Cytochrome b of fish mitochondria is strongly resistant to funiculosin, a powerful inhibitor of respiration
Identifieur interne : 000A22 ( Istex/Corpus ); précédent : 000A21; suivant : 000A23Cytochrome b of fish mitochondria is strongly resistant to funiculosin, a powerful inhibitor of respiration
Auteurs : Mauro Degli Esposti ; Anna Ghelli ; Massimo Crimi ; Alessandra Baracca ; Giancarlo Solaini ; Thierry Tron ; Axel MeyerSource :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1992.
Abstract
We report here some unusual properties of ubiquinol: cytochrome c reductase of eel and other fish mitochondria. The turnover rate of the reductase is clearly higher than in mammalian mitochondria and the binding constant for ubiquinone seems to be larger than in other vertebrates. Additionally, the reductase activity of fish mitochondria is resistant to some powerful inhibitors that bind to cytochrome b, in particular to funiculosin. After sequencing most of the gene of eel cytochrome b and comparing the deduced amino acid sequence with that of other fish and animals, we hypothesize that the decreased binding of funiculosin could be due to a few amino acid replacements in the third and fourth transmembrane helix of the protein. In particular, the presence of methionine instead of alanine at position 125 seems to be largely responsible for the strong resistance to funiculosin and also to the partial resistance to myxothiazol in all fish mitochondria. Correlations between some residue substitutions in cytochrome b and the different effects of funiculosin in different species are also considered.
Url:
DOI: 10.1016/0003-9861(92)90506-R
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Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</mods:affiliation></affiliation></author><author><name sortKey="Ghelli, Anna" sort="Ghelli, Anna" uniqKey="Ghelli A" first="Anna" last="Ghelli">Anna Ghelli</name><affiliation><mods:affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy</mods:affiliation></affiliation></author><author><name sortKey="Crimi, Massimo" sort="Crimi, Massimo" uniqKey="Crimi M" first="Massimo" last="Crimi">Massimo Crimi</name><affiliation><mods:affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. 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Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</mods:affiliation></affiliation></author><author><name sortKey="Ghelli, Anna" sort="Ghelli, Anna" uniqKey="Ghelli A" first="Anna" last="Ghelli">Anna Ghelli</name><affiliation><mods:affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy</mods:affiliation></affiliation></author><author><name sortKey="Crimi, Massimo" sort="Crimi, Massimo" uniqKey="Crimi M" first="Massimo" last="Crimi">Massimo Crimi</name><affiliation><mods:affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</mods:affiliation></affiliation></author><author><name sortKey="Baracca, Alessandra" sort="Baracca, Alessandra" uniqKey="Baracca A" first="Alessandra" last="Baracca">Alessandra Baracca</name><affiliation><mods:affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</mods:affiliation></affiliation></author><author><name sortKey="Solaini, Giancarlo" sort="Solaini, Giancarlo" uniqKey="Solaini G" first="Giancarlo" last="Solaini">Giancarlo Solaini</name><affiliation><mods:affiliation>Scuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, Italy</mods:affiliation></affiliation></author><author><name sortKey="Tron, Thierry" sort="Tron, Thierry" uniqKey="Tron T" first="Thierry" last="Tron">Thierry Tron</name><affiliation><mods:affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</mods:affiliation></affiliation></author><author><name sortKey="Meyer, Axel" sort="Meyer, Axel" uniqKey="Meyer A" first="Axel" last="Meyer">Axel Meyer</name><affiliation><mods:affiliation>Department of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</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="1992">1992</date><biblScope unit="volume">295</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="198">198</biblScope><biblScope unit="page" to="204">204</biblScope></imprint><idno type="ISSN">0003-9861</idno></series><idno type="istex">A2484CB35239548DD4EB34F32FFF902C517A7480</idno><idno type="DOI">10.1016/0003-9861(92)90506-R</idno><idno type="PII">0003-9861(92)90506-R</idno><idno type="ArticleID">9290506R</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report here some unusual properties of ubiquinol: cytochrome c reductase of eel and other fish mitochondria. 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Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</json:string></affiliations></json:item><json:item><name>Anna Ghelli</name><affiliations><json:string>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy</json:string></affiliations></json:item><json:item><name>Massimo Crimi</name><affiliations><json:string>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</json:string></affiliations></json:item><json:item><name>Alessandra Baracca</name><affiliations><json:string>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</json:string></affiliations></json:item><json:item><name>Giancarlo Solaini</name><affiliations><json:string>Scuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, Italy</json:string></affiliations></json:item><json:item><name>Thierry Tron</name><affiliations><json:string>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</json:string></affiliations></json:item><json:item><name>Axel Meyer</name><affiliations><json:string>Department of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Biological oxidations, bioenergetics, and P450 reactions</value></json:item></subject><articleId><json:string>9290506R</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>We report here some unusual properties of ubiquinol: cytochrome c reductase of eel and other fish mitochondria. 