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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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Detalles Bibliográficos
Autor principal: Banyard, M. R.
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 1984
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1977008/
https://www.ncbi.nlm.nih.gov/pubmed/6498078
Descripción
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.