Isolation, sequence, and bacterial expression of a cDNA for (S)-tetrahydroberberine oxidase from cultured berberine-producing Coptis japonica cells
cDNA clones for the (S)-tetrahydroberberine (H4Ber) oxidase of cultured berberine-producing Coptis japonica cells were isolated by screening a C. japonica cDNA library with synthetic nucleotides that can encode the NH2-terminal sequence of this enzyme. Analyses of the nucleotide sequences of the clo...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1989-01, Vol.86 (2), p.534-538 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 538 |
|---|---|
| container_issue | 2 |
| container_start_page | 534 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 86 |
| creator | Okada, N Koizumi, N Tanaka, T Ohkubo, H Nakanishi, S Yamada, Y |
| description | cDNA clones for the (S)-tetrahydroberberine (H4Ber) oxidase of cultured berberine-producing Coptis japonica cells were isolated by screening a C. japonica cDNA library with synthetic nucleotides that can encode the NH2-terminal sequence of this enzyme. Analyses of the nucleotide sequences of the cloned cDNA inserts revealed a 759-base-pair open reading frame that encoded a 253-amino acid polypeptide with a Mr of 27,089 and NH2-terminal and internal sequences identical with those of the (S)-H4Ber oxidase, as determined by microsequencing methods. Escherichia coli were transformed with an expression vector carrying (S)-H4Ber oxidase cDNA. The transformed bacteria were induced to overproduce a 28-kDa protein that reacted with Coptis (S)-H4Ber oxidase-specific antibody. A comparison of the derived amino acid sequence of (S)-H4Ber oxidase with sequences in the protein data base of the Protein Research Foundation showed a marked similarity between (S)-H4Ber oxidase and the NH2-terminal portion of mouse P1-450, which is encoded by a single exon of the mouse P1-450 gene. The availability of cloned cDNA for (S)-H4Ber oxidase allows use of the methods of molecular biology to study the regulation of (S)-H4Ber oxidase gene expression in cultured C. japonica cells in relation to berberine biosynthesis. |
| doi_str_mv | 10.1073/pnas.86.2.534 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pnas_</sourceid><recordid>TN_cdi_pnas_primary_86_2_534_fulltext</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>33159</jstor_id><sourcerecordid>33159</sourcerecordid><originalsourceid>FETCH-LOGICAL-c596t-dc36942e27d5d6d0aa8fb57f78bcf4272ed96ab4c9d13a4b6793996e72bc2753</originalsourceid><addsrcrecordid>eNqFkc1u1DAUhSMEKkNhyQaB5AUgkJrBdmI7XrCohr9KFSxa1taNY089ysSp7aDpc_DCeJjpUDYgWfLifPf4Hp-ieErwnGBRvRsHiPOGz-mcVfW9YkawJCWvJb5fzDCmomxqWj8sHsW4whhL1uCj4ojWvOIVnhU_z6LvITk_nKBoriczaHOCYOhQCzqZ4KBHZjMGE2NmkLcIkP7w9RRZH9Cbi7dlMinA1U0XfGtCPm4wyG9cB9EgG_wa6alPUzDZ8FYvx-C7SbthiRZ-TC6iFYx-cDpbm76Pj4sHFvponuzv4-Ly08fLxZfy_Nvns8XpeamZ5KnsdMVlTQ0VHet4hwEa2zJhRdNqW1NBTSc5tLWWHamgbrmQlZTcCNpqKlh1XLzf2Y5TuzadNkNO0qsxuDWEG-XBqb-VwV2ppf-haMMZ5nn-9X4--PxxMam1i9sAMBg_RSWahgpO2X9BwiglmNUZLHegDj7GYOxhGYLVtmy1LVs1XFGVy878i7sJDvS-3ay_3OsQNfQ2wKBdPGCCkLr5HeT5Htu636p3Xnn1D1nZqe-T2aTMPdtxq5h8OIBVRZj8I1rwCpYhr_H9opE4JxfVL1Pk3nI</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15221054</pqid></control><display><type>article</type><title>Isolation, sequence, and bacterial expression of a cDNA for (S)-tetrahydroberberine oxidase from cultured berberine-producing Coptis japonica cells</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Okada, N ; Koizumi, N ; Tanaka, T ; Ohkubo, H ; Nakanishi, S ; Yamada, Y</creator><creatorcontrib>Okada, N ; Koizumi, N ; Tanaka, T ; Ohkubo, H ; Nakanishi, S ; Yamada, Y</creatorcontrib><description>cDNA clones for the (S)-tetrahydroberberine (H4Ber) oxidase of cultured