Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes
Identifieur interne : 000E10 ( Istex/Corpus ); précédent : 000E09; suivant : 000E11Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes
Auteurs : Martine Torres ; Christian Auclair ; Jacques HakimSource :
- Biochemical and Biophysical Research Communications [ 0006-291X ] ; 1979.
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Abstract
Abstract: The granule rich-fraction isolated from human resting polymorphonuclear leukocytes is capable of CN-insensitive NADH oxidation and O2-uptake, accompanied by production of superoxide anion, hydroxyl radicals and H2O2. We showed that H2O2 initiates and maintains NADH oxidation and O2-uptake but is also necessary for the formation of superoxide anion and hydroxyl radicals. It acts as a primary substrate for CN-insensitive protein-mediated formation of hydroxyl radicals, which in turn produce superoxide anions, probably through univalent oxidation of NADH as an intermediary.
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DOI: 10.1016/0006-291X(79)91508-0
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes</title><author><name sortKey="Torres, Martine" sort="Torres, Martine" uniqKey="Torres M" first="Martine" last="Torres">Martine Torres</name><affiliation><mods:affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</mods:affiliation></affiliation></author><author><name sortKey="Auclair, Christian" sort="Auclair, Christian" uniqKey="Auclair C" first="Christian" last="Auclair">Christian Auclair</name><affiliation><mods:affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</mods:affiliation></affiliation></author><author><name sortKey="Hakim, Jacques" sort="Hakim, Jacques" uniqKey="Hakim J" first="Jacques" last="Hakim">Jacques Hakim</name><affiliation><mods:affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:C6EF34B4FA28C4A2F9A51477198C35601FDCE001</idno><date when="1979" year="1979">1979</date><idno type="doi">10.1016/0006-291X(79)91508-0</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-NWVGCRQS-G/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000E10</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000E10</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes</title><author><name sortKey="Torres, Martine" sort="Torres, Martine" uniqKey="Torres M" first="Martine" last="Torres">Martine Torres</name><affiliation><mods:affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</mods:affiliation></affiliation></author><author><name sortKey="Auclair, Christian" sort="Auclair, Christian" uniqKey="Auclair C" first="Christian" last="Auclair">Christian Auclair</name><affiliation><mods:affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</mods:affiliation></affiliation></author><author><name sortKey="Hakim, Jacques" sort="Hakim, Jacques" uniqKey="Hakim J" first="Jacques" last="Hakim">Jacques Hakim</name><affiliation><mods:affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochemical and Biophysical Research Communications</title><title level="j" type="abbrev">YBBRC</title><idno type="ISSN">0006-291X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1979">1979</date><biblScope unit="volume">88</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="1003">1003</biblScope><biblScope unit="page" to="1009">1009</biblScope></imprint><idno type="ISSN">0006-291X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-291X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>GRF</term><term>H2O2</term><term>HO•</term><term>O2•</term><term>PB</term><term>PMN</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Assay medium</term><term>Benzoate</term><term>Biophysical research communications</term><term>Bovine serum albumin</term><term>Catalase</term><term>Chem</term><term>Febs letts</term><term>Ferricytochrome</term><term>Ferrocytochrome</term><term>Hydroxyl radicals</term><term>Incubation medium</term><term>Incubation time</term><term>Nadh</term><term>Nadh oxidation</term><term>Nadh oxidation nadh oxidation</term><term>Nmol</term><term>Scavenger</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The granule rich-fraction isolated from human resting polymorphonuclear leukocytes is capable of CN-insensitive NADH oxidation and O2-uptake, accompanied by production of superoxide anion, hydroxyl radicals and H2O2. We showed that H2O2 initiates and maintains NADH oxidation and O2-uptake but is also necessary for the formation of superoxide anion and hydroxyl radicals. It acts as a primary substrate for CN-insensitive protein-mediated formation of hydroxyl radicals, which in turn produce superoxide anions, probably through univalent oxidation of NADH as an intermediary.