A case of IgA2m(1) benign monoclonal gammopathy showed double IgA precipitate lines on immunoelectrophoresis.

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Serum from 56 year-old male patient with moderately elevated β-fraction by cellulose acetate electrophoresis was investigated. Immunoelectrophoresis of the serum showed obvious M-bow formation with anti-IgA antibody and also found to have another faint precipitation line which showed spur formation with the M-protein. Single Radial Immunodiffusion method for quantitation of IgA showed double precipitation rings. Initially we speculated that the M-protein as the half molecular IgA. Although, Sephacryl S-300 gel filtration of the M-protein bid not show any molecular aberrations. Also Jacalin, a lectin which is known to bound specifically to IgA1 of the IgA subclass, could not absorb this M-protein. From those findings described above, the M-protein in this patient was thought to be IgA2 type. In addition to this, SDS-PAGE under non-reducing condition showed discrete band at 45Kd and thought to be dimetric free light chains of the immunoglobulin. Since it was known that IgA2m (1) allotype easily release dimetric light chains from the IgA molecules in SDS-PAGE under non-reducing condition, we concluded that the M-protein in this patient as the IgA2m(1) allotype.
日本電気泳動学会の論文