dc.contributor.author | Gowda, N.M. | |
dc.contributor.author | Goswami, U. | |
dc.contributor.author | Khan, M.I. | |
dc.date.accessioned | 2008-04-01T07:21:08Z | |
dc.date.available | 2008-04-01T07:21:08Z | |
dc.date.issued | 2008 | |
dc.identifier.citation | Fish & Shellfish Immunology, vol.24(4); 450-458p. | |
dc.identifier.other | no | |
dc.identifier.uri | http://drs.nio.org/drs/handle/2264/1046 | |
dc.description.abstract | A novel lectin was purified from the coelomic fluid of the sea cucumber Holothuria scabra (HSL), subjected to bacterial challenge. HSL is a monomeric glycoprotein of molecular mass 182 kDa. The lectin is highly thermostable as it retains full activity for 1 h at 80 degrees C. Further, the hemagglutination activity of HSL is unaffected by pH in the range 2-11. Unlike other lectins purified from marine invertebrates, the hemagglutination activity of HSL does not require any divalent metal ions. The affinity profile of HSL was studied by a combination of hemagglutination inhibition and fluorescence spectroscopy. HSL binds to desialylated glycoproteins, Me alpha Gal, T-antigen and T (alpha - ser)-antigen with a distinction between Beta 1-4 and Beta 1-3 linkages. Me alpha -T-antigen was a potent ligand having highest affinity (K sub (a) 8.32 x 10 sup (7) M sup(-1)). Monosaccharide binding is enthalphically driven while disaccharide binding involves both entropic and enthalpic contributions. | |
dc.language.iso | en | |
dc.publisher | Elsevier | |
dc.rights | Copyright [2008] Elsevier | |
dc.subject | Marine invertebrate | |
dc.subject | Holothuria scabra | |
dc.subject | Fluorescence spectroscopy | |
dc.subject | sea cucumber | |
dc.title | Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra) | |
dc.type | Journal Article | |