Complete solubilization and purification of recombinant human growth hormone produced in Escherichia coli.

ABSTRACT: High-level expression of recombinant human growth hormone (hGH) in Escherichia coli (E. coli) leads to the formation of insoluble aggregates as inclusion bodies devoid of biological activity. Until recently, significant efforts have been made to improve the recovery of active hGH from inclusion bodies. Here, we developed an efficient procedure for the production of completely soluble hGH by minimizing the formation of inclusion bodies and optimizing protein purification conditions. Under the newly established conditions we were able to obtain most of the total hGH in the soluble fraction. We show that the soluble protein can be efficiently purified in high yield by a series of chromatographic procedures. We analyzed the resulting hGH using various analytical techniques such as reversed-pha

SUBMITTER: Kim MJ 

PROVIDER: S-EPMC3567055 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature