Hydrophobic interaction chromatography of proteins: Studies of unfolding upon adsorption by isothermal titration calorimetry

Rodler Agnes; Beyer Beate; Ueberbacher Rene; Hahn Rainer; Jungbauer Alois

摘要

Abstract > Heat of adsorption is an excellent measure for adsorption strength and, therefore, very useful to study the influence of salt and temperature in hydrophobic interaction chromatography. The adsorption of bovine serum albumin and β‐lactoglobulin to Toyopearl Butyl‐650?M was studied with isothermal titration calorimetry to follow the unfolding of proteins on hydrophobic surfaces. Isothermal titration calorimetry is established as an experimental method to track conformational changes of proteins on stationary phases. Experiments were carried out at two different salt concentrations and five different temperatures. Protein unfolding, as indicated by large changes of molar enthalpy of adsorption Δ h <sub>ads</sub> , was observed to be dependent on temperature and salt concentration. Δ h <sub>ads</sub> were significantly higher for bovine serum albumin and ranged from 578 (288?K) to 811 (308?K) kJ/mol for 1.2?mol/kg ammonium sulfate. Δ h <sub>ads</sub> for β‐lactoglobulin ranged from 129?kJ/mol (288?K) to 186?kJ/mol (308?K). For both proteins, Δ h <sub>ads</sub> increased with increasing temperature. The influence of salt concentration on Δ h <sub>ads</sub> was also more pronounced for bovine serum albumin than for β‐lactoglobulin. The comparison of retention analysis evaluated by the van't Hoff algorithm shows that beyond adsorption other processes occur simultaneously. Further interpretation such as unfolding upon adsorption needs other in situ techniques. </abstract> </span> <span class="z_kbtn z_kbtnclass hoverxs" style="display: none;">展开▼</span> </div> <div class="translation abstracttxt"> <span class="zhankaihshouqi fivelineshidden" id="abstract"> <span>机译：</span><Abstract Type =“Main”XML：Lang =“en”> <标题类型=“main”>抽象</标题> >吸附热是吸附强度的出色措施，因此非常有用盐和温度在疏水相互作用色谱中的影响。用等温滴定热量研究牛血清白蛋白和β-乳酰叶蛋白与Toyopearl丁基-650·m的吸附，以遵循疏水表面上蛋白质的展开。等温滴定热量测定法作为跟踪固定阶段蛋白质构象变化的实验方法。实验以两种不同的盐浓度和五种不同的温度进行。蛋白质展开，如受吸附δ1摩尔焓的大变化所示，观察到依赖于温度和盐浓度。施用牛血清白蛋白显着较高，牛血清白蛋白显着高于578（288×k）至811（308×k）kj / mol，为1.2？mol / kg铵硫酸盐。 δ <sub>β-乳蛋白的ADS </ sub>范围为129Ω·kJ / mol（288 k）至186Ω·kj / mol（308 k）。对于两种蛋白质，δ2</ i> <sub> ADS </ sub>随着温度的增加而增加。对于牛血清白蛋白，盐浓度对δ3/ i> <sub> Ads </ sub>的影响比β-乳蛋白也更为显着。 VARET HOFF算法评估的保留分析的比较表明，超越吸附其他过程同时发生。进一步的解释，例如在吸附时展开，需要其他原位技术。 </ p> </ abstract> </span> <span class="z_kbtn z_kbtnclass hoverxs" style="display: none;">展开▼</span> </div> </div> <div class="record"> <h2 class="all_title" id="enpatent33" >著录项</h2> <ul> <li> <span class="lefttit">来源</span> <div style="width: 86%;vertical-align: text-top;display: inline-block;"> <a href='/journal-foreign-35800/'>《Journal of separation science.》</a> <b style="margin: 0 2px;">|</b><span>2018年第15期</span><b style="margin: 0 2px;">|</b><span>共12页</span> </div> </li> <li> <div class="author"> <span class="lefttit">作者</span> <p id="fAuthorthree" class="threelineshidden zhankaihshouqi"> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Rodler Agnes&option=202" target="_blank" rel="nofollow">Rodler Agnes;</a> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Beyer Beate&option=202" target="_blank" rel="nofollow">Beyer Beate;</a> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Ueberbacher Rene&option=202" target="_blank" rel="nofollow">Ueberbacher Rene;</a> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Hahn Rainer&option=202" target="_blank" rel="nofollow">Hahn Rainer;</a> <a href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=Jungbauer Alois&option=202" target="_blank" rel="nofollow">Jungbauer Alois;</a> </p> <span class="z_kbtnclass z_kbtnclassall hoverxs" id="zkzz" style="display: none;">展开▼</span> </div> </li> <li> <div style="display: flex;"> <span class="lefttit">作者单位</span> <div style="position: relative;margin-left: 3px;max-width: 639px;"> <div class="threelineshidden zhankaihshouqi" id="fOrgthree"> <p>Department of BiotechnologyUniversity of Natural Resources and Life Sciences ViennaVienna Austria;</p> <p>Department of BiotechnologyUniversity of Natural Resources and Life Sciences ViennaVienna Austria;</p> <p>Department of BiotechnologyUniversity of Natural Resources and Life Sciences ViennaVienna Austria;</p> <p>Department of BiotechnologyUniversity of Natural Resources and Life Sciences ViennaVienna Austria;</p> <p>Department of BiotechnologyUniversity of Natural Resources and Life Sciences ViennaVienna Austria;</p> </div> <span class="z_kbtnclass z_kbtnclassall hoverxs" id="zhdw" style="display: none;">展开▼</span> </div> </div> </li> <li > <span class="lefttit">收录信息</span> <span style="width: 86%;vertical-align: text-top;display: inline-block;"></span> </li> <li> <span class="lefttit">原文格式</span> <span>PDF</span> </li> <li> <span class="lefttit">正文语种</span> <span>eng</span> </li> <li> <span class="lefttit">中图分类</span> <span><a href="https://www.zhangqiaokeyan.com/clc/159.html" title="化学">化学;</a></span> </li> <li class="antistop"> <span class="lefttit">关键词</span> <p style="width: 86%;vertical-align: text-top;"> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=bovine serum albumin&option=203" rel="nofollow">bovine serum albumin;</a> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=lactoglobulin&option=203" rel="nofollow">lactoglobulin;</a> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=stationary phases&option=203" rel="nofollow">stationary phases;</a> <a style="color: #3E7FEB;" href="/search.html?doctypes=4_5_6_1-0_4-0_1_2_3_7_9&sertext=van't Hoff analysis&option=203" rel="nofollow">van't Hoff analysis;</a> </p> <div class="translation"> 机译：牛血清白蛋白;乳酸杆菌;固定阶段;VAN'T HOFF分析; 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