Specific antigen binding by proteins secreted by an antigen-specific T cell hybrid.
Antigen-specific molecules secreted by a murine T cell hybrid specific for azobenzene arsonate (ABA) were purified from ascites fluid by ion exchange chromatography and affinity for antigen. The antigen-specific proteins were purified 250 fold and were resolved predominantly as Mr 110,000 polypeptides by reduction and SDS-polyacrylamide gel electrophoresis. The ability of these molecules to bind antigen was analyzed by an ELISA using antigen-coated microtiter trays. Binding of the T cell proteins to antigen was detected with antisera specific for the proteins. Antigen binding to ABA-ovalbumin but not ovalbumin was optimal at 37 degrees C and protein derived from another T cell hybrid did not bind ABA-ovalbumin. Solid phase antigen binding was inhibited specifically by soluble ABA-ovalbumin, indicating that these T cell-derived proteins bind nominal antigen in the solid or liquid phase. It is suggested that these proteins represent a soluble, antigen specific manifestation of some T cell function.
Cone
R E
RE
Department of Pathology, University of Connecticut Health Center, Farmington 06030.
Weischedel
A K
AK
Urbanski
M
M
Kristie
J
J
D000818:Animals; D000941:Antigens / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D051379:Mice; D010047:Ovalbumin / Q000276:immunology; D011506:Proteins / Q000276:immunology / Q000302:isolation & purification*; D011817:Rabbits; D013601:T-Lymphocytes / Q000276:immunology*; D010132:p-Azobenzenearsonate / Q000276:immunology
D000941:Antigens; D011506:Proteins; D010132:p-Azobenzenearsonate; D010047:Ovalbumin