Szewczuk M R, Mukkur T K
Immunology. 1977 Jul;33(1):11-6.
Investigation of the binding of epsilon-DNP-1-lysine to the subunits (Fab') of bovine colostral IgG1 anti-DNP over a wide range of temperatures yielded non-linear van't Hoff plots with curvatures which were indicative of large positive heat capacity changes. Thermodynamic functions which were calculated using a non-linear least-squares procedure revealed an enthalpy-entropy compensation mechanism for binding. While the enthalpy factor was the driving force for the hapten-subunit interaction(s) at low temperatures, the entropy factor assumed greater importance with increasing temperatures. In addition, the enthalpy-entropy compensation plot for the interaction of epsilon-DNP-1-lysine with bovine colostral Fab' anti-DNP, intact anti-DNP IgG1 and rabbit IgG anti-DNP revealed a constant compensation temperature (T degrees c) of 27 degrees which might be considered as indicative of a single kind of protein-solvent conformation.
在很宽的温度范围内研究ε-二硝基苯-1-赖氨酸与牛初乳IgG1抗二硝基苯亚基（Fab'）的结合，得到了非线性的范特霍夫图，其曲率表明有很大的正热容变化。使用非线性最小二乘法程序计算的热力学函数揭示了结合的焓-熵补偿机制。虽然在低温下焓因子是半抗原-亚基相互作用的驱动力，但随着温度升高熵因子变得更为重要。此外，ε-二硝基苯-1-赖氨酸与牛初乳Fab'抗二硝基苯、完整抗二硝基苯IgG1和兔IgG抗二硝基苯相互作用的焓-熵补偿图显示，恒定补偿温度（T℃）为27℃，这可能被视为单一类型蛋白质-溶剂构象的指示。
