Thioredoxin-catalyzed Refolding of Recombinant Protein: Refolding of Human Pro-urokinase(Biological Chemistry)

概要

論文の詳細を見る
Thioredoxin-catalyzed refolding of recombinant protein was examined for the first time using human prourokinase as an example. The refolding maximum was significantly increased by adding thioredoxin to the conventional refolding system of pro-urokinase with the glutathione redox state adjusted. Thioredoxin was further effective in the refolding of reduced pro-urokinase. The refolding of reduced pro-urokinase proceeded efficiently with only thioredoxin added to the system without adjusting the proper redox state of glutathione. These results suggested that thioredoxin can be used as a general agent for the refolding of recombinant proteins containing disulfide bonds.
社団法人日本農芸化学会の論文
1988-11-23