In Vitro Maturation of Prehead-like Bacteriophage T4 Polyheads: Structural Changes Accompanying Proteolytic Cleavage and Lattice Expansion
Identifieur interne : 002529 ( Istex/Corpus ); précédent : 002528; suivant : 002530In Vitro Maturation of Prehead-like Bacteriophage T4 Polyheads: Structural Changes Accompanying Proteolytic Cleavage and Lattice Expansion
Auteurs : M. Müller ; V. V. Mesyanzhinov ; U. AebiSource :
- Journal of Structural Biology [ 1047-8477 ] ; 1994.
Abstract
Abstract: We have studied cleavage and expansion of the major T4 phage capsid protein gp23 (56 kDa) using polyheads, an aberrant, polymorphic tubular variant of bacteriophage T4D, as a model system. In a first step, we have cleaved the 65-amino-acid-long amino-terminal "Δ piece" by limited proteolysis with Staphylococcus aureus V8 protease (type XVII) at exactly the same position, i.e., between residues 65 and 66, at which the phage-coded T4Ppase cleaves, to yield mature gp23* (48.7 kDa) without significantly affecting a second potential cleavage site between amino acids 142 and 143. Negatively stained preparations of thus cleaved polyheads revealed a near-hexagonal lattice with a 11.2-nm lattice constant. One-sided correlation averages of these cleaved/unexpanded polyheads yielded capsomeres that were rounder than those of prehead-like (i.e., uncleaved) control polyheads, with distinct trimers of mass (specifically, trimers of Δ pieces in the area where three protomers are shared among three different capsomeres) removed, as revealed by difference maps computed from the correlation averages. Quantitative expansion of the 11.2-nm near-hexagonal lattice into the 13-nm near-hexagonal lattice characteristic of mature phage heads could be induced by pelleting the cleaved/unexpanded polyheads and resuspending them in water. This expansion step was inhibited by the presence of 100 mM phosphate. Cleavage of prehead-like polyheads to the 41-kDa gp23+ either between residues 142 and 143 by V8 protease or between residues 143 and 144 by trypsin rendered the polyheads unable to expand. In contrast, cleaved/expanded gp23* polyheads became resistant to cleavage to gp23+. As revealed by difference maps, the 7.3-kDa mass was additionally missing at the comers where the Δ-piece trimers contact the protomers.
Url:
DOI: 10.1006/jsbi.1994.1021
Links to Exploration step
ISTEX:430FFEC1C00D348F2927655325571B6DC57506F8Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">In Vitro Maturation of Prehead-like Bacteriophage T4 Polyheads: Structural Changes Accompanying Proteolytic Cleavage and Lattice Expansion</title><author><name sortKey="Muller, M" sort="Muller, M" uniqKey="Muller M" first="M." last="Müller">M. Müller</name><affiliation><mods:affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</mods:affiliation></affiliation></author><author><name sortKey="Mesyanzhinov, V V" sort="Mesyanzhinov, V V" uniqKey="Mesyanzhinov V" first="V. V." last="Mesyanzhinov">V. V. Mesyanzhinov</name><affiliation><mods:affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</mods:affiliation></affiliation></author><author><name sortKey="Aebi, U" sort="Aebi, U" uniqKey="Aebi U" first="U." last="Aebi">U. Aebi</name><affiliation><mods:affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:430FFEC1C00D348F2927655325571B6DC57506F8</idno><date when="1994" year="1994">1994</date><idno type="doi">10.1006/jsbi.1994.1021</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-TGKLLC3H-2/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">002529</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002529</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">In Vitro Maturation of Prehead-like Bacteriophage T4 Polyheads: Structural Changes Accompanying Proteolytic Cleavage and Lattice Expansion</title><author><name sortKey="Muller, M" sort="Muller, M" uniqKey="Muller M" first="M." last="Müller">M. Müller</name><affiliation><mods:affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</mods:affiliation></affiliation></author><author><name sortKey="Mesyanzhinov, V V" sort="Mesyanzhinov, V V" uniqKey="Mesyanzhinov V" first="V. V." last="Mesyanzhinov">V. V. Mesyanzhinov</name><affiliation><mods:affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</mods:affiliation></affiliation></author><author><name sortKey="Aebi, U" sort="Aebi, U" uniqKey="Aebi U" first="U." last="Aebi">U. Aebi</name><affiliation><mods:affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Structural Biology</title><title level="j" type="abbrev">YJSBI</title><idno type="ISSN">1047-8477</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">112</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="199">199</biblScope><biblScope unit="page" to="215">215</biblScope></imprint><idno