Production of rat epidermal growth factor by Escherichia coli cells containing a secretion plasmid
A DNA sequence encoding rat submaxillary epidermal growth factor (EGF) was designed and chemically synthesized based on the amino acid sequence described by Simpson et al. [(1985) Eur. J. Biochem. 153, 629–637]. A secretion plasmid pREGF2 was constructed which contains a hybrid gene coding for rat E...
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| Veröffentlicht in: | Journal of biotechnology 1989, Vol.10 (2), p.151-160 |
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| container_title | Journal of biotechnology |
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| creator | Ohgai, Hideo Kumakura, Takeshi Komoto, Shoichi Matsuo, Yasushi Ohshiden, Kazuhide Koide, Takao Yanaihara, Chizuko Yanaihara, Noboru |
| description | A DNA sequence encoding rat submaxillary epidermal growth factor (EGF) was designed and chemically synthesized based on the amino acid sequence described by Simpson et al. [(1985) Eur. J. Biochem. 153, 629–637]. A secretion plasmid pREGF2 was constructed which contains a hybrid gene coding for rat EGF directly preceded by the signal sequence of
E. coli β-lactamase. Rat EGF having the natural structure was secreted into the periplasm and culture medium from
E. coli cells containing the secretion plasmid. Purified synthetic rat EGF was found to possess various biological activities as reported. The effect upon [
3H]thymidine incorporation into DNA of Balb/c 3T3 cells at low dosages were slightly weaker than those of human and mouse EGFs, which might be due to the species difference among EGFs in the binding affinity to the receptor used. |
| doi_str_mv | 10.1016/0168-1656(89)90037-0 |
| format | Article |
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E. coli β-lactamase. Rat EGF having the natural structure was secreted into the periplasm and culture medium from
E. coli cells containing the secretion plasmid. Purified synthetic rat EGF was found to possess various biological activities as reported. The effect upon [
3H]thymidine incorporation into DNA of Balb/c 3T3 cells at low dosages were slightly weaker than those of human and mouse EGFs, which might be due to the species difference among EGFs in the binding affinity to the receptor used.</description><identifier>ISSN: 0168-1656</identifier><identifier>EISSN: 1873-4863</identifier><identifier>DOI: 10.1016/0168-1656(89)90037-0</identifier><identifier>CODEN: JBITD4</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Biological and medical sciences ; Biotechnology ; DNA ; Epidermal growth factor ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; Genetic engineering ; Genetic technics ; Methods. Procedures. Technologies ; Molecular cloning ; plasmids ; Recombinant DNA ; Secretion ; Signal sequence ; Synthetic gene</subject><ispartof>Journal of biotechnology, 1989, Vol.10 (2), p.151-160</ispartof><rights>1989</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-f3b31dae26c00960c27a7f877b55f65aef243ca9d154cd7790e8cefc82383003</citedby><cites>FETCH-LOGICAL-c400t-f3b31dae26c00960c27a7f877b55f65aef243ca9d154cd7790e8cefc82383003</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0168165689900370$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7374419$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Ohgai, Hideo</creatorcontrib><creatorcontrib>Kumakura, Takeshi</creatorcontrib><creatorcontrib>Komoto, Shoichi</creatorcontrib><creatorcontrib>Matsuo, Yasushi</creatorcontrib><creatorcontrib>Ohshiden, Kazuhide</creatorcontrib><creatorcontrib>Koide, Takao</creatorcontrib><creatorcontrib>Yanaihara, Chizuko</creatorcontrib><creatorcontrib>Yanaihara, Noboru</creatorcontrib><title>Production of rat epidermal growth factor by Escherichia coli cells containing a secretion plasmid</title><title>Journal of biotechnology</title><description>A DNA sequence encoding rat submaxillary epidermal growth factor (EGF) was designed and chemically synthesized based on the amino acid sequence described by Simpson et al. [(1985) Eur. J. Biochem. 153, 629–637]. A secretion plasmid pREGF2 was constructed which contains a hybrid gene coding for rat EGF directly preceded by the signal sequence of
