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PMID: 3903748 Published · ppublish English Journal Article

Synthesis and secretion of human epidermal growth factor by Escherichia coli.

Oka T, Sakamoto S, Miyoshi K, Fuwa T, Yoda K, Yamasaki M, Tamura G, Miyake T

Abstract

A synthetic gene for human epidermal growth factor (hEGF) was joined to a sequence encoding the signal peptide of Escherichia coli alkaline phosphatase. This hybrid gene was placed under the control of the alkaline phosphatase gene (phoA) promoter in a recombinant plasmid, which was used to transfect E. coli. The hybrid protein that was expressed in host cells under conditions of phosphate limitation was processed accurately during the secretion process, and mature hEGF was recovered in the periplasmic fraction. On the other hand, no EGF was detected in the periplasmic space when the synthetic hEGF gene was not accompanied by the phoA signal sequence.

MeSH Terms
Alkaline Phosphatase/genetics Amino Acid Sequence Bacterial Proteins/genetics Epidermal Growth Factor/biosynthesis,genetics,metabolism Escherichia coli/genetics,metabolism Gene Expression Regulation Genes, Synthetic Humans Promoter Regions, Genetic Protein Processing, Post-Translational Protein Sorting Signals/genetics Recombinant Proteins/genetics,metabolism
Chemicals
Bacterial Proteins Protein Sorting Signals Recombinant Proteins Epidermal Growth Factor Alkaline Phosphatase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Oka T
Sakamoto S
Miyoshi K
Fuwa T
Yoda K
Yamasaki M
Tamura G
Miyake T
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30 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1985-11-00
Pages
7212-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC390819
Subset
IM
Databases
GENBANK
M11936
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