Expression and secretion of human epidermal growth factor in Escherichia coli.

Itô, Akira; Katoh, Tomoko; Gomi, Hideyuki; Kishimoto, Fumitaka; Agui, Hideo; Ogino, Shigeo; Yoda, Koji; Yamasaki, Makari; Tamura, Gakuzo

doi:10.1271/bbb1961.50.1381

Cited by 9 publications

(4 citation statements)

References 4 publications

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“…However, further increase of temperature was harmful to product formation. In contrast to the most suitable temperature (30°C) for the intracellular hEGF expressing system obtained in the previous studies [8], the highest hEGF productivity in our system was achieved at 32°C, a temperature that is more favorable for growth.…”

Section: Effects Of Culture and Induction Conditionscontrasting

confidence: 82%

Factors influencing excretive production of human epidermal growth factor (hEGF) with recombinant Escherichia coli K12 system

Liu

Chen

et al. 2000

Bioprocess Engineering

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Human epidermal growth factor (hEGF) was expressed and excreted into culture medium in an excretory recombinant Escherichia coli system. Conditions for the production of hEGF in this system were investigated. Results showed that the slight reduction of promoter strength improved the stability of plasmid and the production of hEGF in this recombinant system. One favorable MMBL medium for hEGF production was formulated by evaluating the effects of medium components, ampicilin addition and pH. hEGF production was affected obviously by culture conditions, especially fermentation temperature. High temperature (32°C) was very bene®cial for culture process by increasing productivity and reducing the quantity of isopropyl-b-D D-thiogalactopyranoside (IPTG) for suf®cient induction. High cell density and hEGF productivity could be accomplished concomitantly by inducing the culture at middle or late log phase of cell growth. In comparison with the batch process, fed-batch cultivation could improve plasmid stability from ca. 72% to ca. 83%, and increased hEGF productivity by 24.4%. Under all these circumstances, almost all expressed hEGF (³95%) was fully excreted into the culture medium.

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Section: Effects Of Culture and Induction Conditionscontrasting

confidence: 82%

Factors influencing excretive production of human epidermal growth factor (hEGF) with recombinant Escherichia coli K12 system

Liu

Chen

et al. 2000

Bioprocess Engineering

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“…These results suggest either that the tac promoter was not effective in these hydrogen-utilizing bacteria or that EGF was expressed but not secreted, resulting in the degradation of EGF by protease. Ito et al (16) reported that the expression of EGF in the cytoplasm of E. coli resulted in low-level production because of the instability of EGF in the cytoplasm.…”

Section: Fig 2 Sds-page (A) Andmentioning

confidence: 99%

“…We chose human epidermal growth factor (EGF), a single peptide comprising 53 amino acids (11), as a model compound to establish the peptide-producing system by autotrophically grown hydrogen-utilizing bacteria. Although the production of EGF was tried with Escherichia coli by using secretion vectors (9,16,20,23,24), this is the first report on the production and secretion of EGF in autotrophic culture using a recombinant hydrogen-utilizing bacterium.…”

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confidence: 99%

Secretion of human epidermal growth factor (EGF) in autotrophic culture by a recombinant hydrogen-utilizing bacterium, Pseudomonas pseudoflava, carrying broad-host-range EGF secretion vector pKSEGF2

Hayase

Ishiyama

Niwano

1994

Appl Environ Microbiol

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We constructed the broad-host-range human epidermal growth factor (EGF) secretion plasmid pKSEGF2 by inserting the Escherichia coli tac promoter, the signal sequence of Pseudomonas stutzeri amylase, and the synthesized EGF gene into the broad-host-range vector pKT230. E. coli JM109 carrying pKSEGF2 secreted EGF into the periplasm and the culture medium under the control of the tac promoter. Pseudomonas aeruginosa

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“…A "gift of nature," easy to extract, and extremely useful in the past for their biochemical characterization and for studying their biological roles. Only in very recent years techniques of recombinant DNA may have represented a powerful alternative in producing several GFs, and providing, as an example, highly purified EGF for human therapeutical uses (Nakagawa et al, 1985;Ito et al, 1986;Brown et al, 1986). Despite the fact that most of the scientific investigations carried out during the past thirty years concerned developmental aspects of NGF biology, the actual molecules used in these studies were from adult structures (salivary glands) of unknown functioning.…”

Section: Presence Of Gfs In Adult Vertebratesmentioning

confidence: 99%

Physiological Roles of Nerve Growth Factor in Adult Rodents: A Biobehavioral Perspective

Alleva¹,

Aloe²

1989

International Journal of Comparative Psychology

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Expression and secretion of human epidermal growth factor in Escherichia coli.

Cited by 9 publications

References 4 publications

Factors influencing excretive production of human epidermal growth factor (hEGF) with recombinant Escherichia coli K12 system

Factors influencing excretive production of human epidermal growth factor (hEGF) with recombinant Escherichia coli K12 system

Secretion of human epidermal growth factor (EGF) in autotrophic culture by a recombinant hydrogen-utilizing bacterium, Pseudomonas pseudoflava, carrying broad-host-range EGF secretion vector pKSEGF2

Physiological Roles of Nerve Growth Factor in Adult Rodents: A Biobehavioral Perspective

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