E. coli β-lactamase. Rat EGF having the natural structure was secreted into the periplasm and culture medium from
E. coli cells containing the secretion plasmid. Purified synthetic rat EGF was found to possess various biological activities as reported. The effect upon [
3H]thymidine incorporation into DNA of Balb/c 3T3 cells at low dosages were slightly weaker than those of human and mouse EGFs, which might be due to the species difference among EGFs in the binding affinity to the receptor used.</description><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>DNA</subject><subject>Epidermal growth factor</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular cloning</subject><subject>plasmids</subject><subject>Recombinant DNA</subject><subject>Secretion</subject><subject>Signal sequence</subject><subject>Synthetic gene</subject><issn>0168-1656</issn><issn>1873-4863</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNp9kE1PwzAMhiMEEuPjH3DIASE4FJKmbdILEpr4kpDgwD3yXIcFdc1IOtD-Pe2GduRg2YfHr_2-jJ1JcS2FrG6GMpmsyurS1Fe1EEpnYo9NpNEqK0yl9tlkhxyyo5Q-hRBFXcoJm73F0Kyw96HjwfEIPaelbyguoOUfMfz0c-4A-xD5bM3vE84pepx74Bhaz5HaNg1j14PvfPfBgSfCSBu9ZQtp4ZsTduCgTXT614_Z-8P9-_Qpe3l9fJ7evWRYCNFnTs2UbIDyCoWoK4G5Bu2M1rOydFUJ5PJCIdSNLAtstK4FGSSHJldGDZ6P2cVWdhnD14pSbxc-jf9BR2GVrCyVqGReDmCxBTGGlCI5u4x-AXFtpbBjnnYMy45hWVPbTZ521D__04eE0LoIHfq029VKF4WsB-x2i9Fg9dtTtAk9dUiNj4S9bYL__84va7WKQw</recordid><startdate>1989</startdate><enddate>1989</enddate><creator>Ohgai, Hideo</creator><creator>Kumakura, Takeshi</creator><creator>Komoto, Shoichi</creator><creator>Matsuo, Yasushi</creator><creator>Ohshiden, Kazuhide</creator><creator>Koide, Takao</creator><creator>Yanaihara, Chizuko</creator><creator>Yanaihara, Noboru</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>1989</creationdate><title>Production of rat epidermal growth factor by Escherichia coli cells containing a secretion plasmid</title><author>Ohgai, Hideo ; Kumakura, Takeshi ; Komoto, Shoichi ; Matsuo, Yasushi ; Ohshiden, Kazuhide ; Koide, Takao ; Yanaihara, Chizuko ; Yanaihara, Noboru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-f3b31dae26c00960c27a7f877b55f65aef243ca9d154cd7790e8cefc82383003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>DNA</topic><topic>Epidermal growth factor</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Methods. Procedures. 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[(1985) Eur. J. Biochem. 153, 629–637]. A secretion plasmid pREGF2 was constructed which contains a hybrid gene coding for rat EGF directly preceded by the signal sequence of
E. coli β-lactamase. Rat EGF having the natural structure was secreted into the periplasm and culture medium from
E. coli cells containing the secretion plasmid. Purified synthetic rat EGF was found to possess various biological activities as reported. The effect upon [
3H]thymidine incorporation into DNA of Balb/c 3T3 cells at low dosages were slightly weaker than those of human and mouse EGFs, which might be due to the species difference among EGFs in the binding affinity to the receptor used.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><doi>10.1016/0168-1656(89)90037-0</doi><tpages>10</tpages></addata></record> |
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| ispartof | Journal of biotechnology, 1989, Vol.10 (2), p.151-160 |
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| source | Elsevier ScienceDirect Journals |
| subjects | Biological and medical sciences Biotechnology DNA Epidermal growth factor Escherichia coli Fundamental and applied biological sciences. Psychology Genetic engineering Genetic technics Methods. Procedures. Technologies Molecular cloning plasmids Recombinant DNA Secretion Signal sequence Synthetic gene |
| title | Production of rat epidermal growth factor by Escherichia coli cells containing a secretion plasmid |
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