Mixtures of antibodies were sufficient for serologic studies since extremely specific antisera could detect micrograms of an idiotype present in milligrams of an immunoglobulin mixture. The ground rules for the biochemical analysis of antibodies, however, are completely different. These studies require large amounts of antibodies that are not only directed against a single specificity, but that represent a single protein moiety.
KeywordsLight Chain Heavy Chain Versus Region Hypervariable Region Complete Amino Acid Sequence
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References and Bibliography
- Capra, J. D., 1971, A hypervariable region in human immunoglobulin heavy chains, Nature (London) 230: 62.Google Scholar
- Capra, J. D., and Kehoe, J. M., 1975, Hypervariable regions, idiotypy and the antibody combining site, Adv. Immunol. 30: 1975.Google Scholar
- Fougereau, M., Bourgois, A., De Preval, C., Rocca-Serra, J., and Schiff, C., 1976, Ann. Immunol. 127c: 607.Google Scholar
- Franek, F., 1969, The character of variable sequences in immunoglobulin and its evolutionary origin, in: Symposium on Developmental Aspects of Antibody Formation and Structure (J. Sterzl and I. Riha, eds. ), Prague, p. 311.Google Scholar
- Kunkel, H. G., 1965, Myeloma proteins and antibodies, Harvey Lect. 59: 219.Google Scholar
- McCumber, L. J., Wasserman, R., and Capra, J. D., 1980, Primary structural conservation in the evolution of IgM, Biologic Basis of Immunodeficiency (E. W. Gelfand and H.-M. Dosch, eds.), Raven Press, New York, pp. 169–176.Google Scholar