berberine-producing Coptis japonica cells were isolated by screening a C. japonica cDNA library with synthetic nucleotides that can encode the NH2-terminal sequence of this enzyme. Analyses of the nucleotide sequences of the cloned cDNA inserts revealed a 759-base-pair open reading frame that encoded a 253-amino acid polypeptide with a Mr of 27,089 and NH2-terminal and internal sequences identical with those of the (S)-H4Ber oxidase, as determined by microsequencing methods. Escherichia coli were transformed with an expression vector carrying (S)-H4Ber oxidase cDNA. The transformed bacteria were induced to overproduce a 28-kDa protein that reacted with Coptis (S)-H4Ber oxidase-specific antibody. A comparison of the derived amino acid sequence of (S)-H4Ber oxidase with sequences in the protein data base of the Protein Research Foundation showed a marked similarity between (S)-H4Ber oxidase and the NH2-terminal portion of mouse P1-450, which is encoded by a single exon of the mouse P1-450 gene. The availability of cloned cDNA for (S)-H4Ber oxidase allows use of the methods of molecular biology to study the regulation of (S)-H4Ber oxidase gene expression in cultured C. japonica cells in relation to berberine biosynthesis.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.86.2.534</identifier><identifier>PMID: 2463630</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>ACIDE AMINE ; ADN ; Amino Acid Sequence ; AMINO ACIDS ; AMINOACIDOS ; Antibodies ; Base Sequence ; Berberine - biosynthesis ; Berberine Alkaloids - biosynthesis ; Biological and medical sciences ; Biotechnology ; Blotting, Western ; CELL CULTURE ; Cell culture techniques ; Cells, Cultured ; Chromatography, High Pressure Liquid ; CLONACION ; CLONAGE ; CLONING ; Complementary DNA ; Coptis japonica ; CULTIVO DE CELULAS ; CULTURE DE CELLULES ; Cultured cells ; CYTOCHROMES ; DNA ; DNA - genetics ; Electrophoresis, Polyacrylamide Gel ; Enzymes ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; gene expression ; Gene Expression Regulation ; Genetic engineering ; Genetic technics ; GENETICA ; GENETICS ; GENETIQUE ; Messenger RNA ; METABOLITE ; METABOLITES ; METABOLITOS ; METALLOPROTEINE ; METALLOPROTEINS ; METALPROTEINAS ; Methods. Procedures. Technologies ; Molecular cloning ; Molecular Sequence Data ; Nucleic Acid Hybridization ; NUCLEOTIDE ; Nucleotide sequences ; NUCLEOTIDES ; NUCLEOTIDOS ; Oxidases ; OXIDOREDUCTASES ; Oxidoreductases - biosynthesis ; Oxidoreductases - genetics ; Oxidoreductases Acting on CH-CH Group Donors ; OXIDORREDUCTASAS ; OXYDOREDUCTASE ; Plants ; Plasmids ; PROTEINAS ; PROTEINE ; PROTEINS ; RANUNCULACEAE ; Restriction Mapping ; RNA - genetics</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1989-01, Vol.86 (2), p.534-538</ispartof><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c596t-dc36942e27d5d6d0aa8fb57f78bcf4272ed96ab4c9d13a4b6793996e72bc2753</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/86/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/33159$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/33159$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7114806$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2463630$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okada, N</creatorcontrib><creatorcontrib>Koizumi, N</creatorcontrib><creatorcontrib>Tanaka, T</creatorcontrib><creatorcontrib>Ohkubo, H</creatorcontrib><creatorcontrib>Nakanishi, S</creatorcontrib><creatorcontrib>Yamada, Y</creatorcontrib><title>Isolation, sequence, and bacterial expression of a cDNA for (S)-tetrahydroberberine oxidase from cultured berberine-producing Coptis japonica cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>cDNA clones for the (S)-tetrahydroberberine (H4Ber) oxidase of cultured berberine-producing Coptis japonica cells were isolated by screening a C. japonica cDNA library with synthetic nucleotides that can encode the NH2-terminal sequence of this enzyme. Analyses of the nucleotide sequences of the cloned cDNA inserts revealed a 759-base-pair open reading frame that encoded a 253-amino acid polypeptide with a Mr of 27,089 and NH2-terminal and internal sequences identical with those of the (S)-H4Ber oxidase, as determined by microsequencing methods. Escherichia coli were transformed with an expression vector carrying (S)-H4Ber oxidase cDNA. The transformed bacteria were induced to overproduce a 28-kDa protein that reacted with Coptis (S)-H4Ber oxidase-specific antibody. A comparison of the derived amino acid sequence of (S)-H4Ber oxidase with sequences in the protein data base of the Protein Research Foundation showed a marked similarity between (S)-H4Ber oxidase and the NH2-terminal portion of mouse P1-450, which is encoded by a single exon of the mouse P1-450 gene. The availability of cloned cDNA for (S)-H4Ber oxidase allows use of the methods of molecular biology to study the regulation of (S)-H4Ber oxidase gene expression in cultured C. japonica cells in relation to berberine biosynthesis.</description><subject>ACIDE AMINE</subject><subject>ADN</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACIDS</subject><subject>AMINOACIDOS</subject><subject>Antibodies</subject><subject>Base Sequence</subject><subject>Berberine - biosynthesis</subject><subject>Berberine Alkaloids - biosynthesis</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Blotting, Western</subject><subject>CELL CULTURE</subject><subject>Cell culture techniques</subject><subject>Cells, Cultured</subject><subject>Chromatography, High Pressure Liquid</subject><subject>CLONACION</subject><subject>CLONAGE</subject><subject>CLONING</subject><subject>Complementary DNA</subject><subject>Coptis japonica</subject><subject>CULTIVO DE CELULAS</subject><subject>CULTURE DE CELLULES</subject><subject>Cultured cells</subject><subject>CYTOCHROMES</subject><subject>DNA</subject><subject>DNA - genetics</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene expression</subject><subject>Gene Expression Regulation</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>GENETICA</subject><subject>GENETICS</subject><subject>GENETIQUE</subject><subject>Messenger RNA</subject><subject>METABOLITE</subject><subject>METABOLITES</subject><subject>METABOLITOS</subject><subject>METALLOPROTEINE</subject><subject>METALLOPROTEINS</subject><subject>METALPROTEINAS</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular cloning</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Hybridization</subject><subject>NUCLEOTIDE</subject><subject>Nucleotide sequences</subject><subject>NUCLEOTIDES</subject><subject>NUCLEOTIDOS</subject><subject>Oxidases</subject><subject>OXIDOREDUCTASES</subject><subject>Oxidoreductases - biosynthesis</subject><subject>Oxidoreductases - genetics</subject><subject>Oxidoreductases Acting on CH-CH Group Donors</subject><subject>OXIDORREDUCTASAS</subject><subject>OXYDOREDUCTASE</subject><subject>Plants</subject><subject>Plasmids</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>RANUNCULACEAE</subject><subject>Restriction Mapping</subject><subject>RNA - genetics</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhSMEKkNhyQaB5AUgkJrBdmI7XrCohr9KFSxa1taNY089ysSp7aDpc_DCeJjpUDYgWfLifPf4Hp-ieErwnGBRvRsHiPOGz-mcVfW9YkawJCWvJb5fzDCmomxqWj8sHsW4whhL1uCj4ojWvOIVnhU_z6LvITk_nKBoriczaHOCYOhQCzqZ4KBHZjMGE2NmkLcIkP7w9RRZH9Cbi7dlMinA1U0XfGtCPm4wyG9cB9EgG_wa6alPUzDZ8FYvx-C7SbthiRZ-TC6iFYx-cDpbm76Pj4sHFvponuzv4-Ly08fLxZfy_Nvns8XpeamZ5KnsdMVlTQ0VHet4hwEa2zJhRdNqW1NBTSc5tLWWHamgbrmQlZTcCNpqKlh1XLzf2Y5TuzadNkNO0qsxuDWEG-XBqb-VwV2ppf-haMMZ5nn-9X4--PxxMam1i9sAMBg_RSWahgpO2X9BwiglmNUZLHegDj7GYOxhGYLVtmy1LVs1XFGVy878i7sJDvS-3ay_3OsQNfQ2wKBdPGCCkLr5HeT5Htu636p3Xnn1D1nZqe-T2aTMPdtxq5h8OIBVRZj8I1rwCpYhr_H9opE4JxfVL1Pk3nI</recordid><startdate>19890101</startdate><enddate>19890101</enddate><creator>Okada, N</creator><creator>Koizumi, N</creator><creator>Tanaka, T</creator><creator>Ohkubo, H</creator><creator>Nakanishi, S</creator><creator>Yamada, Y</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19890101</creationdate><title>Isolation, sequence, and bacterial expression of a cDNA for (S)-tetrahydroberberine oxidase from cultured berberine-producing Coptis japonica cells</title><author>Okada, N ; Koizumi, N ; Tanaka, T ; Ohkubo, H ; Nakanishi, S ; Yamada, Y</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c596t-dc36942e27d5d6d0aa8fb57f78bcf4272ed96ab4c9d13a4b6793996e72bc2753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>ACIDE AMINE</topic><topic>ADN</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACIDS</topic><topic>AMINOACIDOS</topic><topic>Antibodies</topic><topic>Base Sequence</topic><topic>Berberine - biosynthesis</topic><topic>Berberine Alkaloids - biosynthesis</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Blotting, Western</topic><topic>CELL CULTURE</topic><topic>Cell culture techniques</topic><topic>Cells, Cultured</topic><topic>Chromatography, High Pressure Liquid</topic><topic>CLONACION</topic><topic>CLONAGE</topic><topic>CLONING</topic><topic>Complementary DNA</topic><topic>Coptis japonica</topic><topic>CULTIVO DE CELULAS</topic><topic>CULTURE DE CELLULES</topic><topic>Cultured cells</topic><topic>CYTOCHROMES</topic><topic>DNA</topic><topic>DNA - genetics</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene expression</topic><topic>Gene Expression Regulation</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>GENETICA</topic><topic>GENETICS</topic><topic>GENETIQUE</topic><topic>Messenger RNA</topic><topic>METABOLITE</topic><topic>METABOLITES</topic><topic>METABOLITOS</topic><topic>METALLOPROTEINE</topic><topic>METALLOPROTEINS</topic><topic>METALPROTEINAS</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular cloning</topic><topic>Molecular Sequence Data</topic><topic>Nucleic Acid Hybridization</topic><topic>NUCLEOTIDE</topic><topic>Nucleotide sequences</topic><topic>NUCLEOTIDES</topic><topic>NUCLEOTIDOS</topic><topic>Oxidases</topic><topic>OXIDOREDUCTASES</topic><topic>Oxidoreductases - biosynthesis</topic><topic>Oxidoreductases - genetics</topic><topic>Oxidoreductases Acting on CH-CH Group Donors</topic><topic>OXIDORREDUCTASAS</topic><topic>OXYDOREDUCTASE</topic><topic>Plants</topic><topic>Plasmids</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>RANUNCULACEAE</topic><topic>Restriction Mapping</topic><topic>RNA - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okada, N</creatorcontrib><creatorcontrib>Koizumi, N</creatorcontrib><creatorcontrib>Tanaka, T</creatorcontrib><creatorcontrib>Ohkubo, H</creatorcontrib><creatorcontrib>Nakanishi, S</creatorcontrib><creatorcontrib>Yamada, Y</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Okada, N</au><au>Koizumi, N</au><au>Tanaka, T</au><au>Ohkubo, H</au><au>Nakanishi, S</au><au>Yamada, Y</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation, sequence, and bacterial expression of a cDNA for (S)-tetrahydroberberine oxidase from cultured berberine-producing Coptis japonica cells</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1989-01-01</date><risdate>1989</risdate><volume>86</volume><issue>2</issue><spage>534</spage><epage>538</epage><pages>534-538</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>cDNA