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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-...
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
1984
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1977008/ https://www.ncbi.nlm.nih.gov/pubmed/6498078 |
Sumario: | 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. |
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