type="ISSN">1047-8477</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1047-8477</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: We have studied cleavage and expansion of the major T4 phage capsid protein gp23 (56 kDa) using polyheads, an aberrant, polymorphic tubular variant of bacteriophage T4D, as a model system. In a first step, we have cleaved the 65-amino-acid-long amino-terminal "Δ piece" by limited proteolysis with Staphylococcus aureus V8 protease (type XVII) at exactly the same position, i.e., between residues 65 and 66, at which the phage-coded T4Ppase cleaves, to yield mature gp23* (48.7 kDa) without significantly affecting a second potential cleavage site between amino acids 142 and 143. Negatively stained preparations of thus cleaved polyheads revealed a near-hexagonal lattice with a 11.2-nm lattice constant. One-sided correlation averages of these cleaved/unexpanded polyheads yielded capsomeres that were rounder than those of prehead-like (i.e., uncleaved) control polyheads, with distinct trimers of mass (specifically, trimers of Δ pieces in the area where three protomers are shared among three different capsomeres) removed, as revealed by difference maps computed from the correlation averages. Quantitative expansion of the 11.2-nm near-hexagonal lattice into the 13-nm near-hexagonal lattice characteristic of mature phage heads could be induced by pelleting the cleaved/unexpanded polyheads and resuspending them in water. This expansion step was inhibited by the presence of 100 mM phosphate. Cleavage of prehead-like polyheads to the 41-kDa gp23+ either between residues 142 and 143 by V8 protease or between residues 143 and 144 by trypsin rendered the polyheads unable to expand. In contrast, cleaved/expanded gp23* polyheads became resistant to cleavage to gp23+. As revealed by difference maps, the 7.3-kDa mass was additionally missing at the comers where the Δ-piece trimers contact the protomers.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>M. Müller</name><affiliations><json:string>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</json:string></affiliations></json:item><json:item><name>V.V. Mesyanzhinov</name><affiliations><json:string>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</json:string></affiliations></json:item><json:item><name>U. Aebi</name><affiliations><json:string>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-TGKLLC3H-2</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: We have studied cleavage and expansion of the major T4 phage capsid protein gp23 (56 kDa) using polyheads, an aberrant, polymorphic tubular variant of bacteriophage T4D, as a model system. In a first step, we have cleaved the 65-amino-acid-long amino-terminal "Δ piece" by limited proteolysis with Staphylococcus aureus V8 protease (type XVII) at exactly the same position, i.e., between residues 65 and 66, at which the phage-coded T4Ppase cleaves, to yield mature gp23* (48.7 kDa) without significantly affecting a second potential cleavage site between amino acids 142 and 143. Negatively stained preparations of thus cleaved polyheads revealed a near-hexagonal lattice with a 11.2-nm lattice constant. One-sided correlation averages of these cleaved/unexpanded polyheads yielded capsomeres that were rounder than those of prehead-like (i.e., uncleaved) control polyheads, with distinct trimers of mass (specifically, trimers of Δ pieces in the area where three protomers are shared among three different capsomeres) removed, as revealed by difference maps computed from the correlation averages. Quantitative expansion of the 11.2-nm near-hexagonal lattice into the 13-nm near-hexagonal lattice characteristic of mature phage heads could be induced by pelleting the cleaved/unexpanded polyheads and resuspending them in water. This expansion step was inhibited by the presence of 100 mM phosphate. Cleavage of prehead-like polyheads to the 41-kDa gp23+ either between residues 142 and 143 by V8 protease or between residues 143 and 144 by trypsin rendered the polyheads unable to expand. In contrast, cleaved/expanded gp23* polyheads became resistant to cleavage to gp23+. 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E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</affiliation></author><author xml:id="author-0001"><persName><forename type="first">V.V.</forename><surname>Mesyanzhinov</surname></persName><affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</affiliation></author><author xml:id="author-0002"><persName><forename type="first">U.