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-001836nas a2200241   4500008004100000022001400041245017800055210006900233260009500302300001200397490000700409520087500416653001801291653002701309653001901336653002201355653001101377653001701388100002301405700001801428700002601446856012201472       2008                        eng d  a0022-201100aT-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): possible involvement in differential recognition of bacteria0 aTantigen binding lectin with antibacterial activity from marine   a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcOCT  a141-1450 v993 a<p>In invertebrates, cellular and humoral components are evolved to maintain their body immunity and integrity. Both these factors respond to different antigens such as microorganisms, vertebrate erythrocytes and foreign proteins. In this article, we report a study of a lectin (HSL) involved in immune response in the echinoderm, sea Cucumber (Holothuria scabra). Correlative studies indicate that the expression of this defensive lectin is induced by bacterial challenge, wherein cell wall glycoconjugates of bacteria are involved in lectin induction. HSL showed strong broad spectrum antibacterial activity against both gram-positive and gram-negative bacteria. Under in vitro conditions, purified HSL mediate agglutination of the test bacteria, there by indicating a possible mode of action in physiological situation. (c) 2008 Elsevier Inc. All rights reserved.</p>10aagglutination10aantibacterial activity10acoelomic fluid10aHolothuria scabra10aLectin10asea cucumber1 aGowda, Nagaraj, M.1 aGoswami, Usha1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/t-antigen-binding-lectin-antibacterial-activity-marine-invertebrate-sea-cucumber-002493nas a2200229   4500008004100000022001400041245010300055210006900158260006900227300001200296490000700308520163100315653002501946653002501971653002501996653002702021100001602048700002302064700002502087700002002112856013102132       2009                        eng d  a1011-134400aRhodotorula aurantiaca penicillin V acylase: active site characterization and fluorometric studies0 aRhodotorula aurantiaca penicillin V acylase active site characte  aPO BOX 564, 1001 LAUSANNE, SWITZERLANDbELSEVIER SCIENCE SAcNOV  a109-1160 v973 a<p>Penicillin V acylase (PVA), a member of newly evolved Ntn-hydrolase superfamily, is a pharmaceutically important enzyme to produce 6-aminopenicillanic acid. Active site characterization of recently purified monomeric PVA from Rhodotorula aurantiaca (Ra-PVA), the yeast source, showed the involvement of serine and tryptophan in the enzyme activity. Modification of the protein with serine and tryptophan specific reagents such as PMSF and NBS showed partial loss of PVA activity and substrate protection. Ra-PVA was found to be a multi-tryptophan protein exhibiting one tryptophan, in native and, four in its denatured condition. Various solute quenchers and substrate were used to probe the microenvironment of the putative reactive tryptophan through fluorescence quenching. The results obtained indicate that the tryptophan residues of Ra-PVA were largely buried in hydrophobic core of the protein matrix. Quenching of the fluorescence by acrylamide was collisional. Acrylamide was the most effective quencher amongst all the used quenchers, which quenched 71.6% of the total intrinsic fluorescence of the protein, at a very less final concentration of 0.1 M. Surface tryptophan residues were found to have predominantly more electropositively charged amino acids around them, however differentially accessible for ionic quenchers. Denaturation led to shift lambda(max) from 336, in native state, to 357 nm and more exposed to the solvent, consequently increase in fluorescence quenching with all quenchers. This is an attempt towards the conformational studies of Ra-PVA. (C) 2009 Elsevier B.V. All rights reserved.</p>10aactive site residues10aFluorometric studies10aPenicillin V acylase10aRhodotorula aurantiaca1 aKumar, Atul1 aGowda, Nagaraj, M.1 aGaikwad, Sushama, M.1 aPundle, Archana  uhttps://library.ncl.res.in/content/rhodotorula-aurantiaca-penicillin-v-acylase-active-site-characterization-and-fluorometric-002404nas a2200229   4500008004100000022001400041245016300055210006900218260007500287300001400362490000700376520146300383653002201846653002101868653001101889653004301900653002901943100002301972700002501995700002602020856012802046       2013                        eng d  a1053-050900aKinetics and thermodynamics of glycans and glycoproteins binding to holothuria scabra lectin: a fluorescence and surface plasmon resonance spectroscopic study0 aKinetics and thermodynamics of glycans and glycoproteins binding  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScNOV  a1147-11550 v233 a<p>Holothuria scabra produces a monomeric lectin (HSL) of 182 kDa. HSL showed strong antibacterial activity and induced bacterial agglutination under in vitro conditions, indicating its role in animals' innate immune responses. Very few lectins have been reported from echinoderms and none of these lectins have been explored in detail for their sugar-binding kinetics. Affinity, kinetics and thermodynamic analysis of glycans and glycoproteins binding to HSL were studied by fluorescence and surface plasmon resonance spectroscopy. Lectin binds with higher affinity to O-linked than N-linked asialo glycans, and the affinities were relatively higher than that for sialated glycans and glycoproteins. T-antigen alpha-methyl glycoside was the most potent ligand having the highest affinity (Ka 8.32 x10(7) M-1). Thermodynamic and kinetic analysis indicated that the binding of galactosyl Tn-antigen and asialo glycans is accompanied by an enthalpic contribution in addition to higher association rate coupled by low activation energy for the association process. Presence of sialic acid or protein matrix inhibits binding. Higher affinity of HSL for O-glycans than N-glycans had biological implications; since HSL specifically recognizes bacteria, which have mucin or O-glycan cognate on their cell surfaces and play a major role in animal innate immunity. Since, HSL had higher affinity to T-antigen, makes it a useful tool for cancer diagnostic purpose.</p>10aHolothuria scabra10aKinetic analysis10aLectin10aSurface plasmon resonance spectroscopy10aThermodynamic properties1 aGowda, Nagaraj, M.1 aGaikwad, Sushama, M.1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/kinetics-and-thermodynamics-glycans-and-glycoproteins-binding-holothuria-scabra-lectin-0