Abstract

Abstract Glycopeptides of human teratoma cells were studied. Two glycopeptide fractions (Fractions A and C) obtained from pronase digests of the human teratoma stem cells of line PA 1 were analyzed. Fraction A glycopeptides were of large size (M r > 7400). They could be labeled by supplying the cells with 3 H-mannose, 3 H-fucose, 3 H-galactose, 3 H-glucosamine, 3 H-glucose and 35 S-sulfate. Acid hydrolysates of Fraction A contained at least mannose and fucose. A part of Fraction A glycopeptides could be obtained by affinity chromatography on Concanavalin A-Sepharose in a form virtually free of 35 S-sulfate; at least these glycopeptides may represent molecules different from glucosaminoglycans. A pulse-chase experiment with 3 H-mannose suggested that Fraction A glycopeptides may derive their mannose units from Fraction C glycopeptides, which were of the same molecular size (850–2200 daltons) as the common oligomannosyl type asparagine glycopeptides, and which had also labeling characteristics typical to the oligomannosyl glycopeptides. Fraction A glycopeptides were probably present on the surface of the PA 1 cells, as they could be released by mild trypsin treatment of the living cells.

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