</forename><surname>Aebi</surname></persName><affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</affiliation></author><idno type="istex">430FFEC1C00D348F2927655325571B6DC57506F8</idno><idno type="ark">ark:/67375/6H6-TGKLLC3H-2</idno><idno type="DOI">10.1006/jsbi.1994.1021</idno><idno type="PII">S1047-8477(84)71021-5</idno></analytic><monogr><title level="j">Journal of Structural Biology</title><title level="j" type="abbrev">YJSBI</title><idno type="pISSN">1047-8477</idno><idno type="PII">S1047-8477(00)X0051-2</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994"></date><biblScope unit="volume">112</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="199">199</biblScope><biblScope unit="page" to="215">215</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1994</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: We have studied cleavage and expansion of the major T4 phage capsid protein gp23 (56 kDa) using polyheads, an aberrant, polymorphic tubular variant of bacteriophage T4D, as a model system. In a first step, we have cleaved the 65-amino-acid-long amino-terminal "Δ piece" by limited proteolysis with Staphylococcus aureus V8 protease (type XVII) at exactly the same position, i.e., between residues 65 and 66, at which the phage-coded T4Ppase cleaves, to yield mature gp23* (48.7 kDa) without significantly affecting a second potential cleavage site between amino acids 142 and 143. Negatively stained preparations of thus cleaved polyheads revealed a near-hexagonal lattice with a 11.2-nm lattice constant. One-sided correlation averages of these cleaved/unexpanded polyheads yielded capsomeres that were rounder than those of prehead-like (i.e., uncleaved) control polyheads, with distinct trimers of mass (specifically, trimers of Δ pieces in the area where three protomers are shared among three different capsomeres) removed, as revealed by difference maps computed from the correlation averages. Quantitative expansion of the 11.2-nm near-hexagonal lattice into the 13-nm near-hexagonal lattice characteristic of mature phage heads could be induced by pelleting the cleaved/unexpanded polyheads and resuspending them in water. This expansion step was inhibited by the presence of 100 mM phosphate. Cleavage of prehead-like polyheads to the 41-kDa gp23+ either between residues 142 and 143 by V8 protease or between residues 143 and 144 by trypsin rendered the polyheads unable to expand. In contrast, cleaved/expanded gp23* polyheads became resistant to cleavage to gp23+. As revealed by difference maps, the 7.3-kDa mass was additionally missing at the comers where the Δ-piece trimers contact the protomers.</p></abstract></profileDesc><revisionDesc><change when="1994">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-TGKLLC3H-2/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier converted-article found"><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>YJSBI</jid><aid>71021</aid><ce:pii>S1047-8477(84)71021-5</ce:pii><ce:doi>10.1006/jsbi.1994.1021</ce:doi><ce:copyright type="full-transfer" year="1994">Academic Press</ce:copyright></item-info><head><ce:dochead><ce:textfn>Regular Article</ce:textfn></ce:dochead><ce:title><ce:italic>In Vitro</ce:italic> Maturation of Prehead-like Bacteriophage T4 Polyheads: Structural Changes Accompanying Proteolytic Cleavage and Lattice Expansion</ce:title><ce:author-group><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Müller</ce:surname></ce:author><ce:author><ce:given-name>V.V.</ce:given-name><ce:surname>Mesyanzhinov</ce:surname></ce:author><ce:author><ce:given-name>U.</ce:given-name><ce:surname>Aebi</ce:surname></ce:author><ce:affiliation><ce:textfn>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</ce:textfn></ce:affiliation></ce:author-group><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>We have studied cleavage and expansion of the major T4 phage capsid protein gp23 (56 kDa) using polyheads, an aberrant, polymorphic tubular variant of bacteriophage T4D, as a model system. In a first step, we have cleaved the 65-amino-acid-long amino-terminal "Δ piece" by limited proteolysis with <ce:italic>Staphylococcus aureus</ce:italic> V8 protease (type XVII) at exactly the same position, i.e., between residues 65 and 66, at which the phage-coded T4Ppase cleaves, to yield mature gp23<ce:sup>*</ce:sup> (48.7 kDa) without significantly affecting a second potential cleavage site between amino acids 142 and 143. Negatively stained preparations of thus cleaved polyheads revealed a near-hexagonal lattice with a 11.2-nm lattice constant. One-sided correlation averages of these cleaved/unexpanded polyheads yielded capsomeres that were rounder than those of prehead-like (i.e., uncleaved) control polyheads, with distinct trimers of mass (specifically, trimers of Δ pieces in the area where three protomers are shared among three different capsomeres) removed, as revealed by difference maps computed from the correlation averages. Quantitative expansion of the 11.2-nm near-hexagonal lattice into the 13-nm near-hexagonal lattice characteristic of mature phage heads could be induced by pelleting the cleaved/unexpanded polyheads and resuspending them in water. This expansion step was inhibited by the presence of 100 m<ce:italic>M</ce:italic> phosphate. Cleavage of prehead-like polyheads to the 41-kDa gp23<ce:sup>+</ce:sup> either between residues 142 and 143 by V8 protease or between residues 143 and 144 by trypsin rendered the polyheads unable to expand. In contrast, cleaved/expanded gp23<ce:sup>*</ce:sup> polyheads became resistant to cleavage to gp23<ce:sup>+</ce:sup>. As revealed by difference maps, the 7.3-kDa mass was additionally missing at the comers where the Δ-piece trimers contact the protomers.