New ganglioside analogs that inhibit influenze virus sialidase
Identifieur interne : 000315 ( Istex/Corpus ); précédent : 000314; suivant : 000316New ganglioside analogs that inhibit influenze virus sialidase
Auteurs : Yasuo Suzuki ; Katsuhiko Sato ; Makoto Kiso ; Akira HasegawaSource :
- Glycoconjugate Journal [ 0282-0080 ] ; 1990-07-01.
English descriptors
- KwdEn :
- Teeft :
- Active site, Analog, Arthrobacter ureafaciens, Bacterial sialidase, Bacterial sialidases, Biochemical nomenclature, Biochim biophys acta, Biol chem, Carbohydr chem, Chem, Clostridium perfringens, Different subtypes, Dixon plot, Effective detergent, Enzyme activity, Enzyme preparation, Final concentration, Ganglioside, Ganglioside analogs, Gangliosides, Glycoprotein, Influenza, Influenza virus, Influenza virus sialidase, Influenza viruses, Inhibitor, Inhibitor concentration, Inhibitory activity, Matsumoto, Neu5ac, Newcastle disease virus, Nmol, Perfringens, Potent inhibitor, Reaction mixtures, Same buffer, Scientific research, Several kinds, Sialic, Sialic acid, Sialidase, Sialidase inhibitor, Sialidases, Sodium acetate buffer, Sodium taurodeoxycholate, Spike glycoprotein, Suzuki, Thioglycoside, Thioglycoside analogs, Ureafaciens, Viral, Viral membranes, