Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts
Identifieur interne : 001B44 ( Istex/Corpus ); précédent : 001B43; suivant : 001B45Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts
Auteurs : F. Rebeille ; M. D. HatchSource :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1986.
English descriptors
- KwdEn :
- Chloroplast, Dehydrogenase, Dhap, Electron flux, Enzyme activity, Ferredoxin, Final concentrations, Intact chloroplasts, Light intensity, Maize, Mesophyll, Mesophyll chloroplasts, Nadp, Nadp ratio, Nadph, Nadph concentration, Nadpmdh, Oxidized, Oxidized thioredoxin, Photosynthesis, Photosynthetic metabolites, Redox, Redox state, Reduceable, Reduceable substrates, Thioredoxin, Thioredoxin content, Thioredoxin redox state, Total amount.
- Teeft :
- Chloroplast, Dehydrogenase, Dhap, Electron flux, Enzyme activity, Ferredoxin, Final concentrations, Intact chloroplasts, Light intensity, Maize, Mesophyll, Mesophyll chloroplasts, Nadp, Nadp ratio, Nadph, Nadph concentration, Nadpmdh, Oxidized, Oxidized thioredoxin, Photosynthesis, Photosynthetic metabolites, Redox, Redox state, Reduceable, Reduceable substrates, Thioredoxin, Thioredoxin content, Thioredoxin redox state, Total amount.
Abstract
Abstract: NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in Zea mays chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of pyridine nucleotide as NADPH increased from about 25 to 90%, and the proportion of thioredoxin in the reduced form increased from 20 to more than 90%, in less than 1 min. After transfer back to the dark, NADPH levels dropped very rapidly to the initial values recorded before illumination, while enzyme activity and reduced thioredoxin levels decreased more slowly. Addition of oxaloacetate or 3-phosphoglyerate to illuminated chloroplasts results in a decrease of about 70% in the activity of NADP-malate dehydrogenase, a 30% decrease in the level of NADPH, and a 25% decrease in the reduced thioredoxin content. Adding dihydroxyacetone phosphate and pyruvate had no effect. These results are considered in relation to the hypothesis that NADP-malate dehydrogenase activity in chloroplasts may be determined by factors regulating the ratio of NADPH to NADP as well as those influencing the redox state of thioredoxin.
Url:
DOI: 10.1016/0003-9861(86)90572-2
Links to Exploration step
ISTEX:90E866557803B321AE5B1B97A60F5B24F7952018Le document en format XML
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Hatch</name><affiliation><mods:affiliation>Division of Plant Industry, CSIRO, GPO Box 1600, Canberra City, ACT 2601, Australia</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986">1986</date><biblScope unit="volume">249</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="171">171</biblScope><biblScope unit="page" to="179">179</biblScope></imprint><idno type="ISSN">0003-9861</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chloroplast</term><term>Dehydrogenase</term><term>Dhap</term><term>Electron flux</term><term>Enzyme activity</term><term>Ferredoxin</term><term>Final concentrations</term><term>Intact chloroplasts</term><term>Light intensity</term><term>Maize</term><term>Mesophyll</term><term>Mesophyll chloroplasts</term><term>Nadp</term><term>Nadp ratio</term><term>Nadph</term><term>Nadph concentration</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Photosynthesis</term><term>Photosynthetic metabolites</term><term>Redox</term><term>Redox state</term><term>Reduceable</term><term>Reduceable substrates</term><term>Thioredoxin</term><term>Thioredoxin content</term><term>Thioredoxin redox state</term><term>Total amount</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Chloroplast</term><term>Dehydrogenase</term><term>Dhap</term><term>Electron flux</term><term>Enzyme activity</term><term>Ferredoxin</term><term>Final concentrations</term><term>Intact chloroplasts</term><term>Light intensity</term><term>Maize</term><term>Mesophyll</term><term>Mesophyll chloroplasts</term><term>Nadp</term><term>Nadp ratio</term><term>Nadph</term><term>Nadph concentration</term><term>Nadpmdh</term><term>Oxidized</term><term>Oxidized thioredoxin</term><term>Photosynthesis</term><term>Photosynthetic metabolites</term><term>Redox</term><term>Redox state</term><term>Reduceable</term><term>Reduceable substrates</term><term>Thioredoxin</term><term>Thioredoxin content</term><term>Thioredoxin redox state</term><term>Total amount</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in Zea mays chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of pyridine nucleotide as NADPH increased from about 25 to 90%, and the proportion of thioredoxin in the