. Experimental strategies for the assessment of antibody sialylation are discussed. Thorough analysis of the lectin-binding fraction revealed that the antibody Fc region only binds to S. nigra lectin when two sialic acids are present, whereas for other glycoprotein ligands, one sialic acid appears sufficient.
         datePublished:2010-04-14T00:00:00Z
         dateModified:2010-04-14T00:00:00Z
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            Internal Medicine
            Medical Microbiology
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      description:This review focuses on the role of antibody sialylation and methods for its quantitation. The recent attribution of the anti-inflammatory activity of IgG to the sialylation of its glycans in the Fc region has raised interest in the fine structure and analysis of the glycans. The anti-inflammatory fraction of intravenous IgG could be isolated with the Sambucus nigra lectin. Experimental strategies for the assessment of antibody sialylation are discussed. Thorough analysis of the lectin-binding fraction revealed that the antibody Fc region only binds to S. nigra lectin when two sialic acids are present, whereas for other glycoprotein ligands, one sialic acid appears sufficient.
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         Antibody glycosylation
         sialic acid
         IVIG
         anti-inflammatory
         Immunology
         Infectious Diseases
         Internal Medicine
         Medical Microbiology
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