RENATURATION OF RECOMBINANT HUMAN INTERFERON GAMMA IN THE PRESENCE OF MINICHAPERONE GROEL 191-345

摘要

Minichaperone GroEL 191-345, fragments encompassing the apical domain of GroEL, facilitates the refolding of some proteins in vitro with the absence of GroES and ATP which behave as the cage structure of multimeric GroEL. In this paper, the refolding conditions of recombinant human interferon gamma (rhIFN-γ) assisted by the soluble recombinant GroEL191-345 with a 6xHis tag in the suspended system were investigated. Optimal operating parameters were refolding temperature 15℃, refolding time 4hr, refolding system pH 7.7 and the mol ratio of GroEL191-345 versus rhIFN-γ 2:1. Compared with dilution and dialysis method, the presence of GroEL191-345 in the refolding buffer not only enhanced the specific activity, but also improved the refolding efficiency.