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Purification and properties of a fucoidan-binding protein from human placenta and its identification as
F Y Zeng1, U Wegenka, H J Gabius
1Institut für Pharmazeutische Chemie, Abteilung Glykobiochemie und Angewandte Tumorlektinologie, Marburg, Fed. Rep. Germany.
Abstract:
1. A fucoidan-binding protein from human placenta was purified by affinity chromatography on immobilized fucoidan. 2. Characterization of molecular and immunological properties and peptide mapping indicated that the fucoidan-binding protein is an immunoglobulin G. 3. Cleavage with papain and transblot analysis with labelled fucoidan ascertained binding properties of the F(ab) fragments. 4. The specificity for fucoidan was furthermore substantiated by hapten inhibition of haemagglutination as well as by solid-phase assays with biotinylated fucoidan as ligand. The results emphasized the importance of structural features instead of simple ionic interactions. 5. Chemical modification with group-specific reagents to lysine, arginine, tryptophan, tyrosine and histidine resulted in substantial inactivation, their impact being markedly reduced by the presence of fucoidan in the cases of lysine, arginine and tryptophan.