reduced form increased from 20 to more than 90%, in less than 1 min. After transfer back to the dark, NADPH levels dropped very rapidly to the initial values recorded before illumination, while enzyme activity and reduced thioredoxin levels decreased more slowly. Addition of oxaloacetate or 3-phosphoglyerate to illuminated chloroplasts results in a decrease of about 70% in the activity of NADP-malate dehydrogenase, a 30% decrease in the level of NADPH, and a 25% decrease in the reduced thioredoxin content. Adding dihydroxyacetone phosphate and pyruvate had no effect. These results are considered in relation to the hypothesis that NADP-malate dehydrogenase activity in chloroplasts may be determined by factors regulating the ratio of NADPH to NADP as well as those influencing the redox state of thioredoxin.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>chloroplast</json:string><json:string>nadp</json:string><json:string>thioredoxin</json:string><json:string>nadph</json:string><json:string>redox</json:string><json:string>ferredoxin</json:string><json:string>dehydrogenase</json:string><json:string>maize</json:string><json:string>redox state</json:string><json:string>nadp ratio</json:string><json:string>reduceable</json:string><json:string>photosynthesis</json:string><json:string>oxidized</json:string><json:string>intact chloroplasts</json:string><json:string>reduceable substrates</json:string><json:string>nadpmdh</json:string><json:string>dhap</json:string><json:string>mesophyll</json:string><json:string>enzyme activity</json:string><json:string>oxidized thioredoxin</json:string><json:string>thioredoxin redox state</json:string><json:string>light intensity</json:string><json:string>total amount</json:string><json:string>mesophyll chloroplasts</json:string><json:string>photosynthetic metabolites</json:string><json:string>final concentrations</json:string><json:string>nadph concentration</json:string><json:string>thioredoxin content</json:string><json:string>electron flux</json:string></teeft></keywords><subject><json:item><lang><json:string>eng</json:string></lang><value>Plant molecular biology, biochemistry, and photosynthesis</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>185</abstractWordCount><abstractCharCount>1222</abstractCharCount><keywordCount>1</keywordCount><score>7.525</score><pdfWordCount>3305</pdfWordCount><pdfCharCount>25633</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>9</pdfPageCount><pdfPageSize>504 x 720 pts</pdfPageSize></qualityIndicators><title>Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts</title><pii><json:string>0003-9861(86)90572-2</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Archives of Biochemistry and Biophysics</title><language><json:string>unknown</json:string></language><publicationDate>1986</publicationDate><issn><json:string>0003-9861</json:string></issn><pii><json:string>S0003-9861(00)X0420-1</json:string></pii><volume>249</volume><issue>1</issue><pages><first>171</first><last>179</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1986</json:string></date><geogName></geogName><orgName><json:string>Sigma Chemical Company</json:string><json:string>Biochem</json:string><json:string>Division of Plant Industry</json:string><json:string>Academic Press, Inc.</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>M. 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Rebeille</name><affiliations><json:string>Departement de Biologie, Service de Radioagronomie, CEN-Cadarache, BP No. 1, 13115 St. Paul lez Durance, France</json:string></affiliations></json:item><json:item><name>M.D. Hatch</name><affiliations><json:string>Division of Plant Industry, CSIRO, GPO Box 1600, Canberra City, ACT 2601, Australia</json:string></affiliations></json:item></author><articleId><json:string>86905722</json:string></articleId><arkIstex>ark:/67375/6H6-CXZHZPW5-T</arkIstex><abstract>Abstract: NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in Zea mays chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of pyridine nucleotide as NADPH increased from about 25 to 90%, and the proportion of thioredoxin in the reduced form increased from 20 to more than 90%, in less than 1 min. After transfer back to the dark, NADPH levels dropped very rapidly to the initial values recorded before illumination, while enzyme activity and reduced thioredoxin levels decreased more slowly. Addition of oxaloacetate or 3-phosphoglyerate to illuminated chloroplasts results in a decrease of about 70% in the activity of NADP-malate dehydrogenase, a 30% decrease in the level of NADPH, and a 25% decrease in the reduced thioredoxin content. Adding dihydroxyacetone phosphate and pyruvate had no effect. These results are considered in relation to the hypothesis that NADP-malate dehydrogenase activity in chloroplasts may be determined by factors regulating the ratio of NADPH to NADP as well as those influencing the redox state of thioredoxin.