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Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation></author><author xml:id="author-2"><persName><forename type="first">Anna</forename><surname>Ghelli</surname></persName><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy</affiliation></author><author xml:id="author-3"><persName><forename type="first">Massimo</forename><surname>Crimi</surname></persName><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation></author><author xml:id="author-4"><persName><forename type="first">Alessandra</forename><surname>Baracca</surname></persName><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation></author><author xml:id="author-5"><persName><forename type="first">Giancarlo</forename><surname>Solaini</surname></persName><affiliation>Scuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, Italy</affiliation></author><author xml:id="author-6"><persName><forename type="first">Thierry</forename><surname>Tron</surname></persName><note type="biography">On leave from Unité de Métabolisme Energétique, LCB-CNRS, Marseille, France.</note><affiliation>On leave from Unité de Métabolisme Energétique, LCB-CNRS, Marseille, France.</affiliation><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation></author><author xml:id="author-7"><persName><forename type="first">Axel</forename><surname>Meyer</surname></persName><affiliation>Department of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation></author></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)X0440-7</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992"></date><biblScope unit="volume">295</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="198">198</biblScope><biblScope unit="page" to="204">204</biblScope></imprint></monogr><idno type="istex">A2484CB35239548DD4EB34F32FFF902C517A7480</idno><idno type="DOI">10.1016/0003-9861(92)90506-R</idno><idno type="PII">0003-9861(92)90506-R</idno><idno type="ArticleID">9290506R</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1992</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>We report here some unusual properties of ubiquinol: cytochrome c reductase of eel and other fish mitochondria. The turnover rate of the reductase is clearly higher than in mammalian mitochondria and the binding constant for ubiquinone seems to be larger than in other vertebrates. Additionally, the reductase activity of fish mitochondria is resistant to some powerful inhibitors that bind to cytochrome b, in particular to funiculosin. After sequencing most of the gene of eel cytochrome b and comparing the deduced amino acid sequence with that of other fish and animals, we hypothesize that the decreased binding of funiculosin could be due to a few amino acid replacements in the third and fourth transmembrane helix of the protein. In particular, the presence of methionine instead of alanine at position 125 seems to be largely responsible for the strong resistance to funiculosin and also to the partial resistance to myxothiazol in all fish mitochondria. Correlations between some residue substitutions in cytochrome b and the different effects of funiculosin in different species are also considered.</p></abstract><textClass><keywords scheme="keyword"><list><head>article-category</head><item><term>Biological oxidations, bioenergetics, and P450 reactions</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1992-01-23">Modified</change><change when="1992">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/A2484CB35239548DD4EB34F32FFF902C517A7480/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>9290506R</aid><ce:pii>0003-9861(92)90506-R</ce:pii><ce:doi>10.1016/0003-9861(92)90506-R</ce:doi><ce:copyright type="unknown" year="1992"></ce:copyright><ce:doctopics><ce:doctopic><ce:text>Biological oxidations, bioenergetics, and P450 reactions</ce:text></ce:doctopic></ce:doctopics></item-info><head><ce:title>Cytochrome b of fish mitochondria is strongly resistant to funiculosin, a powerful inhibitor of respiration</ce:title><ce:author-group><ce:author><ce:given-name>Mauro Degli</ce:given-name><ce:surname>Esposti</ce:surname><ce:cross-ref refid="COR1"><ce:sup loc="post">1</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Anna</ce:given-name><ce:surname>Ghelli</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Massimo</ce:given-name><ce:surname>Crimi</ce:surname></ce:author><ce:author><ce:given-name>Alessandra</ce:given-name><ce:surname>Baracca</ce:surname></ce:author><ce:author><ce:given-name>Giancarlo</ce:given-name><ce:surname>Solaini</ce:surname><ce:cross-ref refid="AFF2"><ce:sup loc="post">∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Thierry</ce:given-name><ce:surname>Tron</ce:surname><ce:cross-ref refid="FN1"><ce:sup loc="post">2</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Axel</ce:given-name><ce:surname>Meyer</ce:surname><ce:cross-ref refid="AFF3"><ce:sup loc="post">†</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>∗</ce:label><ce:textfn>Scuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, Italy</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>†</ce:label><ce:textfn>Department of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>1</ce:label><ce:text>To whom correspondence should be addressed.