A mathematical approach to the analysis of diversity in antibody gene families.
In this article, we develop a mathematical approach for the analysis of diversity in antibody gene families. This approach is arrived at by examing two general questions about protein populations: (1) What is a relative measure of the diversity exhibited by one protein family when compared with a second? (2) What is the probability that two protein populations were derived from a single common population? These quantitative approaches permit a variety of precise evolutionary, genetic, and developmental questions to be asked of antibody gene families. Using this methodology, we demonstrate that the diversity in mouse K-immunoglobulin chains is considerably greater than in their human K counterparts. We also show that the variable (Vl) regions of light chains associated with IgG and IgA immunoglobulins in the mouse appear to have been derived from a common population of Vl genes. This approach also can be used to analyse sequence data from other informational multigene families.
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D002460:Cell Line; D006801:Humans; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains; D008433:Mathematics; D051379:Mice; D008807:Mice, Inbred BALB C; D008967:Molecular Biology; D013045:Species Specificity
D000906:Antibodies; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains