Szewczuk M R, Mukkur T K
Immunology. 1977 Feb;32(2):111-9.
The effect of varying the temperature over a wide range (-3 dergees -67 degrees) on the binding of xi-DNP-L-Lysine to bovine colostral anti-DNA IgG1, and also rabbit anti-DNP IgG revealed non-linear van't Hoff plots. The extent of the curvatures were found to be indicative of large positive heat capacity changes; and the thermodynamic parameters, calculated using a non-linear least-squares computer procedure for these anti-DNP antibody preparations, revealed an enthalpy-entropy compensation mechanism for hapten-antibody binding. The enthalpy factor was found to be the primary contributor for the binding process at low temperatures, but at increasing temperatures the entropy factor assumed greater importance. At physiological temperature (37 degrees), the entropy factor was the major contributor to the free energy of reaction for rabbit anti-DNP IgG, while for bovine colostral anti-DNP IgG it was predominant at temperatures higher than 37 degrees.
在很宽的温度范围（-3℃至67℃）内改变温度，对ξ-二硝基-L-赖氨酸与牛初乳抗DNA IgG1以及兔抗二硝基苯酚IgG结合的影响显示出非线性的范特霍夫图。发现曲率程度表明有很大的正热容变化；使用非线性最小二乘法计算机程序为这些抗二硝基苯酚抗体制剂计算的热力学参数，揭示了半抗原-抗体结合的焓-熵补偿机制。发现焓因素是低温下结合过程的主要贡献者，但随着温度升高，熵因素变得更加重要。在生理温度（37℃）下，熵因素是兔抗二硝基苯酚IgG反应自由能的主要贡献者，而对于牛初乳抗二硝基苯酚IgG，它在高于37℃的温度下占主导地位。
