Inhibition of Human Anti-Gd Cold Agglutinins by Sialyllactose

Abstract
Two examples of IgM χ-monolypic cold agglutinins occurring in patients with non-Hodgkin lymphomas, reacted with erythrocyte autoantigens, which were protease-resistant but were inactivated by neuraminidase. The cold agglutinins were inhibited by the trisaccharide sialyllactose [NcuNAc (α,2→3)Gal (β,1→+4)Glc], which is not related to oligosaccharides known to inhibit anti-I/-i cold agglutinins. Anti-Pr cold agglutinins are not inhibited by sialyllactose, although N-acetylneuramimc acid (NeuNAc) is an essential component not only of Gd but also of Pr determinants. Gd determinants are not bound lo erythrocyte membrane glycoproteins, but are apparently bound to membrane glycolipids (gangliosidcs).