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>In Vitro Maturation of Prehead-like Bacteriophage T4 Polyheads: Structural Changes Accompanying Proteolytic Cleavage and Lattice Expansion</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Maturation of Prehead-like Bacteriophage T4 Polyheads: Structural Changes Accompanying Proteolytic Cleavage and Lattice Expansion</title></titleInfo><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Müller</namePart><affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">V.V.</namePart><namePart type="family">Mesyanzhinov</namePart><affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">U.</namePart><namePart type="family">Aebi</namePart><affiliation>M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, CH-4056 Basel, Switzerland; Department of Basic Virology, Ivanovsky Institute of Virology, 123098 Moscow, Russia; and Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205</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">1994</dateIssued><copyrightDate encoding="w3cdtf">1994</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: We have studied cleavage and expansion of the major T4 phage capsid protein gp23 (56 kDa) using polyheads, an aberrant, polymorphic tubular variant of bacteriophage T4D, as a model system. In a first step, we have cleaved the 65-amino-acid-long amino-terminal "Δ piece" by limited proteolysis with Staphylococcus aureus V8 protease (type XVII) at exactly the same position, i.e., between residues 65 and 66, at which the phage-coded T4Ppase cleaves, to yield mature gp23* (48.7 kDa) without significantly affecting a second potential cleavage site between amino acids 142 and 143. Negatively stained preparations of thus cleaved polyheads revealed a near-hexagonal lattice with a 11.2-nm lattice constant. One-sided correlation averages of these cleaved/unexpanded polyheads yielded capsomeres that were rounder than those of prehead-like (i.e., uncleaved) control polyheads, with distinct trimers of mass (specifically, trimers of Δ pieces in the area where three protomers are shared among three different capsomeres) removed, as revealed by difference maps computed from the correlation averages. Quantitative expansion of the 11.2-nm near-hexagonal lattice into the 13-nm near-hexagonal lattice characteristic of mature phage heads could be induced by pelleting the cleaved/unexpanded polyheads and resuspending them in water. This expansion step was inhibited by the presence of 100 mM phosphate. Cleavage of prehead-like polyheads to the 41-kDa gp23+ either between residues 142 and 143 by V8 protease or between residues 143 and 144 by trypsin rendered the polyheads unable to expand. In contrast, cleaved/expanded gp23* polyheads became resistant to cleavage to gp23+. As revealed by difference maps, the 7.3-kDa mass was additionally missing at the comers where the Δ-piece trimers contact the protomers.</abstract><note type="content">Section title: Regular Article</note><relatedItem type="host"><titleInfo><title>Journal of Structural Biology</title></titleInfo><titleInfo type="abbreviated"><title>YJSBI</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">1994</dateIssued></originInfo><identifier type="ISSN">1047-8477</identifier><identifier type="PII">S1047-8477(00)X0051-2</identifier><part><date>1994</date><detail type="volume"><number>112</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue-pages"><start>172</start><end>259</end></extent><extent unit="pages"><start>199</start><end>215</end></extent></part></relatedItem><identifier type="istex">430FFEC1C00D348F2927655325571B6DC57506F8</identifier><identifier type="ark">ark:/67375/6H6-TGKLLC3H-2</identifier><identifier type="DOI">10.1006/jsbi.1994.1021</identifier><identifier type="PII">S1047-8477(84)71021-5</identifier><accessCondition type="use and reproduction" contentType="copyright">©1994 Academic Press</accessCondition><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><recordOrigin>Academic Press, ©1994</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-TGKLLC3H-2/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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