Artigo Revisado por pares

Direct expression of urogastrone gene in Escherichia coli

1986; Elsevier BV; Volume: 45; Issue: 3 Linguagem: Inglês

10.1016/0378-1119(86)90029-6

ISSN

1879-0038

Autores

Kishimoto Fumitaka, Hideyuki Gomi, Kanaoka Masaharu, Nakatani Tomoyuki, Akira Itô, Katoh Tomoko, Agui Hideo, Sumida Seizo, Shigeo Ogino,

Tópico(s)

Toxin Mechanisms and Immunotoxins

Resumo

Human epidermal growth factor (urogastrone; UG) is a 53-amino acid polypeptide hormone. A 192-bp DNA fragment containing the coding sequence for methionyl UG (Met-UG) and the ribosome-binding site (RBS) was chemically synthesized and placed downstream from the promoter for the Escherichia coli outer-membrane lipoprotein gene (Ipp) on a plasmid. E. coli cells harboring the plasmid directed the synthesis of Met-UG at 102-102 molecules per cell. Next, the coding sequence for Met-UG was inserted in a runaway-replication plasmid and expressed under the control of the lpp promoter and the RBS derived from bacteriophage Mu cII gene. Upon heat induction, the cells harboring the recombinant plasmid synthesized 105 molecules of Met-UG per cell.

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