An understanding of the structure of antibodies has provided important insights into their function. The analysis of antibody structure also paved the way to the eventual characterization of the genetic organization of antigen receptor genes in both B and T cells and the elucidation of the mechanisms of immune diversity, issues that will be considered in depth in Chapter 8.
Early studies of antibody structure relied on antibodies purified from the blood of individuals immunized with various antigens. It was not possible, using this approach, to define antibody structure precisely because serum contains a mixture of different antibodies produced by many clones of B lymphocytes that may each respond to different portions (epitopes) of an antigen (so-called polyclonal antibodies). A major breakthrough in obtaining antibodies whose structures could be elucidated was the discovery that patients with multiple myeloma, a monoclonal tumor of antibody-producing plasma cells, often have large amounts of biochemically identical antibody molecules (produced by the neoplastic clone) in their blood and urine. Immunologists found that these antibodies could be purified to homogeneity and analyzed. The recognition that myeloma cells make monoclonal immunoglobulins led to an extremely powerful technique for producing monoclonal antibodies, described later in the chapter. The availability of homogeneous populations of antibodies and monoclonal antibody-producing plasma cells permitted the detailed structural analysis and molecular cloning of the genes for individual antibody molecules, which remain some of the major advances in our understanding of the immune system.
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