01832nas 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<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>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-0