Characterization of the two oligosaccharides present in the preferential hormonogenic domain of human thyroglobulin

Abstract

The N-terminal fragment of human thyroglobulin (residues 1 to 171) contains the preferential hormonogenic site of the molecule and 2 potential sites of N-glycosylation (Asn 57 and Asn 91). This fragment was isolated from a human thyroglobulin purified from a single goiter. The tryptic peptides bearing the glycosylation sites were separated by Bio-Gel P-30 and HPLC columns. The oligosaccharides borne at each site were analyzed, after tritium labeling, by concanavalin A-Sepharose and HPLC. At both sites the structures observed are heterogenous, with a majority of biantennary complex type structures.