A lectin in the skin muscus of the dragonet Repomucenus richardsonii was purified to an electrophoretically pure state by affinity chromatography on Sepharose 4B and HPLC on Chemcosorb 300-7CM. The purified lectin was an acidic glycoprotein with an isoelectric point of 6.1. Its molecular weigh was determined to be 48000 by HPLC on TSK-gel G3000SW or 12000 by SDS electrophoresis, suggesting that it exists as a tetramer of the same subunit. The amino acid composition was characterized by the abundance of glycine, acidic amino acids and hydroxy amino acids and the absence of sulfur-containing amino acids. Inhibition tests revealed that the purified lectin has high affinity for D-galactose related sugars, especially lactose, and two glycoproteins(asialofetuin and mucin).
