Abstract
Purified molecules (70,000 mol wt) from a T-suppressor (Ts) clone bind to sheep erythrocyte glycophorin and specifically suppress the response to this antigen. Papain splits purified 70,000-mol wt Ts molecules into two peptides: mol wt 45,000 and 24,000. The 45,000-mol wt peptide nonspecifically suppresses antibody response to several antigens and lacks antigen-binding activity. The 24,000-mol wt peptide does not suppress but retains antigen-binding activity. The results indicate that papain splits the Ts molecule into a "constant" region responsible for function and a "variable" region responsible for antigen-binding. Since binding of the 70,000-mol wt molecule to antigen also results in release of the 45,000 mol wt subunit, this cleavage may allow Ts molecules specific for one determinant to suppress immunity to complex foreign proteins.