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The extract of the soft coral Lobophytum variatum agglutinated horse erythrocytes but not human ABO or rabbit erythrocytes in the presense of calcium ions. The activity was inhibited by mucin Type I from the bovine 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 chromatography on Mono-Q. Both lectins were glycoproteins composed of covalently bond ed subunits of 53 kDa. The sequence of the amino-terminal region of LVL-1 was determined as Ala-IleAsn-Gln-Ser-Ser-Gly-Asn-Leu-(X)-Asp-Arg-Leu-Gln-Glu-Arg-Phe-(X)-Leu-Asp-His-, where X is an unidentified residue.

Purification and Characterization of the Lectins of the soft Coral <i>Lobophytum variatum</i>