title: Analytical and Functional Aspects of Antibody Sialylation.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Natural Resources and Applied Life Sciences (BOKU), Muthgasse 18, 1190, Vienna, Austria.
authors.forename: Johannes
authors.initials: J
authors.lastname: Stadlmann
authors.forename: Martin
authors.initials: M
authors.lastname: Pabst
authors.forename: Friedrich
authors.initials: F
authors.lastname: Altmann
mesh_terms: D000906:Antibodies / Q000276:immunology / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000276:immunology / Q000378:metabolism*; D007074:Immunoglobulin G / Q000276:immunology / Q000378:metabolism*; D007249:Inflammation / Q000276:immunology; D018836:Inflammation Mediators / Q000276:immunology*; D012794:Sialic Acids / Q000737:chemistry*
chemical_list: D000906:Antibodies; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D018836:Inflammation Mediators; D012794:Sialic Acids
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