PURIFICATION AND CHARACTERIZATION OF THE LECTINS OF THE SOFT CORAL LOBOPHYTUM-VARIATUM

The extract of the soft coral Lobophytum variatum agglutinated horse e rythrocytes but not human ABO or rabbit erythrocytes in the presense o f calcium ions. The activity was inhibited by mucin Type I from the bo vine submaxillary gland and also by simple sugars such as D-ribose and N-acetylneuraminic acid. Two lectins, LVL-1 and LVL-2, were purified by gel filtration on Sepharose 4B succeeded by ion-exchange chromatogr aphy on Mono-Q. Both lectins were glycoproteins composed of covalently bonded subunits of 53 kDa. The sequence of the amino-terminal region of LVL-1 was determined as -(X)-Asp-Arg-Leu-Gln-Glu-Arg-Phe-(X)-Leu-As p-His-, where X is an unidentified residue.