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化学学报
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化学学报 ›› 1998, Vol. 56 ›› Issue (8): 807-811. 上一篇    下一篇

研究论文

蛋白质在疏水色谱中的变性热力学

边六交;陈国亮;李蓉;李华儒   

  1. 西北大学化学工程系
  • 发布日期:1998-08-15

Denatured thermodynamics for proteins in hydrophobic interaction chromatography

BIAN LIUJIAO;CHEN GUOLIANG;LI RONG;LI HUARU   

  • Published:1998-08-15

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被引次数

9 | 3

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(ΔH°, ΔS°和ΔG°), 根据标准熵变(ΔS°)和标准自由能变(ΔG°)判断蛋白质在色谱过程中的构象变化, 通过ΔH°-ΔS°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。

关键词: 热力学, 保留, 参数, 构象, 蛋白质, 疏水反应相色谱, 热力学分析, 陕西省自然科学基金

The thermodynamic behaviors for some proteins and small molecules in hydrophobic interaction chromatography are studied in the temperature range of 21-80℃. The thermodynamic parameters (ΔH°, ΔS°, ΔG°) of these proteins are determined by using Van't Hoff relationship (lnk'-1/T). By using the obtained standard entropy change (ΔS°) and free energy change (ΔG°), the conformational change of the proteins is judged in chromatographic process. The linear relationships between ΔH° and ΔS° can be used to evaluate "compensation temperature" (β) at the protein denaturation and identify the identity of the protein retention mechanism in hydrophobic interaction chromatography.

Key words: THERMODYNAMICS, RETENTION, PARAMETER, CONFORMATION, PROTEIN, HYDROPHOBIC INTERACTION CHROMATOGRAPHY, THERMODYNAMIC ANALYSIS

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