HOMOGENOUS IGA MONOMERS, DIMERS, TRIMERS AND TETRAMERS FROM THE SAME IGA MYELOMA SERUM

Starting from two IgA1 myeloma sera, the isolation of monoclonal monom eric, dimeric, trimeric and tetrameric IgA in a high state of purity a nd size homogeneity for each serum is described. The method combined r epetitive gelfiltrations on Ultrogel AcA22 with affinity chromatograph y on Jacalin-Sepharose. These various forms of pure polymeric IgA obta ined 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 lec tins.