Characteristics of purified protoporphyrinogen oxidase from barley
The membrane bound enzyme oxidizing protoporphyrinogen to protoporphyrin, a step in heme and chlorophyll synthesis, was purified to a single prominent polypeptide band on SDS/PAGE from barley mitochondrial fractions. It contained a variety of lipids including 0.66 mg of phosphatidyl ethanolamine and...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1989-06, Vol.161 (2), p.790-796 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 796 |
|---|---|
| container_issue | 2 |
| container_start_page | 790 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 161 |
| creator | Jacobs, Nicholas J. Borotz, Susan E. Jacobs, Judith M. |
| description | The membrane bound enzyme oxidizing protoporphyrinogen to protoporphyrin, a step in heme and chlorophyll synthesis, was purified to a single prominent polypeptide band on SDS/PAGE from barley mitochondrial fractions. It contained a variety of lipids including 0.66 mg of phosphatidyl ethanolamine and 0.46 mg of free fatty acid per mg of protein. Iron, but no flavins or cytochromes, was detected. In the presence of glutathione, enzymatic oxidation was inhibited by the iron chelator o-phenanthroline but was stimulated by iron EDTA. The purified enzyme was inhibited by reductants such as glutathione, ascorbate, NADH and NADPH. These findings are compatible with some direct or indirect involvement of lipids and iron in this oxidation in plants. |
| doi_str_mv | 10.1016/0006-291X(89)92669-7 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79026429</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006291X89926697</els_id><sourcerecordid>15308315</sourcerecordid><originalsourceid>FETCH-LOGICAL-c482t-28441474d0b28e6dd3469db0db07737805398ad3d3e35d7c0bd48bf8711ce7643</originalsourceid><addsrcrecordid>eNqFkUtr3DAUhUVoSSeT_IHQgBeltAunV4-xpE2hHfqCQBdtIDshS9eJgsdyJU_p_PvInWGWLQhpcc499_CJkJcUrinQ5h0ANDXT9O6N0m81axpdyxOyoKChZhTEM7I4Wl6Qs5wfASgVjT4lp0zylWZ8QT6uH2yybsIU8hRcrmJXjdsUuoC-GlOc4hjT-LBLYYj3OFTxT_A2Y9WluKlam3rcnZPnne0zXhzeJbn9_Onn-mt98_3Lt_WHm9oJxaaaKSGokMJDyxQ23vNSxbdQjpRcKlhxraznniNfeemg9UK1nZKUOpSN4Evyep9bav3aYp7MJmSHfW8HjNtspAbWCKb_a6QrDoqXe0nE3uhSzDlhZ8YUNjbtDAUzMzYzQDMDNEqbv4yNLGNXh_xtu0F_HDpALfqrg26zs32X7OBCPtokUyVp3n65t3U2GntfPsDc_lCac0bnHe_3IhaivwMmk13AwaEPCd1kfAz_LvkE9gegAw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15308315</pqid></control><display><type>article</type><title>Characteristics of purified protoporphyrinogen oxidase from barley</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Jacobs, Nicholas J. ; Borotz, Susan E. ; Jacobs, Judith M.</creator><creatorcontrib>Jacobs, Nicholas J. ; Borotz, Susan E. ; Jacobs, Judith M.</creatorcontrib><description>The membrane bound enzyme oxidizing protoporphyrinogen to protoporphyrin, a step in heme and chlorophyll synthesis, was purified to a single prominent polypeptide band on SDS/PAGE from barley mitochondrial fractions. It contained a variety of lipids including 0.66 mg of phosphatidyl ethanolamine and 0.46 mg of free fatty acid per mg of protein. Iron, but no flavins or cytochromes, was detected. In the presence of glutathione, enzymatic oxidation was inhibited by the iron chelator o-phenanthroline but was stimulated by iron EDTA. The purified enzyme was inhibited by reductants such as glutathione, ascorbate, NADH and NADPH. These findings are compatible with some direct or indirect involvement of lipids and iron in this oxidation in plants.