Phylogenetic Aspects of Immunoglobulin Variable Region Diversity
There is now widespread agreement that the antigen-binding function of immunoglobulin molecules is mediated by the variable regions of their heavy and light polypeptide chains. Studies from a number of laboratories have shown that many general features of antibodies, such as the capacity to interact with a given antigen (e.g., dinitrophenyl), susceptibility to proteolytic cleavage, and mediation of biological properties (e.g., complement fixation), are shared across a wide phylogenetic spectrum of animal species. From a broad biological standpoint, an important question arises. To what extent do these various animal species produce similar immunoglobulin proteins to fulfill the functional requirements of the humoral response system? One approach to answering this question is to study the molecular products of the humoral response in a wide variety of species, especially including amino acid sequence analyses. Unfortunately, such studies have been impeded by the difficulty of obtaining sufficient quantities of pure material from the different species, in large part because of the restriction of the availability, until recently, of homogeneous myeloma proteins to man and the mouse. However, the discovery and sequence analysis of myeloma proteins from dogs and cats (Kehoe and Capra, 1972), progress in amino acid sequence studies of murine myeloma proteins (Bourgois and Fougereau, 1970; Hood and Talmage, 1970; Rudikoff et al., 1973), the recent discovery of myeloma proteins in rats (Bazin et al., 1972; Querinjean et al., 1974), and the remarkable complete sequence analyses performed by Cebra et al. (1971) on pools of immunoglobulins from inbred guinea pigs has considerably widened the scope of the available sequence data on the characteristics of antibody proteins from various species.
KeywordsHeavy Chain Myeloma Protein Heavy Chain Variable Region Human Myeloma Protein
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- Bazin, H., Deckers, C., Beckers, A., and Heremans, J. F., 1972, Int. J. Cancer 10:568. Bourgois, A., and Fougereau, M., 1970, FEBS Letters 8: 265.Google Scholar
- Capra, J. D., Chuang, C., Kaplan, R. D., and Kehoe, J. M., 1973a, IgA Symposium, Birmingham, Alabama.Google Scholar
- Cebra, J. J., Ray, A., Benjamin, D., and Birshstein, B., 1971, in Amos, B. (ed.) Progress in Immunology, Academic Press, New York, pp. 269–284.Google Scholar
- Kehoe, J. M., Bourgois, A., Capra, J. D., and Fougereau, M., 1973, Biochemistry,in press. Kohler, H., Shimizu, A., Paul, C., Moore, V., and Putnam, F. W., 1970, Nature 227:1318.Google Scholar
- Kubo, R. T., Rosenblum, I. Y., and Benedict, A. A., 1971, J. Immunol. 107: 1781.Google Scholar
- Milstein, C., 1967,Nature (Loud.) 216:330.Google Scholar
- Pink, J. R. L., Buttery, S. H., De Vries, G. M., and Milstein, C., 1970, Biochem. J. 177: 33.Google Scholar
- Potter, M., 1972,Physiol. Rev. 52:631.Google Scholar
- Querinjean, P. J., Bazin, H., Beckers, A., Kehoe, J. M., Schulman, J., and Capra, J. D., 1974, Fed. Proc. (abs.) 33:809.Google Scholar
- Wasserman, R. L., Kehoe, J. M., and Capra, J. D., 1974, Fed. Proc. (abs.) 33:809.Google Scholar