Immunochemical studies of the intramolecular heterogeneity of the carcinoembryonic antigen (CEA) of the human digestive system

Joshua Michael Gold, C. Banjo, S. O. Freedman, P. Gold

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Previous studies have shown that in addition to the tumor specific site on the carcinoembryonic antigen (CEA), this molecule also contains a blood group A like grouping. To study the A like site on the CEA molecule, a radioimmunoassay was devised in which anti A bodies were coupled to either Sepharose or Sephadex beads. The following observations were made. The monosaccharide, N acetyl D galactosamine was capable of inhibiting the interaction between 125I CEA and a preparation of anti A antibodies. A glycopeptide (GP 1), containing the tumor specific antigenic site of the CEA, which was obtained by the enzymatic degradation of the CEA molecule was capable of binding to anti A antibodies. The ratio, by weight, of GP 1 to N acetyl D galactosamine required to achieve equivalent binding was 10-3 to 10-4 to 1. GP 1 has a molecular weight of about 4000 daltons, and although it contains N acetyl D glucosamine, D mannose, D galactose, and L fucose, the glycopeptide is apparently devoid of N acetyl D galactosamine.

Original languageEnglish (US)
Pages (from-to)1872-1879
Number of pages8
JournalJournal of Immunology
Volume111
Issue number6
StatePublished - Dec 1 1973

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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