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(89)92669-7</identifier><identifier>PMID: 2735923</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Chelating Agents - pharmacology ; Cytochromes - analysis ; Edible Grain - enzymology ; Enzymes and enzyme inhibitors ; ENZYMIC ACTIVITY ; Flavins - analysis ; Fundamental and applied biological sciences. Psychology ; Glutathione - pharmacology ; Hordeum - enzymology ; HORDEUM VULGARE ; Iron - analysis ; Mitochondria - analysis ; NADH ; NADPH ; NUCLEOTIDE ; NUCLEOTIDES ; NUCLEOTIDOS ; Oxidation-Reduction ; OXIDOREDUCTASES ; Oxidoreductases - isolation & purification ; Oxidoreductases Acting on CH-CH Group Donors ; OXIDORREDUCTASAS ; OXYDOREDUCTASE ; Phospholipids - analysis ; Protoporphyrinogen Oxidase</subject><ispartof>Biochemical and biophysical research communications, 1989-06, Vol.161 (2), p.790-796</ispartof><rights>1989</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-28441474d0b28e6dd3469db0db07737805398ad3d3e35d7c0bd48bf8711ce7643</citedby><cites>FETCH-LOGICAL-c482t-28441474d0b28e6dd3469db0db07737805398ad3d3e35d7c0bd48bf8711ce7643</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X89926697$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7289265$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2735923$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jacobs, Nicholas J.</creatorcontrib><creatorcontrib>Borotz, Susan E.</creatorcontrib><creatorcontrib>Jacobs, Judith M.</creatorcontrib><title>Characteristics of purified protoporphyrinogen oxidase from barley</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The membrane bound enzyme oxidizing protoporphyrinogen to protoporphyrin, a step in heme and chlorophyll synthesis, was purified to a single prominent polypeptide band on SDS/PAGE from barley mitochondrial fractions. It contained a variety of lipids including 0.66 mg of phosphatidyl ethanolamine and 0.46 mg of free fatty acid per mg of protein. Iron, but no flavins or cytochromes, was detected. In the presence of glutathione, enzymatic oxidation was inhibited by the iron chelator o-phenanthroline but was stimulated by iron EDTA. The purified enzyme was inhibited by reductants such as glutathione, ascorbate, NADH and NADPH. These findings are compatible with some direct or indirect involvement of lipids and iron in this oxidation in plants.</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chelating Agents - pharmacology</subject><subject>Cytochromes - analysis</subject><subject>Edible Grain - enzymology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ENZYMIC ACTIVITY</subject><subject>Flavins - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glutathione - pharmacology</subject><subject>Hordeum - enzymology</subject><subject>HORDEUM VULGARE</subject><subject>Iron - analysis</subject><subject>Mitochondria - analysis</subject><subject>NADH</subject><subject>NADPH</subject><subject>NUCLEOTIDE</subject><subject>NUCLEOTIDES</subject><subject>NUCLEOTIDOS</subject><subject>Oxidation-Reduction</subject><subject>OXIDOREDUCTASES</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Oxidoreductases Acting on CH-CH Group Donors</subject><subject>OXIDORREDUCTASAS</subject><subject>OXYDOREDUCTASE</subject><subject>Phospholipids - analysis</subject><subject>Protoporphyrinogen Oxidase</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtr3DAUhUVoSSeT_IHQgBeltAunV4-xpE2hHfqCQBdtIDshS9eJgsdyJU_p_PvInWGWLQhpcc499_CJkJcUrinQ5h0ANDXT9O6N0m81axpdyxOyoKChZhTEM7I4Wl6Qs5wfASgVjT4lp0zylWZ8QT6uH2yybsIU8hRcrmJXjdsUuoC-GlOc4hjT-LBLYYj3OFTxT_A2Y9WluKlam3rcnZPnne0zXhzeJbn9_Onn-mt98_3Lt_WHm9oJxaaaKSGokMJDyxQ23vNSxbdQjpRcKlhxraznniNfeemg9UK1nZKUOpSN4Evyep9bav3aYp7MJmSHfW8HjNtspAbWCKb_a6QrDoqXe0nE3uhSzDlhZ8YUNjbtDAUzMzYzQDMDNEqbv4yNLGNXh_xtu0F_HDpALfqrg26zs32X7OBCPtokUyVp3n65t3U2GntfPsDc_lCac0bnHe_3IhaivwMmk13AwaEPCd1kfAz_LvkE9gegAw</recordid><startdate>19890615</startdate><enddate>19890615</enddate><creator>Jacobs, Nicholas J.</creator><creator>Borotz, Susan E.</creator><creator>Jacobs, Judith M.