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Over the last two decades a great deal of information has accumulated on the structure and function of the immunoglobulin molecules. Structural studies of the myeloma proteins defined the variable and constant regions. Analysis of the variable regions showed the existence of hypervariable regions (1) and began to give insight into the nature of the interaction between the antibody molecule and its specific antigen. The existence of both variable and constant regions on the same molecule gave rise to the concept "two genes-one polypeptide chain" (2), which challenged then-accepted genetic ideas. With the advent of modern molecular biologic techniques it became clear that the immunoglobulin (Ig) molecule, both heavy and light chain, was encoded by multiple DNA segments. In order to generate a gene encoding a functional Ig molecule, somatic rearrangements of distinct DNA segments must take place. For a complete light-chain gene a V region must be brought next to a J segment to create an active transcription unit. For a heavy-chain gene, V, D, and J segments must be assembled next to a constant-region gene; the initial constant-region gene utilized is the j.1 gene. In addition, during immune response maturation heavy-chain class switching can occur, whereupon
Annual Review of Immunology – Annual Reviews
Published: Apr 1, 1984
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