The mouse T cell receptor: structural heterogeneity of molecules of normal T cells defined by xenoantiserum

• Published in: Cell Vol. 34; no. 3; p. 739
• Main Authors: McIntyre, B W, Allison, J P
• Format: Journal Article
• Language: English
• Published: United States 01-01-1983
• Subjects: Amino Acid Sequence; Animals; Antibodies, Monoclonal - immunology; B-Lymphocytes - immunology; Disulfides - immunology; Epitopes - analysis; Immune Sera - immunology; Male; Mice; Mice, Inbred C57BL; Rabbits; Receptors, Antigen, T-Cell - immunology; T-Lymphocytes - immunology; Trypsin - metabolism
• ISSN: 0092-8674
• DOI: 10.1016/0092-8674(83)90530-5

We have previously demonstrated that T lymphomas may express clonally specific epitopes that are carried by a T-cell-restricted, disulfide-bonded heterodimeric glycoprotein. We have used a monoclonal antibody, 124-40, to isolate the lymphoma-specific antigen and raise a xenoantiserum to the molecule. This antiserum immunoprecipitates a family of disulfide-bonded dimers from normal thymocytes and T cells, but is unreactive with B cells. Peptide maps prepared after limited proteolytic digestion indicate that the molecules from the different cell populations have homologous primary structures. Comparison of two-dimensional tryptic peptide maps indicate that, in addition to several common peptides, the molecules exhibit considerable structural heterogeneity. Taken together, these data indicate that the T-cell-specific heteroduplex has regions of constant and variable structure consistent with the properties expected for the T cell antigen receptor.