小型类胰岛素生长因子-1的制备及其体外解折叠的初步研究

Purification and Putative in Vitro Unfolding Pathway of Mini-IGF-1

构建mini-IGF-1作为IGF-1的模型肽,利用酿酒酵母高效表达系统表达,并对模型肽进行分离纯化。利用二硫键稳定性测试,得到在[GSH/GSSG]为30/1和40/1条件时mini-IGF-1体外解折叠中间体最多。采用[GSH/GSSG]为30/1的比例对mini-IGF-1进行体外解折叠,通过对mini-IGF-1解折叠过程中间体的分析,得出mini-IGF-1解折叠和重折叠的过程是可逆的结论。

Construction of mini-IGF-1 as a model peptide of IGF-1, the high-level expression system of Saccharomyces cerevisiae expression of the model peptide purified. In the disulfide-stabilized test, mini- IGF-1 in vitro unfolding under the condition of [GSH/GSSG] at 30/1 and 40/1 intermediates maximum. The approach is in a 30/1 ration of reduced glutathione to oxidized glutathione. The authors study the in vitro unfolding pathways of mini-IGF-1, and analyse the intermediates. The result shows the in vitro foldoing/unfolding pathway may be similar and share some common intermediates but reverse.