TY - JOUR
T1 - The mouse T cell receptor
T2 - Structural heterogeneity of molecules of normal T cells defined by Xenoantiserum
AU - McIntyre, Bradley W.
AU - Allison, James P.
N1 - Funding Information:
We wish to thank Joanne Lund and David Walker for technical assistance, and Judy Ing for help with preparation of the art work. We also thank Dr. Mike Gallatin and Dr. John Carlson for helpful discussions and critical reading of the manuscript. This work was supported by grant CA 26321 from the Nattonal Institutes of Health. B. W. McIntyre is the recipient of the J. S. Abercrombie Foundation predoctoral fellowship.
PY - 1983/10
Y1 - 1983/10
N2 - 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.
AB - 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.
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U2 - 10.1016/0092-8674(83)90530-5
DO - 10.1016/0092-8674(83)90530-5
M3 - Article
C2 - 6194888
AN - SCOPUS:0020593643
SN - 0092-8674
VL - 34
SP - 739
EP - 746
JO - Cell
JF - Cell
IS - 3
ER -