Serological characterization of humoral lectin from Heterometrus granulomanus scorpion hemolymph.
A lectin in the hemolymph of Indian scorpion Heterometrus granulomanus was detected by agglutination of human and animal erythrocytes. The agglutinating activity was enhanced in presence of Ca2+ ion. The lectin shows specificity for sialic acid like many other sialic acid-specific lectins such as "Limulin", as the agglutination of erythrocytes was completely abolished by treatment with Vibrio cholerae neuraminidase. However, neuraminidase-treated rat and mouse erythrocytes exhibited high titers. This result was substantiated by crossed-absorption test which suggests the adjunct specificity of the Heterometrus lectin for these cells. Hemagglutination-inhibition results of the lectin indicate that sialic acid including its derivatives and sialoglycoconjugates are the inhibitors among which glycophorin was most potent.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D006385:Hemagglutination Inhibition Tests; D006386:Hemagglutination Tests; D006458:Hemolymph / Q000032:analysis*; D037102:Lectins / Q000302:isolation & purification*; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000494:pharmacology; D012605:Scorpions / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism
C049849:Heterometrus granulomanus lectin; D037102:Lectins; D012794:Sialic Acids; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid; D002118:Calcium