Abstract
A lectin was isolated from the hemolymph of Asian horseshoe crab Tachypleus tridentatus by using glycophorin HA affinity chromatography and Sephacryl S-300 gel filtration. The lectin's molecular weight was approx. 533 kDa; being a simple protein comprised of two non-identical subunits with molecular weights fo 30 and 32 kDa. The hemagglutinating activity of the lectin against equine erythrocytes was strongly inhibited by several sialoglycoproteins and weakly inhibited by sialic acid, although not inhibited by neutral sugars, hexosamines, N-acetylhexosamines, glucronic acid, or several asialoglycoproteins. In addition, glycophorin HA was more effective than glycophorin HA digested with trypsin in inhibiting hemagglutination of the lectin. These result suggest that the purified lectin specifically reacts with sialic acids containing glycoprotein.
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