Recombinant murine growth hormone from E. coli inclusion bodies: expression, high-pressure solubilization and refolding, and characterization of activity and structure.

We expressed recombinant murine growth hormone (rmGH) in E. coli as a cost-effective way to produce large quantities (gram scale) of the protein for use in murine studies of immunogenicity to therapeutic proteins. High hydrostatic pressure was used to achieve high solubility and high refolding yields of rmGH protein produced in E.