文献类型：期刊文献

英文题名：Improving the refolding of NTA protein by urea gradient and arginine gradient size-exclusion chromatography

作者：Fan, Xiangdong[1];Xu, DianSheng[1];Lu, Bing[1];Xia, Jie[1];Wei, Dongzhi[1]

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2008

卷号：70

期号：6

起止页码：1130

外文期刊名：JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000256393200049)】；

语种：英文

外文关键词：refolding; two gradients; NTA protein; aggregation; chromatography

摘要：Inclusion body refolding processes play a major role in the production of recombinant proteins. Improvement of the size-exclusion chromatography refolding process was achieved by combining a decreasing urea gradient with an increasing arginine gradient (two gradients) for the refolding of NTA protein (a new thrombolytic agent) in this paper. Different refolding methods and different operating conditions in two gradients gel filtration process were investigated with regard to increasing the NTA protein activity recovery and inhibition of aggregation. The refolding of denatured NTA protein showed this method could significantly increase the activity recovery of protein at high protein concentration. The activity recovery of 37% was obtained from the initial NTA protein concentration up to 20 mg/ml. The conclusions presented in this study could also be applied to the refolding of lysozyme. (c) 2008 Elsevier B.V. All rights reserved.