@article { ISI:000251714500004,
	title = {Complex carbohydrate specificity of lectin from fruiting body of ganoderma lucidum. a surface plasmon resonance study},
	journal = {IUBMB Life},
	volume = {59},
	number = {12},
	year = {2007},
	month = {JAN},
	pages = {758-764},
	publisher = {JOHN WILEY \& SONS INC},
	type = {Article},
	address = {111 RIVER ST, HOBOKEN, NJ 07030 USA},
	abstract = {<p>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.</p>},
	keywords = {ganoderma lucidum, glycans, Lectin, SPR},
	issn = {1521-6543},
	doi = {10.1080/15216540701663463},
	author = {Thakur, Atul and Pal, Lakhan 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 = {<p>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.</p>},
	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}
}
