Specific enrichment of antigen-binding receptors from sensitized murine lymphocytes.

Splenic T and B lymphocytes from sensitized mice were adsorbed to antigen-coated nylon discs and realesed from the discs by temperature shift as described by Kiefer, H., (Eur. J. Immunol. 1973. 3: 181 and 1975. 5:624). After cell release, lymphocyte-derived antigen-binding material could be recovered from the discs. A major fraction of the activity (70 -80%) binds to anti-immunoglobulin immunosorbents. A minor fraction does not detectably cross-react with gamma, mu, alpha and kappa immunoglobulin poly-peptide chains. When filtrated through Sephadex G-200, the bulk of activity of both fractions elutes in the region of 7 S serum antibody. However, as demonstrated for (4-hydroxy-3-nitro-phenyl)acetyl (NP)-binding material from C57BL/6 lymphocytes, the average affinity for antigen of the two fractions is drastically lower than that of humoral antibody, and the average affinity of the minor fraction is lower than that of the major fraction. The fraction of lymphocyte-derived antigen-binding material that does not adsorb to insolubilized anti-immunoglobulin serum was found to be proportional to the fraction of T lymphocytes in the input cell population and may therefore represent antigen-binding T lymphocyte surface receptors.