Unfolding of pepsin induced by urea or guanidine hydrochloride with fluorescence phase diagram
2007
Liu Li | Dong Faxin | Xu Yaoping
中国人. 蛋白质折叠机理的研究是基因重组蛋白质高效生产的前提条件，对于工业化生产重组蛋白以及治疗与蛋白集聚密切相关的疾病都有重要意义。为了探索一个统一的蛋白质折叠机理， 用荧光相图法分别对脲和盐酸胍诱导的胃蛋白酶的去折叠过程进行了研究。结果表明，无论变性体系中有无还原剂2-巯基乙醇存在，当脲浓度为0~8.0 mol/L时，脲诱导胃蛋白酶的变性过程都符合“二态模型”；而无论变性体系中有无还原剂2-巯基乙醇存在，当盐酸胍浓度为0~6.0 mol/L时，该蛋白的变性过程均符合“三态模型”。
显示更多 [+] 显示较少 [-]英语. The research of the mechanism of the protein folding is the precondition of highly efficient production of genetic recombinant proteins, which has important significance to the industrial production of recombinant protein and treatment of those diseases closely related to the protein aggregation. To explore a unified mechanism of protein folding, the unfolding of pepsin induced by urea or guanidine hydrochloride has been studied by“phase diagram”method of fluorescence. The experimental results show that whether 2-mercaptoethanol exists in the denaturant solution or not, when urea concentrations are changed under the range of 0 to 8.0 mol/ L, the unfolding procedures of pepsin obey a typical “two-state model”; while whether the 2-mercaptoethanol exists in the denaturant solution or not, when guanidine hydrochloride concentrations are changed under the range of 0 to 6.0 mol/ L, the unfolding of pepsin obey a typical “three-state model”.
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