@article { ISI:000244890900006, title = {Chemical, thermal and pH-induced equilibrium unfolding studies of fusarium solani lectin}, journal = {IUBMB Life}, volume = {59}, number = {1}, year = {2007}, month = {DEC}, pages = {34-43}, publisher = {WILEY-BLACKWELL}, type = {Article}, address = {111 RIVER ST, HOBOKEN 07030-5774, NJ USA}, abstract = {

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.

}, keywords = {Denaturation, Fusarium solani, guanidine, Lectin, thermal, Unfolding}, issn = {1521-6543}, doi = {10.1080/15216540601178075}, author = {Khan, Feroz and Ahmad, Absar and Khan, Mohammad Islam} } @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:000274401600036, title = {Steady state and time resolved fluorescence quenching and chemical modification studies of a lectin from endophytic fungus fusarium solani}, journal = {Journal of Fluorescence}, volume = {20}, number = {1}, year = {2010}, month = {JAN}, pages = {305-313}, publisher = {SPRINGER/PLENUM PUBLISHERS}, address = {233 SPRING ST, NEW YORK, NY 10013 USA}, abstract = {

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.

}, keywords = {Chemical modification, fluorescence, Fusarium, Lectin, Quenching, Time-resolved}, issn = {1053-0509}, doi = {10.1007/s10895-009-0556-x}, author = {Khan, Feroz and Ahmad, Absar and Khan, Mohammad Islam} }