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Analytical and Functional Aspects of Antibody Sialylation
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. T...
| Autores principales: | , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Springer US
2010
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883086/ https://www.ncbi.nlm.nih.gov/pubmed/20390325 http://dx.doi.org/10.1007/s10875-010-9409-2 |
| Sumario: | 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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