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Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)

DRS at CSIR-National Institute of Oceanography

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Title Purification and characterization of a T-antigen specific lectin from the coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra)
 
Creator Gowda, N.M.
Goswami, U.
Khan, M.I.
 
Subject Marine invertebrate
Holothuria scabra
Fluorescence spectroscopy
sea cucumber
 
Description 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.
 
Date 2008-04-01T07:21:08Z
2008-04-01T07:21:08Z
2008
 
Type Journal Article
 
Identifier Fish & Shellfish Immunology, vol.24(4); 450-458p.
no
http://drs.nio.org/drs/handle/2264/1046
 
Language en
 
Rights Copyright [2008] Elsevier
 
Publisher Elsevier