Partial structural analysis of concanavalin A binding glycopeptides of large size from human teratocarcinoma-derived cells: cleavage by hydrazinolysis and alkaline borohydride

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Abstract
Pronase digests of cultured teratocarcinoma-derived cells (PA 1) of human origin contain large-sized glycopeptides (relative mass (relative MW) > 7400), of which 15-23% are retained by columns of concanavalin A (Con A)-Sepharose and can be eluted with 10 mM methyl .alpha.-D-mannopyranoside. This fraction (A-Con A II) contains a family of glycopeptides that are degradable with anhydrous hydrazine as well as with 0.05 M NaOH-1 M NaBH4. The cleavage products representing individual oligosaccharide chains, presumably as oligosaccharides and glycopeptides, consisted mostly of medium- (relative MW 1400-6000) and small-sized (relative MW < 1400) molecules. This implies that glycopeptides bearing several oligosaccharide chains were present in A-Con A II. Most of the individual oligosaccharide chains were not bound to Con A-Sepharose, but some were retained by the lectin column in the same way as the original glycopeptides. Some of the oligosaccharides were degraded partially with endo-.beta.-galactosidase from Escherichia freundii suggesting the presence of Gal.beta.GlcNAc.beta. repeats. A-Con A II may be different from the embryonic glycopeptides of mouse teratocarcinoma cells that are reportedly not cleaved by mild alkaline borohydride treatment. A-Con A II is reminiscent of the T-1 glycopeptide of glycophorin.

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