The present study deals with the biochemical properties of high-molecular-weight glycopeptides isolated from the surface of human teratocarcinoma cells. This cell surface material released by mild trypsin digestion from galactose-labeled human teratocarcinoma cells, Tera I and PA1, was digested extensively with pronase. Most of the resulting glycopeptides were large and were excluded from a Sephadex G-50 column. The properties of these large cell surface glycopeptides isolated from Tera I cells have been examined in detail. It is clear from these experiments that they are neither acidic mucopolysaccharides nor mucin-type glycopeptides with short oligosaccharide chains. Although the glycopeptides are hardly hydrolyzed by β-galactosidase even after prior digestion with neuraminidase, around 30% of the glycopeptides are depolymerized by treatment with endo-β-galactosidase from Escherichia freundii. The large cell surface glycopeptides from Tera I cells therefore appear to be very similar to the large glycopeptides seen on mouse embryonal carcinoma cells, which have core structures composed of galactose and N-acetylglucosamine. Like the mouse cell glycopeptides, a fraction of the large glycopeptides from these human cells bind to agarose-conjugated fucose-binding proteins and peanut agglutinin.


This work was aided by grants from the Ministry of Education, Science and Culture, Japan, Ministry of Health and Welfare, Japan, Japan Immuno-Research Laboratories, the Centre National de la Recherche Scientific, the Délégation Générale de le Recherche Scientifique et Technique, the Institut National de la Santé et de la Recherche Médicale, and the Andre Meyer Foundation.

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