Purification and partial characterization of a haemagglutinin from Ulva fasciata

Abstract

A novel haemagglutinin has been detected from Ulva fasciata, a green marine alga. By a combination of ammonium sulphate precipitation and ion-exchange chromatography on DEAE-Cellulose column, we have purified a haemagglutinin and designated it as UFH (Ulva fasciata haemagglutinin). It agglutinated native human blood cells without any blood group specificity. Under reducing and non-reducing conditions, this agglutinin was isolated as a monomeric protein with a relatively low molecular weight of 14.5 kDa. The activity of UFH was thermo-stable, expressing functionality at 40-100 degrees C and not inhibited by the inclusion of divalent cations nor pH changes, being stable at pH values 6.0-10.5. None of the tested monosaccharides and glycoproteins inhibited agglutination by UFH. The observations indicate that the properties of UFH are consistent with its recognition as a haemagglutinin isolated from marine algae. The pH stability, high-level activity and thermo-stability thus support it's candidature for future applicability in lectin research, glycobiology and bio-medical applications.