Purification and Characterisation of an Anti-Sialic Acid Agglutinin from the Red Alga Solieria chordalis (C. Ag.) J. Ag.

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Abstract
Extracts from the marine red alga S. chordalis (C. Ag.) J. Ag. agglutinate native human erythrocytes in the presence of bovine serum albumin. Progressive removal of erythrocyte surface sialic acid with neuraminidase gives corresponding reduction in agglutinin-binding. This novel agglutinin is considered to show the rare specificity anti-sialic acid. Hemagglutination inhibition revealed that the hemagglutinin was inhibited by the sialoglycoproteins fetuin, bovine submaxillary mucin and procine mucin suggesting that the agglutinin binds preferentially to a receptor incorporated in the disaccharide residue, O (2 .fwdarw. 6) glucoside of sialic acid and 2-acetamido-2-deoxy-D-galactopyranose. Removal of sialic acid by neuraminidase reduced the inhibitory capacity of these substances. Batch affinity-chromatographic procedures and electrophoretic studies showed that the activity of the extract was due to the presence of an agglutinin with a MW of .apprx. 35,000 daltons. This may be a subunit of larger molecular forms.