Abstract
1. 1. We have purified a 19 kDa lectin from the freshwater prawn Macrobrachium rosenbergii by single-step affinity chromatography on a rat stroma column. 2. 2. The lectin is a glycoprotein composed of two monomeric subunits of 9.6 kDa bound by a disulfide bridge; 7% of its contents are carbohydrates. 3. 3. It has an S 20, w value of 1.4, a pI of 5.4–6.1, and is rich in glycine, serine, glutamic and aspartic acid residues. 4. 4. It requires divalent cations to function. 5. 5. It recognizes sialic acid. 6. 6. The hemagglutinating and hapten inhibition assays strongly suggest that it is 9- O-acetylsialic acid residue-specific.
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