High–Level Expression, Efficient Secretion and Folding of Human Growth Hormone in Escherichia coli View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-11

AUTHORS

Hansen M. Hsiung, Nancy G. Mayne, Gerald W. Becker

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. More... »

PAGES

991

References to SciGraph publications

Journal

TITLE

Nature Biotechnology

ISSUE

11

VOLUME

4

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt1186-991

    DOI

    http://dx.doi.org/10.1038/nbt1186-991

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1019022620


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