A comparison of the expression of the DIDS-binding proteins from normal and tumorigenic human cells.
A monoclonal antibody was prepared against DIDS, an inhibitor of anion transport, and used to compare the occurrence and distribution of DIDS-binding sites of tumorigenic and non-tumorigenic human somatic-cell hybrids. The monoclonal antibody (E8) was produced by the fusion of the mouse myeloma (NS-1) with mouse spleen cells and is of the IgG1 subclass. The apparent half-saturation of DIDS for HEp-2 cells is 16 microM and the reaction is rapid. The number of binding sites on tumorigenic and non-tumorigenic hybrid cells was the same. The DIDS-binding protein occurs homogeneously on all cells, a characteristic which distinguishes it from the possible tumour antigen recognised by the M/27 monoclonal antibody.
D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid / Q000031:analogs & derivatives / Q000276:immunology / Q000378:metabolism*; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D001665:Binding Sites; D002352:Carrier Proteins / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D009369:Neoplasms / Q000378:metabolism*; D013267:Stilbenes / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D002352:Carrier Proteins; D013267:Stilbenes; D012856:4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid