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Cytotoxicity with antibody‐glucose oxidase conjugates specific for a human colonic cancer and carcinoembryonic antigen
Author(s) -
Shearer William T.,
Turnbaugh Thomas R.,
Coleman William E.,
Aach Richard D.,
Philpott Gordon W.,
Parker Charles W.
Publication year - 1974
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910140414
Subject(s) - cytotoxicity , carcinoembryonic antigen , antibody , lactoperoxidase , chemistry , microbiology and biotechnology , antibody dependent cell mediated cytotoxicity , conjugate , biochemistry , glucose oxidase , antiserum , antigen , enzyme , biology , in vitro , peroxidase , immunology , cancer , mathematical analysis , mathematics , genetics
Abstract Rabbit or goat antibodies to a human colonic cancer cell line (HT‐29) and to carcinoembryonic antigen (CEA) were studied with respect to their ability to cause complement‐mediated and enzyme‐mediated cytotoxicity. IgG fractions of normal sera and antisera to CEA and HT‐29 were prepared and conjugated to glucose oxidase, an enzyme which permits specific iodination of cell membranes in the presence of glucose, iodide, and lactoperoxidase. Cytotoxicity was evaluated with several established tumor‐cell lines in vitro by measuring the uptake of 125 I‐iododeoxyuridine after 24 h in tissue culture. Specific iodination and cytotoxicity were observed with both enzyme‐antibody conjugates, but the enzyme‐antibody conjugate specific for CEA was much less effective than that for HT‐29. Complement‐mediated cytotoxicity was obtained with both antibodies, but with anti‐CEA antibody effects were obtained only at high antibody concentrations. The attachment of enzyme to antibody produced manifold enhancement of the inherent cytotoxicity of the antibody.