Abstract
The lectins Sambucus nigraagglutinin (SNA) and Ricinus communisagglutinin (RCA), specific for α2,6 linked sialylation, and terminal galactose respectively were used to study the occurrence, linkage and distribution of human immunoglobulin G (IgG) sialylation. SNA was shown to bind N-glycan α2,6-linked sialic acid only. Sialidase analysis confirmed that this is the dominant, if not exclusive linkage. Total IgG sialylation was estimated at 1.0[emsp4 ]μg SA/mg IgG (or about 0.5 mole per mole) using a biochemical sialic acid assay. SNA displayed strong binding to the IgG Fab fragment in both its native and denatured state. In contrast, SNA failed to bind the IgG Fc fragment in its native form, but displayed strong binding after the Fc was denatured. This allowed the construction of quantitative assays capable of measuring both IgG Fab and Fc α2,6-sialylation without the need for enzymatic peptide digestion.
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Dalziel, M., McFarlane, I. & Axford, J.S. Lectin analysis of human immunoglobulin G N-glycan sialylation. Glycoconj J 16, 801–807 (1999). https://doi.org/10.1023/A:1007183915921
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DOI: https://doi.org/10.1023/A:1007183915921