Homogenous IgA monomers, dimers, trimers and tetramers from the same IgA myeloma serum.
Vaerman, Jean-Pierre;Langendries, Agnès;Vander Maelen, C
(1995) Immunological Investigations : a journal of molecular and cellular immunology — Vol. 24, n° 4, p. 631-641 (1995)
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Authors
Vaerman, Jean-PierreUCLouvain
Author
Langendries, AgnèsUCLouvain
Author
Vander Maelen, C
Author
Abstract
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.
Vaerman, J.-P., Langendries, A., & Vander Maelen, C. (1995). Homogenous IgA monomers, dimers, trimers and tetramers from the same IgA myeloma serum. Immunological Investigations : a journal of molecular and cellular immunology, 24(4), 631-641. https://doi.org/10.3109/08820139509066863 (Original work published 1995)