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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Date
1983-06
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Abstract
The binding affinities of some ligands towards the sialic acid-specific lectin
carcinoscorpin, from hemolymph of the horseshoe crab Carcinoscorpius 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-Dgalactitol
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.
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Keywords
Horseshoe crab lectin, sialic acid, fluorescence, ligand-binding
Citation
Mohan S, Dorai D Thambi, Srimal S, Bachhawat B K, Das M K. Fluorescence studies on the interaction of some ligands with carcinoscorpin, the sialic acid specific lectin, from the horseshoe crab, Carcinoscorpius rotundacauda. Journal of Biosciences. 1983 Jun; 5(2): 155-162.