• Fluorescence studies on the interaction of some ligands with carcinoscorpin, the sialic acid specific lectin, from the horseshoe crab,Carcinoscorpius rotundacauda

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    • Keywords


      Horseshoe crab lectin; sialic acid; fluorescence; ligand-binding

    • Abstract


      The binding affinities of some ligands towards the sialic acid-specific lectin carcinoscorpin, from hemolymph of the horseshoe crabCarcinoscorpius rotundacauda have been determined by protein fluorescence quenching in presence of ligands. Among the ligands studied, the disaccharide O-(N-acetylneuraminyl)-(2→6)-2-acetamido-2-deoxy-D-galactitol has the highest Ka(l.15 × 106 M-1) for carcinoscorpin. Studies on the effect of pH on Ka values of disaccharide suggests the possible involvement of amino acid residues having pKa values around 6.0 and 9.0 in the binding activity of carcinoscorpin. There were distinct changes in the accessibility of the fluorescent tryptophan residues of carcinoscorpin by ligand-binding as checked through potassium iodide quenching.

    • Author Affiliations


      S Mohan1 D Thambi Dorai1 S Srimal1 B K Bachhawat1 M K Das1

      1. Enzyme Engineering Laboratory, Indian Institute of Chemical Biology, Jadavpur, Calcutta - 700 032
    • Dates

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