Abstract
Iodinated cell surface components from human thymus lymphocytes labeled by the lactoperoxidase method, were solubilized by papain digestion and then 3 M KCl extraction of the residual cell pellet. Antiserum to human thymus bound three components from this material, mol. wt. ∼ 40 000, 20 000 and 12 000 daltons. This antiserum was absorbed with cultured human lymphoblasts (CHL) until it no longer bound CHL antigens or the HLA‐β2‐microglobulin complex. It continued to bind labeled antigens from thymus, peripheral blood lymphocytes and a “T” cell‐enriched fraction of tonsil lymphocytes. The absorbed antiserum bound a component from papain‐solubilized thymus antigens which had an estimated molecular weight of ∼ 40 000 daltons and which was not associated with β2‐microglobulin. This component seemed to be a human T cell‐specific antigen.