Organization of Immunoglobulin Genes
This extract was created in the absence of an abstract.
Excerpt
Both light and heavy chains of antibody (or immunoglobulin) molecules consist of two regions. About 100 residues at the amino-terminal ends of the polypeptide chains determine the specificity of the molecules and compose variable (V) regions, whereas the remaining residues determine the class or subclass of antibodies to which the molecule belongs and compose constant (C) regions. Two types of heterogeneities exist among antibody molecules. The first distinguishes about 20 types of molecules with respect to their C regions. In mice, three (κ, λI, and λII) and eight (δ, μ, γI, etc.) different C regions are known for the light and heavy chains, respectively. The second type of heterogeneity distinguishes millions of molecules differing with respect to their V regions. This heterogeneity is often called “antibody diversity,” and the question of whether the diversity in the structural genes coding for the V regions (V genes) arose in evolution or arises...