</abstract><pmid><json:string>3740850</json:string></pmid><serie><title>New Series</title><language><json:string>unknown</json:string></language></serie><copyrightDate>1986</copyrightDate><doi><json:string>10.1016/0003-9861(86)90572-2</json:string></doi><id>90E866557803B321AE5B1B97A60F5B24F7952018</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1986</date></publicationStmt><notesStmt><note>This work was carried out in the Division of Plant Industry, CSIRO, Canberra, Australia.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts</title><author xml:id="author-0000"><persName><forename type="first">F.</forename><surname>Rebeille</surname></persName><affiliation>Departement de Biologie, Service de Radioagronomie, CEN-Cadarache, BP No. 1, 13115 St. Paul lez Durance, France</affiliation></author><author xml:id="author-0001"><persName><forename type="first">M.D.</forename><surname>Hatch</surname></persName><affiliation>Division of Plant Industry, CSIRO, GPO Box 1600, Canberra City, ACT 2601, Australia</affiliation></author><idno type="istex">90E866557803B321AE5B1B97A60F5B24F7952018</idno><idno type="DOI">10.1016/0003-9861(86)90572-2</idno><idno type="PII">0003-9861(86)90572-2</idno><idno type="ArticleID">86905722</idno></analytic><monogr><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="pISSN">0003-9861</idno><idno type="PII">S0003-9861(00)X0420-1</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1986"></date><biblScope unit="volume">249</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="171">171</biblScope><biblScope unit="page" to="179">179</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1986</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in Zea mays chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of pyridine nucleotide as NADPH increased from about 25 to 90%, and the proportion of thioredoxin in the reduced form increased from 20 to more than 90%, in less than 1 min. After transfer back to the dark, NADPH levels dropped very rapidly to the initial values recorded before illumination, while enzyme activity and reduced thioredoxin levels decreased more slowly. Addition of oxaloacetate or 3-phosphoglyerate to illuminated chloroplasts results in a decrease of about 70% in the activity of NADP-malate dehydrogenase, a 30% decrease in the level of NADPH, and a 25% decrease in the reduced thioredoxin content. Adding dihydroxyacetone phosphate and pyruvate had no effect. These results are considered in relation to the hypothesis that NADP-malate dehydrogenase activity in chloroplasts may be determined by factors regulating the ratio of NADPH to NADP as well as those influencing the redox state of thioredoxin.</p></abstract><textClass><keywords scheme="keyword"><list><head>article-category</head><item><term>Plant molecular biology, biochemistry, and photosynthesis</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1986-04-17">Modified</change><change when="1986">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YABBI</jid><aid>86905722</aid><ce:pii>0003-9861(86)90572-2</ce:pii><ce:doi>10.1016/0003-9861(86)90572-2</ce:doi><ce:copyright type="unknown" year="1986"></ce:copyright><ce:doctopics><ce:doctopic><ce:text>Plant molecular biology, biochemistry, and photosynthesis</ce:text></ce:doctopic></ce:doctopics></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was carried out in the Division of Plant Industry, CSIRO, Canberra, Australia.</ce:note-para></ce:article-footnote><ce:title>Regulation of NADP-malate dehydrogenase in C<ce:inf loc="post">4</ce:inf> plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts</ce:title><ce:author-group><ce:author><ce:given-name>F.</ce:given-name><ce:surname>Rebeille</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>M.D.