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Abstract.A chemoattractant lectin from the dorsal spines of the redfin velvetfish, Hypodytes rubripinnis , was isolated using a combination of affinity chromatography techniques. The glycoprotein, with a molecular mass of 110 kDa, is named Karatoxin. Karatoxin caused agglutination of rabbit erythrocytes. This agglutination was effectively inhibited by D -mannose. In addition, Karatoxin exhibited not only mitogenic activity in the presence of murine splenocytes, but also chemotactic activity in the presence of guinea-pig neutrophils and macrophages. Thus, Karatoxin appears to be a novel chemoattractant lectin. These results suggest that the redfin velvetfish Hypodytes rubripinnis may be a novel source of biologically active substances.

A novel lectin was purified from the dorsal spines of the devil stinger, Inimicus japonicus using a combination of affinity chromatography techniques. A single band was detected on a native PAGE gel with a relative molecular mass of 97 kDa. The N-terminal partial amino acid of the intact 75 kDa subunit of the 97 kDa lectin was found to be DHEDS. The agglutination of rabbit erythrocytes by the 97 kDa lectin was inhibited most effectively by methyl a-D-mannoside. The 97 kDa lectin stimulated mitogenesis in murine splenocytes. This is the first study to examine the dorsal lectin of I. japonicus and one of the very few studies on venom lectins from venomous scorpaeniform fish. These results suggest that the devil stinger, I. japonicus, may be a novel resource for biologically active substances.