A mean of 98% of lymphocytes in T-enriched preparations of human peripheral blood bound purified chicken anti-human F(ab')2 antibodies to their surface membranes as demonstrated by the mixed antiglobulin rosetting reaction (MARR). By reverse passive hemagglutination these antibodies reacted strongly with kappa light chains and with Fd gamma but gel diffusion analyses, absorption on affinity columns and inhibition experiments established that the anti-F(ab')2 antibodies were not isotype specific and that there was extensive serological cross-reactivity between Fd gamma and kappa and probably also between Fd gamma and mu chains. The antigenic determinants recognized on the T-cells surfaces were not shared by Ig fractions from several other mammalian species. Trypsin treatment of lymphocytes removed all determinants recognized by anti-F(ab')2 antibodies from approximately two-thirds of the cells but these cells almost completely re-expressed these determinants during in vitro culture; this indicates that the T-cell determinants seen by anti-F(ab')2 antibodies are T cell products and do not represent adsorbed Ig. Complete inhibition of the MARR by human F(ab')2 excludes false positive rosette formation due to contaminating specificities directed against non-Ig molecules on T cells. Together the various findings are consistent with the conclusion that most human peripheral blood T cells express Ig or Ig-related molecules in their surface membranes. A mean of 13% of lymphocytes in T-enriched preparations were reactive with mu-chain specific chicken antibodies; it may be that a minority of T cells express mu chain determinants in addition to those recognized by anti-F(ab')2 antibodies.