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Characterization of T-cell surface proteins bound by heterologous antisera to antigen-specific T-cell products.
Author(s) -
Robert E. Cone,
Robert W. Rosenstein,
James H. Murray,
G M Iverson,
W Ptak,
Richard K. Gershon
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.10.6411
Subject(s) - antigen , antiserum , microbiology and biotechnology , heterologous , hapten , biology , t cell , t cell receptor , cell , immunofluorescence , antigen presenting cell , chemistry , antibody , biochemistry , immunology , immune system , gene
Heterologous antisera specific for murine T-cell antigen-recognition molecules were prepared by immunization of rabbits with dinitrophenyl-specific murine T-cell suppressor factors that had been purified by hapten-affinity chromatography. The antisera (i) bind to antigen-specific T-cell products that differ in their antigen-recognizing specificity; (ii) absorb the specific suppressor activity in preparations containing suppressor factors; (iii) stain all Lyt2+ T cells brightly in indirect immunofluorescence examination, stain some Lyt1+ cells (with low intensity), and do not stain B cells; (iv) precipitate cell membrane proteins from T cells that bear striking structural resemblance to the antigen-specific molecules used for immunization. These results suggest that, like B cells, there is a commonality between antigen-specific effector molecules released by T cells and their membrane-associated receptors.

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