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

dc.contributor.authorMohan, S
dc.contributor.authorDorai, D Thambi
dc.contributor.authorSrimal, S
dc.contributor.authorBachhawat, B K
dc.contributor.authorDas, M K
dc.date.accessioned2015-07-21T07:22:14Z
dc.date.available2015-07-21T07:22:14Z
dc.date.issued1983-06
dc.description.abstractThe 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.en_US
dc.identifier.citationMohan 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.en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/160224
dc.language.isoenen_US
dc.source.urihttps://www.ias.ac.in/jarch/jbiosci/5/155-162.pdfen_US
dc.subjectHorseshoe crab lectinen_US
dc.subjectsialic aciden_US
dc.subjectfluorescenceen_US
dc.subjectligand-bindingen_US
dc.titleFluorescence studies on the interaction of some ligands with carcinoscorpin, the sialic acid specific lectin, from the horseshoe crab, Carcinoscorpius rotundacauda.en_US
dc.typeArticleen_US
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