Lapanje S, Cresnar B, Vlachy V, Skerjanc J
Biochim Biophys Acta. 1978 Dec 20;537(2):380-5. doi: 10.1016/0005-2795(78)90522-6.
A thermodynamic study of the isothermal interaction of human immunoglobulin G with guanidinium chloride, a strong denaturant, has been performed. Free energies of interaction were calculated using preferential binding data obtained by measuring densities at constant chemical potential and constant composition, respectively. Enthalpies of interaction were determined calorimetrically. The values of both thermodynamic parameters as well as those of entropies of interaction have been found to depend crucially on the extent of denaturant binding.
已对人免疫球蛋白G与强变性剂氯化胍的等温相互作用进行了热力学研究。利用分别在恒定化学势和恒定组成下测量密度所获得的优先结合数据，计算了相互作用的自由能。通过量热法测定了相互作用焓。已发现这两个热力学参数的值以及相互作用熵的值都关键取决于变性剂的结合程度。
