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      Sera of IgA nephropathy patients contain a heterogeneous population of relatively cationic alpha-heavy chains.

      Nephron. Physiology
      Adult, Blotting, Western, Cations, Densitometry, methods, Electrophoresis, Gel, Two-Dimensional, Glomerulonephritis, IGA, blood, Humans, Immunoglobulin Heavy Chains, Immunoglobulin alpha-Chains, Lectins, Middle Aged

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          Abstract

          Sera of IgA nephropathy (IgAN) patients and normal subjects were analysed by two-dimensional (2-D) gel electrophoresis. Densitometric analysis of the 2-D gels of IgAN patients and normal subjects revealed that their protein maps were comparable. There was no shift of pI values in the major alpha-heavy chain spots. However, the volume of the alpha-heavy chain bands were differently distributed. Distribution was significantly lower at the anionic region in IgAN patients (mean anionic:cationic ratio of 1.184 +/- 0.311) as compared to normal healthy controls (mean anionic:cationic ratio of 2.139 +/- 0.538). Our data are in support of the previously reported findings that IgA1 of IgAN patients were lacking in sialic acid residues.

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          Iga binding lectins isolated from distinct artocarpus species demonstrate differential specificity

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