Fig. 1
From: Pathogenic role of glycan-specific IgG antibodies in IgA nephropathy
Verification of successful preparation of ddIgA1 and IgG-dd-IgA1 complexes. a Glycosylation status of IgA1 and ddIgA1 were detected by two lectins, SNA and VVL, which recognized sialic acid (SA), and N-Acetylgalactosamine (GalNAc), respectively. IgA1 molecules showed high binding capacity to SNA (blank column) and low binding capacity to VVL (filled column). In contrary, ddIgA1 showed low binding capacity to SNA (blank column) and high binding capacity to VVL (filled column). b Existence of dd-IgA1 (upper panel) and IgG (lower panel) in IgG-ddIgA1 complexes were tested by Western blot analysis. Both IgA1 and IgG were existence in IgG-ddIgA1 complexes of recruited individuals (lane 1–4). Isolated ddIgA1 (lane 5), IgA1 (lane 6) and IgG (lane 7) were used as references