PURIFICATION AND PARTIAL CHARACTERIZATION OF THE LECTIN FROM THE MARINE RED ALGA ENANTIOCLADIA-DUPERREYI (AGARDH,C.) FALKENBERG

The marine red alga Enantiocladia duperreyi has been shown to contain a lectin which was isolated by a combination of ammonium sulphate prec iptation, ion-exchange chromatography on DEAF-Cellulose and affinity c hromatography on alpha-lactose-agarose. The lectin preferentially aggl utinated human blood group O erythrocytes and was inhibited by the sim ple sugars fucose, galactose and their derivatives and by the glycopro tein porcine stomach mucin. The molecular weight (MW) of E. duperreyi lectin, determined by gel filtration was 24 700, while SDS-PAGE exhibi ted one single protein band with MW of 16 072. The lectin was stable a t variations of temperature and the activation energy of the inactivat ion process was calculated to be 24.05 Kcal mol(-1).