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. Author manuscript; available in PMC: 2011 Sep 23.
Published in final edited form as: Carbohydr Res. 2010 Jul 17;345(14):1998–2003. doi: 10.1016/j.carres.2010.07.022

Fig. 3.

Fig. 3

The Tn-moieties of the IgA-Tn peptide were modified to T antigens with recombinant human T-synthase (core 1 β-(1→3)-galactosyltransferase), and the products analyzed by MS. Five products were detected, each differing by a mass of 162 due to the addition of a Gal residue. The non-glycosylated IgA peptide was not modified by T-synthase. Thus, IgA-Tn peptides were modified with one to five Gal residues, indicating that all 5 Tn-antigens of the peptide were accessible to galactosylation.