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

作　　者：刘弈岩[1] 赵杰[1] 程龙霄[1] 唐月华[2] 冯佑民[2] 

机构地区：[1]浙江理工大学生命科学学院,杭州310018 [2]中国科学院上海生命科学研究院生物化学与细胞生物学研究所,上海200031

出　　处：《浙江理工大学学报（自然科学版）》2009年第5期782-785,共4页Journal of Zhejiang Sci-Tech University(Natural Sciences)

摘　　要：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.

关 键 词：小型类胰岛素生长因子-1 纯化 解折叠 中间体 

分 类 号：Q518.4[生物学—生物化学]