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A differential scanning calorimetric study on the irreversible thermal unfolding of concanavalin A

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Title A differential scanning calorimetric study on the irreversible thermal unfolding of concanavalin A
 
Creator BANERJEE, TUHINA
NAND KISHORE
 
Subject calorimetry
concanavalin a
irreversible thermal denaturation
enthalpy
activation energy
 
Description A differential scanning calorimetry study on the thermal denaturation of concanavalin A at pH 5.2 where it exists in the dimeric form was carried out. The calorimetric transitions were observed to be irreversible and the transition temperature of the protein increased with increasing scan rate, indicating that the thermal denaturation process is under kinetic control. The thermal unfolding, and its scan rate dependence could be explained according to the kinetic scheme N2 →k 2U with k as first-order kinetic constant whose change with temperature is given by the Arrhenius equation. Using this model, rate constant as a function of temperature and activation energy of the process have been calculated. The average activation energy of the kinetic process using different approaches is 129±10 kJ mol−1. The differential scanning calorimetric results on transition temperatures and calorimetric enthalpies supported by intrinsic fluorescence indicate that the irreversibility in the calorimetric transitions of concanavalin A includes a combination of post-transition aggregation, chain separation and loss of cofactor.
 
Publisher Elsevier
 
Date 2009-03-02T09:30:51Z
2011-11-25T18:22:37Z
2011-12-26T13:06:33Z
2011-12-27T05:54:34Z
2009-03-02T09:30:51Z
2011-11-25T18:22:37Z
2011-12-26T13:06:33Z
2011-12-27T05:54:34Z
2004
 
Type Article
 
Identifier Thermochimica Acta 411(2), 195-201
0040-6031
http://dx.doi.org/10.1016/j.tca.2003.08.012
http://hdl.handle.net/10054/843
http://dspace.library.iitb.ac.in/xmlui/handle/10054/843
 
Language en