Phenotypic similarity between T-cell antigen binding molecules.

T-cell antigen binding molecules (TABM) specific for trinitrophenol (TNP), oxazalone, azobenzenearsonate or sheep erythrocytes were purified by affinity to antigen, adsorption to monoclonal antibodies to antigen binding molecules or were synthesized by translation of immunopurified mRNA for TABM in vitro. These molecules and a T-cell line, BW5147, membrane protein bound by rabbit antibodies to TABM were radiolabeled by 125I, digested with Staphylococcus V8 protease, and peptides of the proteolytic digest were resolved by 2D-gel peptide mapping. Comparison of the peptide maps of these proteins and amino acid analysis of T-cell antigen binding molecules specific for TNP or sheep erythrocytes indicate similarities and distinctions suggesting variable and constant domains in these molecules.