Calorimetric study of nonspecific interaction between lead ions and bovine serum albumin.
The nonspecific interaction between lead ions and bovine serum albumin (BSA) was studied by the calorimetric technique. According to thermodynamic parameters calculated from titration curves, it can be seen that the increase of intermolecular bond energies and decrease of disorder in the system were accompanied by a binding process. This kind of binding is the reaction "driven by enthalpy." Furthermore, the denatured BSA has more binding sites and more changes in enthalpy and entropy than the native BSA because the unfolded chain of denatured BSA could adapt itself to the binding reaction with lead ions more easily.
Peng
Liu
L
Department of Applied Chemistry, School of Sciences, Wuhan University of Technology, Wuhan, PR China. liup567@163.com
Hongyu
Xiao
X
Xi
Li
L
Lifang
Ruan
R
Chaocan
Zhang
Z
D000818:Animals; D002151:Calorimetry; D002417:Cattle; D007477:Ions / Q000737:chemistry*; D007854:Lead / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
D007477:Ions; D012710:Serum Albumin, Bovine; D007854:Lead