蛋白质在疏水色谱中保留的热力学参数的测定  

Determination of Thermodynamic Parameters for Protein Retention in Hydrophobic Interaction Chromatography

作　　者：赵建国[1] 卫引茂[2] 耿信笃[2] 

机构地区：[1]雁北师范学院化学系,山西大同037000 [2]西北大学现代分离科学研究所,西安710069

出　　处：《分析科学学报》2004年第6期583-585,共3页Journal of Analytical Science

基　　金：国家自然科学基金(No.39880003)

摘　　要：研究了0～50℃内五种蛋白质在疏水色谱(HIC)中的保留行为。蛋白分子在HIC中的保留行为遵循Van'tHoff方程,并求得蛋白质分子在HIC中保留的热力学参数(△H°,△S°,△C°p和△G°)。发现蛋白质的保留由熵控制,焓、熵和热容量三个热力学参数都与绝对温度倒数间存在线性关系,并求得热容量为零的收敛温度。The thermodynamic behaviors for five proteins in hydrophobic interaction chromatography were investigated in the temperature range of 0 to 50℃. The thermodynamic parameters (△H°, △S°, △C_(p)°and △G°) of these proteins were determined by using non-linear Van't Hoff equation. It was found that the retention of proteins in HIC is driven by entropy, thermodynamic parameters except △G°correlate linearly with the reciprocal of absolute temperature, and the capacity change was converged to zero at about 592 K.

关 键 词：生物大分子 疏水色谱 保留 热力学参数 

分 类 号：O657.7[理学—分析化学] O642[理学—化学]