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Isolation and characterization of a trisulfide variant of recombinant human growth hormone formed during expression in Escherichia coli

✍ Scribed by ANDERSSON, CLAES ;EDLUND, PER OLOF ;GELLERFORS, PÄR ;HANSSON, YNGVE ;HOLMBERG, ERLAND ;HULT, CARINA ;JOHANSSON, STIG ;KÖRDEL, JOHAN ;LUNDIN, RONNY ;MENDEL-HARTVIG, IB ;NORÉN, BENGT ;WEHLER, THOMAS ;WIDMALM, GÖRAN ;ÖHMAN, JOHAN


Book ID
115099965
Publisher
Wiley (Blackwell Publishing)
Year
2009
Tongue
English
Weight
780 KB
Volume
47
Category
Article
ISSN
0367-8377

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Recombinant DNA derived human growth hormone (rhGH), Genotropin, has been expressed in E. coli cells as a pre-hormone, where the heat stable enterotoxin II signal peptide (STII) was linked to hGH to get secretion of the hormone to the periplasmatic space. The pre-hormone was efficiently cleaved duri