Abstract
Carcinoembryonic antigen (CEA). treated with neuraminidase, reduced with dithiothreitol and carboxymethylated with 14C-iodoacetate, was digested with proteolytic enzymes. Tryptic and chymotryptic peptides were mapped on paper. Autoradiography and specific staining reactions, as well as detection of glycopeptides from samples treated with neuraminidase, galactose oxidase and tritiated sodium borohydride, all revealed considerably fewer peptides than anticipated. This was mainly due to limited separation of glycopeptides. CEA was also citraconylated and digested with trypsin and the peptide mixture fractionated by gel filtration. After deblocking of citraconyl groups, the antigenic activity of the peptides was investigated utilizing an enzyme linked immunoadsorbent assay with monkey anti CEA antibodies either against sequential or against conformation-dependent determinants. Large CEA-fragments were active in both assays.
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