@article { ISI:000243572800014, title = {Purification and characterization of a lectin from endophytic fungus fusarium solani having complex sugar specificity}, journal = {Archives of Biochemistry and Biophysics }, volume = {457}, number = {2}, year = {2007}, month = {JAN}, pages = {243-251}, publisher = {ELSEVIER SCIENCE INC}, type = {Article}, address = {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA}, abstract = {

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.

}, keywords = {endophytic fungus, Fusarium solani, Lectin, Purification, SPR, Thermodynamic properties}, issn = {0003-9861}, doi = {10.1016/j.abb.2006.10.019}, author = {Khan, Feroz and Ahmad, Absar and Khan, Mohammad Islam} } @article { ISI:000256005300018, title = {First principles calculations of thermal, equations of state and thermodynamical properties of MgH2 at finite temperatures}, journal = {Computational Materials Science}, volume = {42}, number = {3}, year = {2008}, month = {MAY}, pages = {510-516}, publisher = {ELSEVIER SCIENCE BV}, type = {Article}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, abstract = {

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({\textquoteright})) 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.

}, keywords = {equation of state, Hydrogen storage, lattice dynamics, magnesium hydride, Thermodynamic properties}, issn = {0927-0256}, doi = {10.1016/j.commatsci.2007.08.014}, author = {Kelkar, Tuhina and Kanhere, Dilip G. and Pal, Sourav} } @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 = {

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.

}, 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} } @article { ISI:000261342600009, title = {Correlations of thermodynamic properties of aqueous amino acid-electrolyte mixtures}, journal = {Journal of Solution Chemistry}, volume = {38}, number = {1}, year = {2009}, month = {JAN}, pages = {95-114}, publisher = {SPRINGER/PLENUM PUBLISHERS}, address = {233 SPRING ST, NEW YORK, NY 10013 USA}, abstract = {

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.

}, keywords = {Amino acids, Electrolytes, Pitzer equation, Thermodynamic properties}, issn = {0095-9782}, doi = {10.1007/s10953-008-9355-2}, author = {Saritha, C. and Satpute, Dilip B. and Badarayani, Rohini and Kumar, Anil} } @article { ISI:000325949600005, title = {Kinetics and thermodynamics of glycans and glycoproteins binding to holothuria scabra lectin: a fluorescence and surface plasmon resonance spectroscopic study}, journal = {Journal of Fluorescence}, volume = {23}, number = {6}, year = {2013}, month = {NOV}, pages = {1147-1155}, publisher = {SPRINGER/PLENUM PUBLISHERS}, address = {233 SPRING ST, NEW YORK, NY 10013 USA}, abstract = {

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{\textquoteright} 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.

}, keywords = {Holothuria scabra, Kinetic analysis, Lectin, Surface plasmon resonance spectroscopy, Thermodynamic properties}, issn = {1053-0509}, doi = {10.1007/s10895-013-1244-4}, author = {Gowda, Nagaraj M. and Gaikwad, Sushama M. and Khan, Mohammad Islam} }