Monoclonal antibodies embedded in their hybridoma cells: an immunodiagnostic concept.

Aldehyde fixation of hybridoma cells during active production of monoclonal antibodies (MAbs) resulted in the formation of an insoluble phase because a large number of immunologically active antibody molecules were immobilized on the fixed hybridoma cells. Such MAb preparations specific to large protein molecules and small haptens were used for the development of a homogeneous immunoassay concept.

Lysis of tumor biopsy cells by autologous T lymphocytes activated in mixed cultures and propagated with T cell growth factor.

Blood lymphocytes from tumor patients were cocultivated with allogeneic lymphocytes (MLC) or autologous tumor cells (ATS), and their cytotoxicity was characterized. The main objective of the study was the lysis of autologous tumor biopsy cells by such effectors. Lymphocytes of patients activated in MLC lysed allogeneic third-party cells and in some cases also lysed autologous tumor cells.

A solid-phase antibody binding-inhibition test, for the assay of Plasmodium berghei antigen and antibodies, using radioiodinated protein A.

Sonicated red blood cells (RBC) of rats infected with Plasmodium berghei (Pb) were used to coat plastic tubes with Pb antigens. The antigen-coated tubes were employed to detect Pb antigens and antibodies, with high efficiency. Anti-Pb antibodies were estimated by treating the tubes with rabbit or rat anti-Pb sera and assaying the bound Ig with radiolabeled Staphylococcus PrA.

Isolation from patients with breast cancer of antibodies specific for antigens associated with breast cancer and other malignant diseases.

Antibodies were specifically purified, with the use of pleural fluid antigens entrapped in a polyacrylamide gel as immunoadsorbent, from a pool of sera from patients with breast cancer and from the pleural effusion of an individual patient. The purified antibodies were radioiodinated and tested for capacity to bind to the pleural fluid adsorbent. Binding of the radiolabeled antibodies was inhibited by many of the sera from women with breast cancer to a much greater extent than by sera of healthy women.

Coexistence in human sera of a cell (membrane?) ANTIGEN AND Of autoantibodies directed against it.

Antibodies purified from sera of patients with Burkitt's lymphoma by absorption onto and elution from cultured lymphoblastoid cells, were labeled with 125I and repurified by repeating the absorption-elution procedure. The doubly purified antibodies could bound with a high degree of efficiency to immunoadsorbents prepared by entrapping in polyacrylamide gel normal human serum or exudate fluids from patients with ovarian or breast cancer. Binding was specific, as it could be inhibited by high dilutions of human sera but not by animal sera.

A radioactive antibody binding-inhibition assay, for the detection of cell-membrane related antigens in body fluids.

Antisera raised in rabbits against glutaraldehyde-fixed human breast cancer cells contain antibodies to human cell membrane components, as determined by immunofluorescence. Adsorption of such antisera onto polymerized human serum, followed by acid elution, yields purified antibodies reacting with human cell surface antigens, indicating that membrane related antigens are present in the serum. The purified antibodies were radioiodinated and shown to bind to an immunoadsorbent prepared by entrapping in a polyacrylamide gel pleural exudate of breast cancer patients.