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Direct demonstration of murine thymus-dependent cell surface endogenous immunoglobin.
Author(s) -
A Szenberg,
John J. Marchalonis,
Noel L. Warner
Publication year - 1977
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.5.2113
Subject(s) - antibody , microbiology and biotechnology , antigen , antiserum , biology , immunoglobulin light chain , immunofluorescence , surface immunoglobulin , lymphoma , bone marrow , sepharose , b cell , chemistry , immunology , biochemistry , enzyme
Antisera raised in mammals to murine immunoglobulin (Ig) do not detect surface Ig on thymus-dependent (T) lymphoma cells as assessed by immunofluorescence analysis. In contrast, chicken antibodies, produced against the (Fab)2 fragment of normal mouse IgG and purified by binding to and elution from IgG-Sepharose 4B, give strong indirect fluorescence with murine T cells and cultured T lymphoma cells. The surface Ig caps, is shed, and reappears, indicating that it is of endogenous origin. Nonlymphoid tumor cells of various myeloid types do not bind this reagent, even though they bear avid Fc receptors. The capacity of chicken antibodies to bind to both bone-marrow-dependent and T cell lymphomas was abolished by adsorption with myeloma-derived kappa chains coupled to Sepharose. The kappa antigenic determinant recognized by the chicken antibodies may thus be different from that seen by mammalian antibodies, and the degree of exposure of Ig on the T lymphoma surface might also affect ease of detectability with these reagents. These data provide direct evidence that T lymphocytes and T lymphoma cells express and synthesize a surface Ig containing determinants that at least 'crossreact with bone-marrow-cell-derived kappa chains.

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