</creator><general>Elsevier Inc</general><general>Elsevier</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890615</creationdate><title>Characteristics of purified protoporphyrinogen oxidase from barley</title><author>Jacobs, Nicholas J. ; Borotz, Susan E. ; Jacobs, Judith M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-28441474d0b28e6dd3469db0db07737805398ad3d3e35d7c0bd48bf8711ce7643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chelating Agents - pharmacology</topic><topic>Cytochromes - analysis</topic><topic>Edible Grain - enzymology</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ENZYMIC ACTIVITY</topic><topic>Flavins - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glutathione - pharmacology</topic><topic>Hordeum - enzymology</topic><topic>HORDEUM VULGARE</topic><topic>Iron - analysis</topic><topic>Mitochondria - analysis</topic><topic>NADH</topic><topic>NADPH</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDES</topic><topic>NUCLEOTIDOS</topic><topic>Oxidation-Reduction</topic><topic>OXIDOREDUCTASES</topic><topic>Oxidoreductases - isolation & purification</topic><topic>Oxidoreductases Acting on CH-CH Group Donors</topic><topic>OXIDORREDUCTASAS</topic><topic>OXYDOREDUCTASE</topic><topic>Phospholipids - analysis</topic><topic>Protoporphyrinogen Oxidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jacobs, Nicholas J.</creatorcontrib><creatorcontrib>Borotz, Susan E.</creatorcontrib><creatorcontrib>Jacobs, Judith M.</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>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>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jacobs, Nicholas J.</au><au>Borotz, Susan E.</au><au>Jacobs, Judith M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characteristics of purified protoporphyrinogen oxidase from barley</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1989-06-15</date><risdate>1989</risdate><volume>161</volume><issue>2</issue><spage>790</spage><epage>796</epage><pages>790-796</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The membrane bound enzyme oxidizing protoporphyrinogen to protoporphyrin, a step in heme and chlorophyll synthesis, was purified to a single prominent polypeptide band on SDS/PAGE from barley mitochondrial fractions. It contained a variety of lipids including 0.66 mg of phosphatidyl ethanolamine and 0.46 mg of free fatty acid per mg of protein. Iron, but no flavins or cytochromes, was detected. In the presence of glutathione, enzymatic oxidation was inhibited by the iron chelator o-phenanthroline but was stimulated by iron EDTA. The purified enzyme was inhibited by reductants such as glutathione, ascorbate, NADH and NADPH. These findings are compatible with some direct or indirect involvement of lipids and iron in this oxidation in plants.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2735923</pmid><doi>10.1016/0006-291X(89)92669-7</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1989-06, Vol.161 (2), p.790-796 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79026429 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Analytical, structural and metabolic biochemistry Biological and medical sciences Chelating Agents - pharmacology Cytochromes - analysis Edible Grain - enzymology Enzymes and enzyme inhibitors ENZYMIC ACTIVITY Flavins - analysis Fundamental and applied biological sciences. Psychology Glutathione - pharmacology Hordeum - enzymology HORDEUM VULGARE Iron - analysis Mitochondria - analysis NADH NADPH NUCLEOTIDE NUCLEOTIDES NUCLEOTIDOS Oxidation-Reduction OXIDOREDUCTASES Oxidoreductases - isolation & purification Oxidoreductases Acting on CH-CH Group Donors OXIDORREDUCTASAS OXYDOREDUCTASE Phospholipids - analysis Protoporphyrinogen Oxidase |
| title | Characteristics of purified protoporphyrinogen oxidase from barley |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T19%3A33%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characteristics%20of%20purified%20protoporphyrinogen%20oxidase%20from%20barley&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Jacobs,%20Nicholas%20J.&rft.date=1989-06-15&rft.volume=161&rft.issue=2&rft.spage=790&rft.epage=796&rft.pages=790-796&rft.issn=0006-291X&rft.eissn=1090-2104&rft.coden=BBRCA9&rft_id=info:doi/10.1016/0006-291X(89)92669-7&rft_dat=%3Cproquest_cross%3E15308315%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15308315&rft_id=info:pmid/2735923&rft_els_id=0006291X89926697&rfr_iscdi=true |