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研究21～80℃温度范围内一些蛋白质和小分子在疏水相互作用色谱中的热行为.利用Van＇t Hoff作图(lnk＇-1/T)测定蛋白质分子的热力学参数(△H°,△S°和△G°),根据标准熵变(△S°)和标准自由能变(△G°)判断蛋白质在色谱过程中的构象变化,通过△H°-△S°的线性关系估计蛋白质变性时的“补偿温度”(β),鉴定蛋白质在疏水相互作用色谱中保留机理的同一性.
The thermodynamic behavior of some proteins and small molecules in hydrophobic interaction chromatography was investigated in the temperature range of 21-80 C. The thermodynamic parameters (ΔH °, Δ) of protein molecules were determined by Van’t Hoff plotting (lnk’-1 / T) S ° and △ G °), the conformational changes of proteins were judged according to the standard entropy change (△ S °) and the standard free energy change (△ G °), and the protein was estimated by the linear relationship of △ H ° - △ S ° The “compensation temperature” (β) at denaturation identifies the mechanism of protein identity retained by hydrophobic interaction chromatography.