Production of recombinant human glucagon in the form of a fusion protein in Escherichia coli; recovery of glucagon by sequence-specific digestion
Recombinant human glucagon was successfully produced with a high level of expression in Escherichia coli as a fusion protein with human interferon gamma. The synthetic gene was designed to release glucagon, which does not contain glutamic acid residues, from fusion protein with the Staphylococcus au...
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| Veröffentlicht in: | Applied microbiology and biotechnology 1992, Vol.36 (4), p.483-486 |
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| container_title | Applied microbiology and biotechnology |
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| creator | ISHIZAKI, J TAMAKI, M SHIN, M TSUZUKI, H YOSHIKAWA, K TERAOKA, H YOSHIDA, N |
| description | Recombinant human glucagon was successfully produced with a high level of expression in Escherichia coli as a fusion protein with human interferon gamma. The synthetic gene was designed to release glucagon, which does not contain glutamic acid residues, from fusion protein with the Staphylococcus aureus strain V8 protease that specifically cleaves the peptide bond on the carboxyl side of the glutamic acid residue. The resulting glucagon was purified to homogeneity by a combination of C18 reverse-phase HPLC and ion-exchange HPLC. The yield of intact glucagon obtained from 11 of culture was approximately 12 mg. The structure of recombinant human glucagon was confirmed by HPLC and amino acid composition/sequence analyses. |
| doi_str_mv | 10.1007/bf00170188 |
| format | Article |
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The synthetic gene was designed to release glucagon, which does not contain glutamic acid residues, from fusion protein with the Staphylococcus aureus strain V8 protease that specifically cleaves the peptide bond on the carboxyl side of the glutamic acid residue. The resulting glucagon was purified to homogeneity by a combination of C18 reverse-phase HPLC and ion-exchange HPLC. The yield of intact glucagon obtained from 11 of culture was approximately 12 mg. The structure of recombinant human glucagon was confirmed by HPLC and amino acid composition/sequence analyses.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/bf00170188</identifier><identifier>PMID: 1368201</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>Amino Acid Sequence ; Amino Acids - analysis ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Chromatography, High Pressure Liquid ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; gamma -interferon ; Genetic engineering ; Genetic technics ; Genome, Human ; glucagon ; Glucagon - biosynthesis ; Glucagon - genetics ; Glucagon - isolation & purification ; Humans ; Interferon-gamma - biosynthesis ; Interferon-gamma - genetics ; Methods. Procedures. Technologies ; Modification of gene expression level ; Molecular Sequence Data ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - genetics ; Serine Endopeptidases - metabolism ; Technology, Pharmaceutical</subject><ispartof>Applied microbiology and biotechnology, 1992, Vol.36 (4), p.483-486</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c444t-a644ea662e6aae52f73c18024c1a87f2927964c572695d8155866eeff9eacbbe3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5065669$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1368201$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ISHIZAKI, J</creatorcontrib><creatorcontrib>TAMAKI, M</creatorcontrib><creatorcontrib>SHIN, M</creatorcontrib><creatorcontrib>TSUZUKI, H</creatorcontrib><creatorcontrib>YOSHIKAWA, K</creatorcontrib><creatorcontrib>TERAOKA, H</creatorcontrib><creatorcontrib>YOSHIDA, N</creatorcontrib><title>Production of recombinant human glucagon in the form of a fusion protein in Escherichia coli; recovery of glucagon by sequence-specific digestion</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><description>Recombinant human glucagon was successfully produced with a high level of expression in Escherichia coli as a fusion protein with human interferon gamma. The synthetic gene was designed to release glucagon, which does not contain glutamic acid residues, from fusion protein with the Staphylococcus aureus strain V8 protease that specifically cleaves the peptide bond on the carboxyl side of the glutamic acid residue. The resulting glucagon was purified to homogeneity by a combination of C18 reverse-phase HPLC and ion-exchange HPLC. The yield of intact glucagon obtained from 11 of culture was approximately 12 mg. The structure of recombinant human glucagon was confirmed by HPLC and amino acid composition/sequence analyses.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gamma -interferon</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Genome, Human</subject><subject>glucagon</subject><subject>Glucagon - biosynthesis</subject><subject>Glucagon - genetics</subject><subject>Glucagon - isolation & purification</subject><subject>Humans</subject><subject>Interferon-gamma - biosynthesis</subject><subject>Interferon-gamma - genetics</subject><subject>Methods. Procedures. 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Psychology</topic><topic>gamma -interferon</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Genome, Human</topic><topic>glucagon</topic><topic>Glucagon - biosynthesis</topic><topic>Glucagon - genetics</topic><topic>Glucagon - isolation & purification</topic><topic>Humans</topic><topic>Interferon-gamma - biosynthesis</topic><topic>Interferon-gamma - genetics</topic><topic>Methods. Procedures. 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The synthetic gene was designed to release glucagon, which does not contain glutamic acid residues, from fusion protein with the Staphylococcus aureus strain V8 protease that specifically cleaves the peptide bond on the carboxyl side of the glutamic acid residue. The resulting glucagon was purified to homogeneity by a combination of C18 reverse-phase HPLC and ion-exchange HPLC. The yield of intact glucagon obtained from 11 of culture was approximately 12 mg. The structure of recombinant human glucagon was confirmed by HPLC and amino acid composition/sequence analyses.</abstract><cop>Berlin</cop><pub>Springer</pub><pmid>1368201</pmid><doi>10.1007/bf00170188</doi><tpages>4</tpages></addata></record> |
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| identifier | ISSN: 0175-7598 |
| ispartof | Applied microbiology and biotechnology, 1992, Vol.36 (4), p.483-486 |
| issn | 0175-7598 1432-0614 |
| language | eng |
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| subjects | Amino Acid Sequence Amino Acids - analysis Base Sequence Biological and medical sciences Biotechnology Chromatography, High Pressure Liquid Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gamma -interferon Genetic engineering Genetic technics Genome, Human glucagon Glucagon - biosynthesis Glucagon - genetics Glucagon - isolation & purification Humans Interferon-gamma - biosynthesis Interferon-gamma - genetics Methods. Procedures. Technologies Modification of gene expression level Molecular Sequence Data Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - genetics Serine Endopeptidases - metabolism Technology, Pharmaceutical |
| title | Production of recombinant human glucagon in the form of a fusion protein in Escherichia coli; recovery of glucagon by sequence-specific digestion |
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