Abstract
We have constructed a secretion vector containing genes that code for the Escherichia coli ompA signal peptide and human growth hormone (hGH). The recombinant fusion protein was expressed in E. coli cells harboring the vector and the correctly processed hGH was secreted into the E. coli periplasm, yielding 10–15 μg hGH/A600 cells in the periplasm. Purified hGH was shown to have the correct amino terminus, and also the correct disulfide bonds and the proper secondary structure. The results indicate that the E. coli periplasm can provide an environment to facilitate efficient disulfide bond formation and proper folding of hGH. The purification and isolation of the recombinant protein are greatly simplified and the processes needed to refold recombinant proteins derived from the E. coli cytoplasm are eliminated.
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