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>nadh</json:string><json:string>ferrocytochrome</json:string><json:string>benzoate</json:string><json:string>catalase</json:string><json:string>nmol</json:string><json:string>nadh oxidation</json:string><json:string>ferricytochrome</json:string><json:string>chem</json:string><json:string>febs letts</json:string><json:string>incubation time</json:string><json:string>scavenger</json:string><json:string>incubation medium</json:string><json:string>biophysical research communications</json:string><json:string>nadh oxidation nadh oxidation</json:string><json:string>bovine serum albumin</json:string><json:string>hydroxyl radicals</json:string><json:string>assay medium</json:string></teeft></keywords><author><json:item><name>Martine Torres</name><affiliations><json:string>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</json:string></affiliations></json:item><json:item><name>Christian Auclair</name><affiliations><json:string>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</json:string></affiliations></json:item><json:item><name>Jacques Hakim</name><affiliations><json:string>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>PMN : human polymorphonuclear blood cells</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>O2• : superoxide anion radical</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HO• : hydroxyl radical</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>H2O2 : hydrogen peroxide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>GRF : granule-rich fraction</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PB : 0.1 M phosphate buffer (pH 5.5)</value></json:item></subject><articleId><json:string>79915080</json:string></articleId><arkIstex>ark:/67375/6H6-NWVGCRQS-G</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The granule rich-fraction isolated from human resting polymorphonuclear leukocytes is capable of CN-insensitive NADH oxidation and O2-uptake, accompanied by production of superoxide anion, hydroxyl radicals and H2O2. We showed that H2O2 initiates and maintains NADH oxidation and O2-uptake but is also necessary for the formation of superoxide anion and hydroxyl radicals. It acts as a primary substrate for CN-insensitive protein-mediated formation of hydroxyl radicals, which in turn produce superoxide anions, probably through univalent oxidation of NADH as an intermediary.</abstract><qualityIndicators><refBibsNative>true</refBibsNative><abstractWordCount>80</abstractWordCount><abstractCharCount>587</abstractCharCount><keywordCount>6</keywordCount><score>4.252</score><pdfWordCount>1292</pdfWordCount><pdfCharCount>14369</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>7</pdfPageCount><pdfPageSize>483.56 x 720.28 pts</pdfPageSize></qualityIndicators><title>Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes</title><pmid><json:string>223566</json:string></pmid><pii><json:string>0006-291X(79)91508-0</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>Biochemical and Biophysical Research Communications</title><language><json:string>unknown</json:string></language><publicationDate>1979</publicationDate><issn><json:string>0006-291X</json:string></issn><pii><json:string>S0006-291X(00)X0587-6</json:string></pii><volume>88</volume><issue>3</issue><pages><first>1003</first><last>1009</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1979</json:string></date><geogName></geogName><orgName><json:string>- FRANCE Received</json:string><json:string>Academic Press, Inc</json:string><json:string>BIOPHYSICAL RESEARCH COMMUNICATIONS ON GRF</json:string><json:string>BIOPHYSICAL RESEARCH COMMUNICATIONS</json:string><json:string>EXPERIMENTAL RESEARCH COMMUNICATIONS SECTION PMN</json:string><json:string>RESEARCH COMMUNICATIONS</json:string><json:string>INSERM Grant NOATP 61-78-93</json:string></orgName><orgName_funder><json:string>INSERM Grant NOATP 61-78-93</json:string></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Miss M. 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75877 Paris Cedex 18 - France</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Christian</forename><surname>Auclair</surname></persName><affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</affiliation></author><author xml:id="author-0002"><persName><forename type="first">Jacques</forename><surname>Hakim</surname></persName><affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</affiliation></author><idno type="istex">C6EF34B4FA28C4A2F9A51477198C35601FDCE001</idno><idno type="ark">ark:/67375/6H6-NWVGCRQS-G</idno><idno type="DOI">10.1016/0006-291X(79)91508-0</idno><idno type="PII">0006-291X(79)91508-0</idno><idno type="article-id">79915080</idno></analytic><monogr><title level="j">Biochemical and Biophysical Research Communications</title><title level="j" type="abbrev">YBBRC</title><idno type="pISSN">0006-291X</idno><idno type="PII">S0006-291X(00)X0587-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1979"></date><biblScope unit="volume">88</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="1003">1003</biblScope><biblScope unit="page" to="1009">1009</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1979</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The granule rich-fraction isolated from human resting polymorphonuclear leukocytes is capable of CN-insensitive NADH oxidation and O2-uptake, accompanied by production of superoxide anion, hydroxyl radicals and H2O2. We showed that H2O2 initiates and maintains NADH oxidation and O2-uptake but is also necessary for the formation of superoxide anion and hydroxyl radicals. It acts as a primary substrate for CN-insensitive protein-mediated formation of hydroxyl radicals, which in turn produce superoxide anions, probably through univalent oxidation of NADH as an intermediary.