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. 1990 Jan 30;166(2):937-44.
doi: 10.1016/0006-291x(90)90901-x.

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

J L Franc  1 , N Venot, C Marriq
Affiliations

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

J L Franc et al. Biochem Biophys Res Commun. .

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 (Asn57 and Asn91). 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.

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