The carbohydrate moiety of the glycoprotein allergen Ag-54, isolated from the mould Cladosporium herbarum, has been characterised partly, using acetolysis, methylation analysis, and n.m.r. spectroscopy. Ag-54 contained a highly branched galactoglucomannan and two branched mannogluco-oligosaccharide chains. The oligosaccharides contained terminal, (1----4)-, and (1----4,6)-linked alpha-Glc residues and terminal, (1----2)-, and some (1----3)-linked alpha-Man residues. The n.m.r. data indicated the galactoglucomannan to have a main chain made up of (1----6)-linked alpha-Man and (1----4)-linked alpha-Glc residues, with the latter attached to position 6 of alpha-Man residues. Oligosaccharides with (1----6)-linked beta-Galf and (1----2)-linked alpha-Man were attached to the main chain. Acetolysis of the galactoglucomannan yielded linear and branched oligosaccharides. The presence of (1----2,3)-linked alpha-Man residues indicated either that other than (1----6) linkages were present in the main chain or that there was 2,3-branching in the side chains.