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>PMN</term><term>human polymorphonuclear blood cells</term></item><item><term>O2•</term><term>superoxide anion radical</term></item><item><term>HO•</term><term>hydroxyl radical</term></item><item><term>H2O2</term><term>hydrogen peroxide</term></item><item><term>GRF</term><term>granule-rich fraction</term></item><item><term>PB</term><term>0.1 M phosphate buffer (pH 5.5)</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1979">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-NWVGCRQS-G/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>YBBRC</jid><aid>79915080</aid><ce:pii>0006-291X(79)91508-0</ce:pii><ce:doi>10.1016/0006-291X(79)91508-0</ce:doi><ce:copyright type="unknown" year="1979"></ce:copyright></item-info><head><ce:title>Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes</ce:title><ce:author-group><ce:author><ce:given-name>Martine</ce:given-name><ce:surname>Torres</ce:surname></ce:author><ce:author><ce:given-name>Christian</ce:given-name><ce:surname>Auclair</ce:surname></ce:author><ce:author><ce:given-name>Jacques</ce:given-name><ce:surname>Hakim</ce:surname></ce:author><ce:affiliation><ce:textfn>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="10" month="1" year="1979"></ce:date-received><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0010">The granule rich-fraction isolated from human resting polymorphonuclear leukocytes is capable of CN-insensitive NADH oxidation and O<ce:inf loc="post">2</ce:inf>-uptake, accompanied by production of superoxide anion, hydroxyl radicals and H<ce:inf loc="post">2</ce:inf>O<ce:inf loc="post">2</ce:inf>. We showed that H<ce:inf loc="post">2</ce:inf>O<ce:inf loc="post">2</ce:inf> initiates and maintains NADH oxidation and O<ce:inf loc="post">2</ce:inf>-uptake but is also necessary for the formation of superoxide anion and hydroxyl radicals. It acts as a primary substrate for CN-insensitive protein-mediated formation of hydroxyl radicals, which in turn produce superoxide anions, probably through univalent oxidation of NADH as an intermediary.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>PMN</ce:text><ce:keyword><ce:text>human polymorphonuclear blood cells</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text><math altimg="si1.gif">O<inf loc="post">2</inf><ovl type="bar" style="s"><sup loc="post">•</sup></ovl></math></ce:text><ce:keyword><ce:text>superoxide anion radical</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>HO•</ce:text><ce:keyword><ce:text>hydroxyl radical</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>H<ce:inf loc="post">2</ce:inf>O<ce:inf loc="post">2</ce:inf></ce:text><ce:keyword><ce:text>hydrogen peroxide</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>GRF</ce:text><ce:keyword><ce:text>granule-rich fraction</ce:text></ce:keyword></ce:keyword><ce:keyword><ce:text>PB</ce:text><ce:keyword><ce:text>0.1 M phosphate buffer (pH 5.5)</ce:text></ce:keyword></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Protein-mediated hydroxyl radical generation — The primary event in NADH oxidation and oxygen reduction by the granule rich fraction of human resting leukocytes</title></titleInfo><name type="personal"><namePart type="given">Martine</namePart><namePart type="family">Torres</namePart><affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christian</namePart><namePart type="family">Auclair</namePart><affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jacques</namePart><namePart type="family">Hakim</namePart><affiliation>Laboratoire d'Immunologie et d'Hématologie Hôpital Bichat, Université Paris VII 170, boulevard Ney - 75877 Paris Cedex 18 - France</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">1979</dateIssued><copyrightDate encoding="w3cdtf">1979</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The granule rich-fraction isolated from human resting polymorphonuclear leukocytes is capable of CN-insensitive NADH oxidation and O2-uptake, accompanied by production of superoxide anion, hydroxyl radicals and H2O2. We showed that H2O2 initiates and maintains NADH oxidation and O2-uptake but is also necessary for the formation of superoxide anion and hydroxyl radicals. It acts as a primary substrate for CN-insensitive protein-mediated formation of hydroxyl radicals, which in turn produce superoxide anions, probably through univalent oxidation of NADH as an intermediary.</abstract><subject lang="en"><genre>Abbreviations</genre><topic>PMN : human polymorphonuclear blood cells</topic><topic>O2• : superoxide anion radical</topic><topic>HO• : hydroxyl radical</topic><topic>H2O2 : hydrogen peroxide</topic><topic>GRF : granule-rich fraction</topic><topic>PB : 0.1 M phosphate buffer (pH 5.5)</topic></subject><relatedItem type="host"><titleInfo><title>Biochemical and Biophysical Research Communications</title></titleInfo><titleInfo type="abbreviated"><title>YBBRC</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">1979</dateIssued></originInfo><identifier type="ISSN">0006-291X</identifier><identifier type="PII">S0006-291X(00)X0587-6</identifier><part><date>1979</date><detail type="volume"><number>88</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue-pages"><start>753</start><end>1184</end></extent><extent unit="pages"><start>1003</start><end>1009</end></extent></part></relatedItem><identifier type="istex">C6EF34B4FA28C4A2F9A51477198C35601FDCE001</identifier><identifier type="ark">ark:/67375/6H6-NWVGCRQS-G</identifier><identifier type="DOI">10.1016/0006-291X(79)91508-0</identifier><identifier type="PII">0006-291X(79)91508-0</identifier><identifier type="ArticleID">79915080</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/ark:/67375/6H6-NWVGCRQS-G/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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