01956nas a2200229   4500008004100000022001400041245015200055210006900207260008900276300001200365490000700377520103600384653003001420653002201450653001101472653002401483653002901507100002301536700001801559700002601577856012301603       2008                        eng d  a1050-464800aPurification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)0 aPurification and characterization of a Tantigen specific lectin   a24-28 OVAL RD, LONDON NW1 7DX, ENGLANDbACADEMIC PRESS LTD ELSEVIER SCIENCE LTDcAPR  a450-4580 v243 a<p>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-a 8.32 x 10(7) M-1). Monosaccharide binding is enthalphically driven while disaccharide binding involves both entropic and enthalpic contributions. (c) 2008 Elsevier Ltd. All rights reserved.</p>10aFluorescence spectroscopy10aHolothuria scabra10aLectin10amarine invertebrate10aThermodynamic properties1 aGowda, Nagaraj, M.1 aGoswami, Usha1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/purification-and-characterization-t-antigen-specific-lectin-coelomic-fluid-marine-0