title: Periplasmic secretion of human growth hormone by Escherichia coli.
abstract: The gene coding for human growth hormone (hGH) was fused to the coding sequence for the signal peptide of a secreted Escherichia coli protein. STII heat-stable enterotoxin. This hybrid gene was expressed in E. coli. The signal peptide is properly processed and hGH is secreted in to the periplasmic space. In E. coli, some of the material made is proteolytically clipped or deamidated. The effect of culture conditions on the expression and secretion of hGH was studied and several important parameters were identified, including culture temperature and duration, cultivation pH, K+ levels, plasmid structure, and nutrient supplements. Alteration of culture conditions significantly improves the recovery yield and product quality of human growth hormone.
authors.affiliation: Department of Fermentation Research and Process Development, Genentech, Inc., South San Francisco, CA 94080.
authors.forename: J Y
authors.initials: JY
authors.lastname: Chang
authors.forename: R C
authors.initials: RC
authors.lastname: Pai
authors.forename: W F
authors.initials: WF
authors.lastname: Bennett
authors.forename: B R
authors.initials: BR
authors.lastname: Bochner
mesh_terms: D003470:Culture Media; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005818:Genetic Engineering; D013006:Growth Hormone / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D015151:Immunoblotting; D010957:Plasmids; D011188:Potassium / Q000494:pharmacology; D013696:Temperature
chemical_list: D003470:Culture Media; D013006:Growth Hormone; D011188:Potassium