01805nas a2200241 4500008004100000022001400041245012200055210006900177260007900246300001200325490000800337520092300345653002201268653002001290653001101310653001701321653000801338653002901346100001601375700001701391700002601408856012901434 2007 eng d a0003-986100aPurification and characterization of a lectin from endophytic fungus fusarium solani having complex sugar specificity0 aPurification and characterization of a lectin from endophytic fu a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcJAN a243-2510 v4573 a

A lectin from the mycelial extract of an endophytic strain of Fusarium solani was purified. Its hemagglutinating activity was inhibited by glycoproteins possessing N-linked as well as O-linked glycans. The thermodynamics and kinetics of binding of glycans and glycoproteins to F. solani lectin Was Studied using SUH ace plasmon resonance. The lectin showed high affinity for asialofetuin, asia-lofibrinogen, asialofibrinogen, and thyroglobulin: and comparatively low affinity for mucin, fetuin, fibrinogen, and holotransferrin. Glycoproteins showed glycans with significant contribution from enthalpy and positive entropy, suggesting several fold higher affinity than their corresponding g the involvement of non-polar protein-protein interaction. Moreover, the higher affinity of the glycoproteins was due to their faster association rates and low activation energy. (c) 2006 Elsevier Inc. All rights reserved.

10aendophytic fungus10aFusarium solani10aLectin10aPurification10aSPR10aThermodynamic properties1 aKhan, Feroz1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/purification-and-characterization-lectin-endophytic-fungus-fusarium-solani-having-complex02881nas a2200229 4500008004100000022001400041245012700055210006900182260007300251300001200324490000700336520200400343653002202347653002102369653002102390653002202411653002902433100001902462700002302481700001602504856013102520 2008 eng d a0927-025600aFirst principles calculations of thermal, equations of state and thermodynamical properties of MgH2 at finite temperatures0 aFirst principles calculations of thermal equations of state and  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcMAY a510-5160 v423 a

We present the first principles calculations of the thermodynamical properties of magnesium hydride (MgH2) over a temperature range of 0-1000 K. The phonon dispersions are determined within the density functional framework and are used to calculate the free energy of MgH2 within the quasiharmonic approximation (QHA) at each cell volume and temperature T. Using the free energies the thermal equation of state (EOS) is derived at several temperatures. From the thermal EOS structural parameters such as the equilibrium bell volume (V-0) and elastic properties, namely, bulk modulus (K-0) and its pressure derivative (K-0(')) are computed. The free energies are also used to calculate various thermodynamical properties within QHA. These include internal energy E, entropy S, specific heat capacity at constant pressure C-P, thermal pressure P-thermal(V,T) and volume thermal expansion Delta V/V (%). The good agreement of calculated values of S and Cp with experimental data exhibits that QHA can be used as a tool for calculating the thermodynamical properties of MgH2 over a wide temperature range. P-thermal(V,T) increases strongly with T at all the volumes but it is a slowly varying function of volume for T = 298-500 K. According to Karki [B.B. Karki, Am. Miner. 85 (2000) 1447] such volume based variations can be neglected and so it is possible to estimate the thermal EOS only with the knowledge of the measured P-thermal(V,T) versus temperature at ambient pressure and isothermal compression data at ambient temperature. Temperature dependence of Delta V/V(%) shows that V-0 increased with increase in temperature. However, the percentage decrease in K-0 superseded this percentage increase in V-0 even at temperatures moderately higher than 298 K. Therefore, we suggest application of temperature (T > 298 K) as an approach to enhance the hydrogen storage capacity of MgH2 because of its better compressibility at these temperatures. (C) 2007 Elsevier B.V. All rights reserved.

10aequation of state10aHydrogen storage10alattice dynamics10amagnesium hydride10aThermodynamic properties1 aKelkar, Tuhina1 aKanhere, Dilip, G.1 aPal, Sourav uhttps://library.ncl.res.in/content/first-principles-calculations-thermal-equations-state-and-thermodynamical-properties-mgh2-001956nas 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

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.

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-001599nas a2200229 4500008004100000022001400041245008800055210006900143260007500212300001100287490000700298520078500305653001601090653001701106653002001123653002901143100001601172700002301188700002301211700001601234856011901250 2009 eng d a0095-978200aCorrelations of thermodynamic properties of aqueous amino acid-electrolyte mixtures0 aCorrelations of thermodynamic properties of aqueous amino acidel a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScJAN a95-1140 v383 a

Suitable equations have been proposed to correlate thermodynamic properties, like mean ion activity coefficients, volumes and compressibilities, of amino acids in electrolyte solutions. An amino acid-electrolyte-water interaction parameter is extracted from the regression of the amino acid property values in aqueous electrolyte solution that is then transferred to an expression to correlate the properties of the electrolyte in mixtures. The single interaction parameter can successfully correlate the published data on mean ion activity coefficients, apparent molar volumes and compressibilities of amino acids as well as of electrolytes in their aqueous mixtures. The equations are tested against the large number of experimental data sets available in the literature.

10aAmino acids10aElectrolytes10aPitzer equation10aThermodynamic properties1 aSaritha, C.1 aSatpute, Dilip, B.1 aBadarayani, Rohini1 aKumar, Anil uhttps://library.ncl.res.in/content/correlations-thermodynamic-properties-aqueous-amino-acid-electrolyte-mixtures-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

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.

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