Show simple item record

dc.contributor.authorGowda, N.M.
dc.contributor.authorGoswami, U.
dc.contributor.authorKhan, M.I.
dc.date.accessioned2008-04-01T07:21:08Z
dc.date.available2008-04-01T07:21:08Z
dc.date.issued2008
dc.identifier.citationFish & Shellfish Immunology, vol.24(4); 450-458p.
dc.identifier.otherno
dc.identifier.urihttp://drs.nio.org/drs/handle/2264/1046
dc.description.abstractA 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.isoen
dc.publisherElsevier
dc.rightsCopyright [2008] Elsevier
dc.subjectMarine invertebrate
dc.subjectHolothuria scabra
dc.subjectFluorescence spectroscopy
dc.subjectsea cucumber
dc.titlePurification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)
dc.typeJournal Article


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record