clones for the (S)-tetrahydroberberine (H4Ber) oxidase of cultured berberine-producing Coptis japonica cells were isolated by screening a C. japonica cDNA library with synthetic nucleotides that can encode the NH2-terminal sequence of this enzyme. Analyses of the nucleotide sequences of the cloned cDNA inserts revealed a 759-base-pair open reading frame that encoded a 253-amino acid polypeptide with a Mr of 27,089 and NH2-terminal and internal sequences identical with those of the (S)-H4Ber oxidase, as determined by microsequencing methods. Escherichia coli were transformed with an expression vector carrying (S)-H4Ber oxidase cDNA. The transformed bacteria were induced to overproduce a 28-kDa protein that reacted with Coptis (S)-H4Ber oxidase-specific antibody. A comparison of the derived amino acid sequence of (S)-H4Ber oxidase with sequences in the protein data base of the Protein Research Foundation showed a marked similarity between (S)-H4Ber oxidase and the NH2-terminal portion of mouse P1-450, which is encoded by a single exon of the mouse P1-450 gene. The availability of cloned cDNA for (S)-H4Ber oxidase allows use of the methods of molecular biology to study the regulation of (S)-H4Ber oxidase gene expression in cultured C. japonica cells in relation to berberine biosynthesis.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2463630</pmid><doi>10.1073/pnas.86.2.534</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1989-01, Vol.86 (2), p.534-538 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_86_2_534_fulltext |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | ACIDE AMINE ADN Amino Acid Sequence AMINO ACIDS AMINOACIDOS Antibodies Base Sequence Berberine - biosynthesis Berberine Alkaloids - biosynthesis Biological and medical sciences Biotechnology Blotting, Western CELL CULTURE Cell culture techniques Cells, Cultured Chromatography, High Pressure Liquid CLONACION CLONAGE CLONING Complementary DNA Coptis japonica CULTIVO DE CELULAS CULTURE DE CELLULES Cultured cells CYTOCHROMES DNA DNA - genetics Electrophoresis, Polyacrylamide Gel Enzymes Escherichia coli - genetics Fundamental and applied biological sciences. Psychology gene expression Gene Expression Regulation Genetic engineering Genetic technics GENETICA GENETICS GENETIQUE Messenger RNA METABOLITE METABOLITES METABOLITOS METALLOPROTEINE METALLOPROTEINS METALPROTEINAS Methods. Procedures. Technologies Molecular cloning Molecular Sequence Data Nucleic Acid Hybridization NUCLEOTIDE Nucleotide sequences NUCLEOTIDES NUCLEOTIDOS Oxidases OXIDOREDUCTASES Oxidoreductases - biosynthesis Oxidoreductases - genetics Oxidoreductases Acting on CH-CH Group Donors OXIDORREDUCTASAS OXYDOREDUCTASE Plants Plasmids PROTEINAS PROTEINE PROTEINS RANUNCULACEAE Restriction Mapping RNA - genetics |
| title | Isolation, sequence, and bacterial expression of a cDNA for (S)-tetrahydroberberine oxidase from cultured berberine-producing Coptis japonica cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T00%3A25%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pnas_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Isolation,%20sequence,%20and%20bacterial%20expression%20of%20a%20cDNA%20for%20(S)-tetrahydroberberine%20oxidase%20from%20cultured%20berberine-producing%20Coptis%20japonica%20cells&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Okada,%20N&rft.date=1989-01-01&rft.volume=86&rft.issue=2&rft.spage=534&rft.epage=538&rft.pages=534-538&rft.issn=0027-8424&rft.eissn=1091-6490&rft.coden=PNASA6&rft_id=info:doi/10.1073/pnas.86.2.534&rft_dat=%3Cjstor_pnas_%3E33159%3C/jstor_pnas_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15221054&rft_id=info:pmid/2463630&rft_jstor_id=33159&rfr_iscdi=true |