The Analysis of Structural Diversity in the Antibody Response
The heterogeneity of the antibody response presented a major problem to im-munochemists wishing to study antibody structures. Such studies required large amounts of a single immunoglobulin molecule, which could not be obtained from normal immune sera. The discovery that multiple myelomas were tumors originating from a single clone of antibody-producing cells and hence gave rise to a homogeneous source of immunoglobulin was therefore extremely important and enabled the first structural studies of immunoglobulin molecules to be carried out.1,2 Mouse plasmacytomas were particularly important because they provided homogeneous sources of antibodies that could be passaged and adapted to cell culture.3,4 The use of myelomas provided a vast amount of information concerning immunoglobulin structure.5–7 Myelomas also provided the early material to study the immunoglobulin gene organization of mouse and man. It was clear from these studies that a vast amount of structural diversity can be generated from a finite number of immunoglobulin genes (reviewed in Ref. 8). However, a detailed study of the structural diversity of the antibody response to a defined antigen was not possible, since myelomas do not originate from a response to a defined antigen. The most exciting aspect, namely the change during the maturation of the response, could not be defined at the molecular level.
KeywordsAntibody Response Heavy Chain Homogeneous Source mRNA Template Nucleic Acid Level
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