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>2</ce:label><ce:note-para>On leave from Unité de Métabolisme Energétique, LCB-CNRS, Marseille, France.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="25" month="11" year="1991"></ce:date-received><ce:date-revised day="23" month="1" year="1992"></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">We report here some unusual properties of ubiquinol: cytochrome c reductase of eel and other fish mitochondria. The turnover rate of the reductase is clearly higher than in mammalian mitochondria and the binding constant for ubiquinone seems to be larger than in other vertebrates. Additionally, the reductase activity of fish mitochondria is resistant to some powerful inhibitors that bind to cytochrome b, in particular to funiculosin. After sequencing most of the gene of eel cytochrome b and comparing the deduced amino acid sequence with that of other fish and animals, we hypothesize that the decreased binding of funiculosin could be due to a few amino acid replacements in the third and fourth transmembrane helix of the protein. In particular, the presence of methionine instead of alanine at position 125 seems to be largely responsible for the strong resistance to funiculosin and also to the partial resistance to myxothiazol in all fish mitochondria. Correlations between some residue substitutions in cytochrome b and the different effects of funiculosin in different species are also considered.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Cytochrome b of fish mitochondria is strongly resistant to funiculosin, a powerful inhibitor of respiration</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Cytochrome b of fish mitochondria is strongly resistant to funiculosin, a powerful inhibitor of respiration</title></titleInfo><name type="personal"><namePart type="given">Mauro Degli</namePart><namePart type="family">Esposti</namePart><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation><description>To whom correspondence should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Anna</namePart><namePart type="family">Ghelli</namePart><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Massimo</namePart><namePart type="family">Crimi</namePart><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alessandra</namePart><namePart type="family">Baracca</namePart><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Giancarlo</namePart><namePart type="family">Solaini</namePart><affiliation>Scuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, Italy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Thierry</namePart><namePart type="family">Tron</namePart><affiliation>Laboratory of Biochemistry and Biophysics, Department of Biology, University of Bologna, Via Irnerio 42, 40126 Bologna, ItalyScuola Superiore di Studi Universitari e Perfezionamento S. Anna, Pisa, ItalyDepartment of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation><description>On leave from Unité de Métabolisme Energétique, LCB-CNRS, Marseille, France.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Axel</namePart><namePart type="family">Meyer</namePart><affiliation>Department of Ecology and Evolution, Division of Biological Sciences, State University of New York at Stony Brook, Stony Brook, New York 11794-5245 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1992</dateIssued><dateModified encoding="w3cdtf">1992-01-23</dateModified><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">We report here some unusual properties of ubiquinol: cytochrome c reductase of eel and other fish mitochondria. The turnover rate of the reductase is clearly higher than in mammalian mitochondria and the binding constant for ubiquinone seems to be larger than in other vertebrates. Additionally, the reductase activity of fish mitochondria is resistant to some powerful inhibitors that bind to cytochrome b, in particular to funiculosin. After sequencing most of the gene of eel cytochrome b and comparing the deduced amino acid sequence with that of other fish and animals, we hypothesize that the decreased binding of funiculosin could be due to a few amino acid replacements in the third and fourth transmembrane helix of the protein. In particular, the presence of methionine instead of alanine at position 125 seems to be largely responsible for the strong resistance to funiculosin and also to the partial resistance to myxothiazol in all fish mitochondria. Correlations between some residue substitutions in cytochrome b and the different effects of funiculosin in different species are also considered.</abstract><subject><genre>article-category</genre><topic>Biological oxidations, bioenergetics, and P450 reactions</topic></subject><relatedItem type="host"><titleInfo><title>Archives of Biochemistry and Biophysics</title></titleInfo><titleInfo type="abbreviated"><title>YABBI</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19920515</dateIssued></originInfo><identifier type="ISSN">0003-9861</identifier><identifier type="PII">S0003-9861(00)X0440-7</identifier><part><date>19920515</date><detail type="volume"><number>295</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>222</end></extent><extent unit="pages"><start>198</start><end>204</end></extent></part></relatedItem><identifier type="istex">A2484CB35239548DD4EB34F32FFF902C517A7480</identifier><identifier type="DOI">10.1016/0003-9861(92)90506-R</identifier><identifier type="PII">0003-9861(92)90506-R</identifier><identifier type="ArticleID">9290506R</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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