Fluorescence studies on the interaction of some ligands with carcinoscorpin, the sialic acid specific lectin, from the horseshoe crab, Carcinoscorpius rotundacauda.
J Biosci
;
1983 Jun; 5(2): 155-162
Article
Dans Anglais
| IMSEAR
| ID: sea-160224
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.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
langue:
Anglais
Texte intégral:
J Biosci
Année:
1983
Type:
Article
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