Antigen-specific t lymphocyte clones. II. Purifcation and biological characterization of an antigen-specific suppressive protein synthesized by cloned T cells

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Abstract
We have generated an antigen-specific T suppressor clone that synthesizes 70,000-mol wt peptides that have antigen-specific-binding activity. Although these data also indicated that antigen-binding peptides completely inhibited the in vitro primary response to a complex antigen, suppression might reflect the combined biologic activities of many different 70-mol wt polypeptides or polypeptides associated with the 70,000-mol wt material by noncovalent interactions. The protein responsible for antigen-specific suppression was therefore purified to virtual homogeneity after sequential separation of internally labeled supernate peptides on Sephacryl S-200 and DEAE-cellulose columns followed by isoeleetrofocusing. The resulting protein is greater than 95 percent homogeneous according to sodium dodeeyl sulfate-polyacrylamide electrophoresis and represents two peptides having two very close but distinguishable isoelectric point values of approximately 5.0.

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