</ce:given-name><ce:surname>Hatch</ce:surname><ce:cross-ref refid="AFF2"><ce:sup loc="post">†</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>∗</ce:label><ce:textfn>Departement de Biologie, Service de Radioagronomie, CEN-Cadarache, BP No. 1, 13115 St. Paul lez Durance, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>†</ce:label><ce:textfn>Division of Plant Industry, CSIRO, GPO Box 1600, Canberra City, ACT 2601, Australia</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="23" month="1" year="1986"></ce:date-received><ce:date-revised day="17" month="4" year="1986"></ce:date-revised><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0010">NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in <ce:italic>Zea mays</ce:italic> chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of pyridine nucleotide as NADPH increased from about 25 to 90%, and the proportion of thioredoxin in the reduced form increased from 20 to more than 90%, in less than 1 min. After transfer back to the dark, NADPH levels dropped very rapidly to the initial values recorded before illumination, while enzyme activity and reduced thioredoxin levels decreased more slowly. Addition of oxaloacetate or 3-phosphoglyerate to illuminated chloroplasts results in a decrease of about 70% in the activity of NADP-malate dehydrogenase, a 30% decrease in the level of NADPH, and a 25% decrease in the reduced thioredoxin content. Adding dihydroxyacetone phosphate and pyruvate had no effect. These results are considered in relation to the hypothesis that NADP-malate dehydrogenase activity in chloroplasts may be determined by factors regulating the ratio of NADPH to NADP as well as those influencing the redox state of thioredoxin.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Regulation of NADP-malate dehydrogenase in C4 plants: Relationship among enzyme activity, NADPH to NADP ratios, and thioredoxin redox states in intact maize mesophyll chloroplasts</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Regulation of NADP-malate dehydrogenase in C</title></titleInfo><name type="personal"><namePart type="given">F.</namePart><namePart type="family">Rebeille</namePart><affiliation>Departement de Biologie, Service de Radioagronomie, CEN-Cadarache, BP No. 1, 13115 St. Paul lez Durance, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.D.</namePart><namePart type="family">Hatch</namePart><affiliation>Division of Plant Industry, CSIRO, GPO Box 1600, Canberra City, ACT 2601, Australia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1986</dateIssued><dateModified encoding="w3cdtf">1986-04-17</dateModified><copyrightDate encoding="w3cdtf">1986</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: NADP-malate dehydrogenase activity, the ratio of NADPH to NADP, and thioredoxin redox state in Zea mays chloroplasts were determined after various treatments. Following transfer from dark to light, NADP-malate dehydrogenase was activated more than 20-fold within 10 min while the proportion of pyridine nucleotide as NADPH increased from about 25 to 90%, and the proportion of thioredoxin in the reduced form increased from 20 to more than 90%, in less than 1 min. After transfer back to the dark, NADPH levels dropped very rapidly to the initial values recorded before illumination, while enzyme activity and reduced thioredoxin levels decreased more slowly. Addition of oxaloacetate or 3-phosphoglyerate to illuminated chloroplasts results in a decrease of about 70% in the activity of NADP-malate dehydrogenase, a 30% decrease in the level of NADPH, and a 25% decrease in the reduced thioredoxin content. Adding dihydroxyacetone phosphate and pyruvate had no effect. These results are considered in relation to the hypothesis that NADP-malate dehydrogenase activity in chloroplasts may be determined by factors regulating the ratio of NADPH to NADP as well as those influencing the redox state of thioredoxin.</abstract><note>This work was carried out in the Division of Plant Industry, CSIRO, Canberra, Australia.</note><subject><genre>article-category</genre><topic>Plant molecular biology, biochemistry, and photosynthesis</topic></subject><relatedItem type="host"><titleInfo><title>Archives of Biochemistry and Biophysics</title></titleInfo><titleInfo type="abbreviated"><title>YABBI</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">19860815</dateIssued></originInfo><identifier type="ISSN">0003-9861</identifier><identifier type="PII">S0003-9861(00)X0420-1</identifier><part><date>19860815</date><detail type="volume"><number>249</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>253</end></extent><extent unit="pages"><start>171</start><end>179</end></extent></part></relatedItem><identifier type="istex">90E866557803B321AE5B1B97A60F5B24F7952018</identifier><identifier type="ark">ark:/67375/6H6-CXZHZPW5-T</identifier><identifier type="DOI">10.1016/0003-9861(86)90572-2</identifier><identifier type="PII">0003-9861(86)90572-2</identifier><identifier type="ArticleID">86905722</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/90E866557803B321AE5B1B97A60F5B24F7952018/metadata/json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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