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Homogenous IgA monomers, dimers, trimers and tetramers from the same IgA myeloma serum
J P Vaerman1, A Langendries, C Vander Maelen
1Unit of Experimental Medicine, Catholic University of Louvain, Belgium.
Starting from two IgA1 myeloma sera, the isolation of monoclonal monomeric, dimeric, trimeric and tetrameric IgA in a high state of purity and size homogeneity for each serum is described. The method combined repetitive gel filtrations on Ultrogel AcA22 with affinity chromatography on Jacalin-Sepharose. These various forms of pure polymeric IgA obtained from the same monoclonal IgA should allow a precise comparison of their respective structure and reactivity with different IgA-binding proteins, such as IgA Fc-receptors, the polymeric Ig receptor, and lectins.
Starting from two IgA1 myeloma sera, the isolation of monoclonal monomeric, dimeric, trimeric and tetrameric IgA in a high state of purity and size homogeneity for each serum is described. The method combined repetitive gel filtrations on Ultrogel AcA22 with affinity chromatography on Jacalin-Sepharose. These various forms of pure polymeric IgA obtained from the same monoclonal IgA should allow a precise comparison of their respective structure and reactivity with different IgA-binding proteins, such as IgA Fc-receptors, the polymeric Ig receptor, and lectins.