@article { ISI:000254697200009,
	title = {Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)},
	journal = {Fish \& Shellfish Immunology},
	volume = {24},
	number = {4},
	year = {2008},
	month = {APR},
	pages = {450-458},
	publisher = {ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD},
	address = {24-28 OVAL RD, LONDON NW1 7DX, ENGLAND},
	abstract = {<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>},
	keywords = {Fluorescence spectroscopy, Holothuria scabra, Lectin, marine invertebrate, Thermodynamic properties},
	issn = {1050-4648},
	doi = {10.1016/j.fsi.2008.01.002},
	author = {Gowda, Nagaraj M. and Goswami, Usha and Khan, Mohammad Islam}
}
