荧光相图法研究脲诱导牛血清白蛋白的去折叠过程  

Studies on Unfolding of Bovine Serum Albumins Induced by Urea in the Presence of Denaturant by Fluorescence Phase Diagram

作　　者：傅容湛[1] 董发昕[2] 边六交[1] 

机构地区：[1]西北大学基因工程药物研究开发中心,陕西西安710069 [2]西北大学化学系实验中心,陕西西安710069

出　　处：《分析测试学报》2006年第6期19-22,共4页Journal of Instrumental Analysis

摘　　要：用荧光相图法研究了脲诱导的牛血清白蛋白的去折叠过程。实验结果表明,当变性体系中存在还原剂2-巯基乙醇时,牛血清白蛋白在脲溶液中直接从天然态转变为去折叠态,没有中间态存在,此时该蛋白的去折叠过程符合典型的“二态模型”;当变性体系中无还原剂存在时,脲浓度从0 mol/L变化至0.7 mol/L时,牛血清白蛋白从天然态转变为部分折叠中间态,当脲浓度从0.7 mol/L变化至8.0 mol/L时,牛血清白蛋白从中间态转变为完全去折叠态,此时该蛋白的变性过程符合“三态模型”。The unfolding of bovine serum albumins（BSA） induced by urea in the presence of denaturant was studied by fluorescence phase diagram. Experimental results showed that the BSA induced by urea were directly unfolded from native state to unfolded state in the presence of denaturant, 2-mercaptoethanol and no folded intermediates were detected. It was found that the unfolding procedure conformed to a typical two-state model. However, a partially folded BSA intermediate could be detected in the absence of 2-mercaptoethanol at urea concentration varying from 0 mol/L to 0.7 mol/L, and the BSA would transform totally from the intermediate state to unfolded state at urea concentration varying from 0. 7 mol/L to 8.0 mol/L. At this moment, the denaturation process of BSA conformed to a typical three-state model.

关 键 词：牛血清白蛋白 荧光相图法 蛋白质去折叠 脲 还原剂 

分 类 号：O657.3[理学—分析化学]