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Biomedical subjects

Y Gorsky

Publications and source records attributed to Y Gorsky.

12 recordsLinked to original sources

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.

Antibodies, Monoclonal↗

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. Allogeneic but not autologous PHA blasts were also damaged by these effectors. The cytotoxic potential of MLC-activated lymphocytes from healthy donors was similar; allogeneic tumors and phytohemagglutinin (PHA) blasts but not autologous PHA blasts were lysed. The cytotoxicity of lymphocytes activated in ATS were specific for the stimulator because they acted only on the autologous tumor cells. Allogeneic tumors and autologous and allogeneic PHA blasts were not lysed. The pattern of cytotoxicity with regard to this target panel was maintained when the MLC or ATS cultures were further propagated with TCGF. Results obtained in cold target competition assays suggested (a) activated lymphocyte lyse the third party tumor targets because of alloantigen recognition; (b) in MLC several different sets of alloreactive cytotoxic lymphocytes are present simultaneously; and (c) the alloreactive cells are different than those that act on the autologous tumor cells. Thus, the lysis of allogeneic tumor cells by lymphocytes of the patient is not due to recognition of cross-reacting tumor-related antigens, and the autotumor cytotoxicity of the patients' MLC-activated lymphocytes if performed by specifically reacting cells.

Binding, Competitive↗

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. Pb antigens were detected by their capacity to inhibit the binding of the anti-Pb antibodies. Using a rabbit-Pb serum, sonicated, infected RBC (50% parasitemia) gave detectable inhibition up to 1 : 106 dilution.

Animals↗

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. With purified antibodies originating from the serum, 52% of the breast cancer sera and 16% of sera from patients with other malignancies were more inhibitory than were 95% of the sera of healthy women. In the tests with antibodies eluted from pleural fluid, 24% of the breast cancer sera and 25% of the sera from patients with other neoplastic diseases were more inhibitory than were 95% of the normal sera. We concluded that sera of patients with breast cancer may contain antibodies against antigens associated with breast cancer as well as additional antibodies against antigens that are also found in patients with other neoplastic diseases or in normal individuals. Individual breast cancer sera may inhibit binding of the labeled antibodies against breast cancer owing to their content of antibodies, antigen(s), or both.

Antibodies, Neoplasm↗

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. Globulin fractions of human sera were strongly inhibitory. Their capacity to inhibit was lost after treatment with rabbit anti-human IgG serum, indicating that at least part of the inhibition could be ascribed to antibodies. Some inhibitory activity was also found, however, in the "albumin" fractions of sera, suggesting that an antigen was also involved. It appears, therefore, that practically all human sera contain antibodies reacting with an antigen(s) which is present on human cells and is also circulating freely in serum and other body fluids. Sera of patients with Burkitt's lymphoma contained, on the average higher concentrations of these antibodies, as compared to sera of individuals not suffering from this disease. This antigen is thought to be associated with the cell membrane and has been identified in cells of widely differing origin.

Antibody Specificity↗

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. The specificity of the binding was confirmed by inhibition experiments. Data are presented demonstrating that at least some of the antibodies reacting in this radioimmunoassay are directed against antigens related to cell surface components.

Adsorption↗