Production of bovine insulin-like growth factor 2 (bIGF2) in Escherichia coli.
Bovine insulin-like growth factor 2 (bIGF2) was produced in inclusion bodies in the cytoplasm of Escherichia coli and accumulated at high levels: 20-25% of total Coomassie-stained bacterial protein. The level of accumulation of bIGF2 was affected by the choice of codons in the 5' end of the coding sequence and by a rpoH mutation in the host cells. Purified recombinant bIGF2 had the native N terminus and the same mitogenic activity as that of bIGF2 purified from bovine serum.
Easton
A M
AM
Department of Biological Sciences, Monsanto Co., Chesterfield, MO 63198.
Gierse
J K
JK
Seetharam
R
R
Klein
B K
BK
Kotts
C E
CE
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle / Q000235:genetics; D002455:Cell Division / Q000187:drug effects; D003062:Codon; D003593:Cytoplasm / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D007335:Insulin-Like Growth Factor II / Q000096:biosynthesis* / Q000235:genetics / Q000494:pharmacology; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D021382:Protein Sorting Signals / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*
D003062:Codon; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D007335:Insulin-Like Growth Factor II