02294nas a2200241 4500008004100000022001400041245009300055210006900148260006700217300001000284490000700294520147800301653001701779653002001796653001401816653001101830653001201841653001401853100001601867700001701883700002601900856012601926 2007 eng d a1521-654300aChemical, thermal and pH-induced equilibrium unfolding studies of fusarium solani lectin0 aChemical thermal and pHinduced equilibrium unfolding studies of  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcDEC a34-430 v593 a

The effect of urea, guanidine thiocyanate, temperature and pH was studied on the conformational stability of Fusarium solani lectin. Equilibrium unfolding with chemical denaturants showed that the lectin was least stable at pH 12 and maximally stable at pH 8.0 near its pI ( 8.7). Guanidine thiocyanate ( the concentration of denaturant at which the protein is half folded, D-1/2 = 0.49 M at pH 12) was found to be an eight times stronger denaturant than urea (D-1/2 = 3.88 M at pH 12). The unfolding curves obtained with fluorescence and CD measurements showed good agreement indicating a monophasic nature of unfolding and excluded the possibility of formation of any stable intermediate. The effect of pH on the lectin was found to be unusual as at acidic pH, the lectin showed a flexible tertiary structure with pronounced secondary structure, and retained its hemagglutinating activity. On the other hand, the lectin did not show any loss of conformation or activity upto 70 degrees C for 15 min. Moreover, thermal denaturation did not result in the aggregation or precipitation of the protein even at high temperatures. Thermal denaturation was also carried out in the presence of a low concentration of guanidine thiocyanate. Change in the enthalpy of transition (Delta H-m) varied linearly with transition temperature (T-m), which indicated that the heat capacity (Delta C-p =3.95 kJ (.) mol(-1) (.) K-1) of the lectin remained constant during the unfolding.

10aDenaturation10aFusarium solani10aguanidine10aLectin10athermal10aUnfolding1 aKhan, Feroz1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/chemical-thermal-and-ph-induced-equilibrium-unfolding-studies-fusarium-solani-lectin-001832nas a2200229 4500008004100000022001400041245012200055210006900177260006800246300001200314490000700326520101100333653002201344653001201366653001101378653000801389100001701397700001601414700001701430700002601447856012901473 2007 eng d a1521-654300aComplex carbohydrate specificity of lectin from fruiting body of ganoderma lucidum. a surface plasmon resonance study0 aComplex carbohydrate specificity of lectin from fruiting body of a111 RIVER ST, HOBOKEN, NJ 07030 USAbJOHN WILEY & SONS INCcJAN a758-7640 v593 a

The thermodynamics and kinetics of binding of glycans and glycoproteins to Ganoderma lucidum lectin was studied using surface plasmon resonance. The lectin showed highest affinity for asialo triantennary N glycan (Ka = 3.52 x 10(5)) among the glycans tested. There was a several fold increase in affinity for glycoproteins compared to their corresponding glycans and coincident increase in contribution from enthalpy (Delta H), suggesting the involvement of hydrogen bonding in the interaction as well as involvement of protein-protein interactions. Increased affinity also showed increase in unfavorable negative binding entropy (Delta S) which was compensated with higher enthalpy. The glycoproteins showed faster association rates (k(1)) and the activation energy (E-1(double dagger)) in the association process was much lower for the glycoproteins than glycans, resulting in their faster associations. These observations elaborate the role of protein matrix in lectin-glycoconjugate interaction.

10aganoderma lucidum10aglycans10aLectin10aSPR1 aThakur, Atul1 aPal, Lakhan1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/complex-carbohydrate-specificity-lectin-fruiting-body-ganoderma-lucidum-surface-plasmon-001805nas 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-complex02268nas a2200241 4500008004100000022001400041245014300055210006900198260007500267300001200342490000700354520137800361653002601739653001701765653001301782653001101795653001401806653001801820100001601838700001701854700002601871856012901897 2010 eng d a1053-050900aSteady state and time resolved fluorescence quenching and chemical modification studies of a lectin from endophytic fungus fusarium solani0 aSteady state and time resolved fluorescence quenching and chemic a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGER/PLENUM PUBLISHERScJAN a305-3130 v203 a

The solute quenching studies of a lectin from endophytic fungus Fusarium solani were carried out using different quenchers such as acrylamide, succinimide, potassium iodide and cesium chloride. The lectin showed emission maximum at 348 nm indicating relative exposure of tryptophan. The quenchable fraction of the fluorophore was 100% with acrylamide, whereas it was only 50% with succinimide. The ionic quenchers iodide and cesium showed opposite effects at different pH. In the case of cesium, raising the pH resulted in increased quenching and accessibility of typtophan residue, while the iodide showed just opposite effect. These studies showed that the single tryptophan residue of the lectin (per monomer) is relatively exposed, and might be in the vicinity of positively charged amino acid residues. Various amino acids of the F. solani lectin were modified using different reagents to obtain information about the hemagglutinating site. The chemical modification studies suggested tyrosine residues can be modified using N-acetylimidazole, which results in complete loss of hemagglutination activity of the lectin. Kinetics of chemical modification suggested involvement of only 2 tyrosine residues. Modification of arginine, cysteine, histidine, lysine, aspartate, glutamate and tryptophan did not result in loss of hemagglutinating activity of the lectin.

10aChemical modification10afluorescence10aFusarium10aLectin10aQuenching10aTime-resolved1 aKhan, Feroz1 aAhmad, Absar1 aKhan, Mohammad, Islam uhttps://library.ncl.res.in/content/steady-state-and-time-resolved-fluorescence-quenching-and-chemical-modification-studies-0