Detection of circulating antibodies against c-myc protein in cancer patient sera.

We have partially purified an archaebacterial protein of 84 kD which shares common epitopes with the human c-myc protein as shown by its cross-reactivity with a commercialized anti-human c-myc antiserum. An antiserum raised against the 84 kD protein recognizes a 60 kD protein from HL-60 nuclei. This...

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Detalles Bibliográficos
Autores principales: Ben-Mahrez, K., Thierry, D., Sorokine, I., Danna-Muller, A., Kohiyama, M.
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 1988
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246462/
https://www.ncbi.nlm.nih.gov/pubmed/3044429
Descripción
Sumario:We have partially purified an archaebacterial protein of 84 kD which shares common epitopes with the human c-myc protein as shown by its cross-reactivity with a commercialized anti-human c-myc antiserum. An antiserum raised against the 84 kD protein recognizes a 60 kD protein from HL-60 nuclei. This protein is also recognized by the anti-human c-myc antiserum. Using this archaebacterial protein as antigen for Western blot analysis, we found that the human c-myc oncogene product could be immunogenic and that it is possible, in some spontaneously occurring human tumours, to detect antibodies against the c-myc gene product in the serum of cancer patients. IMAGES:

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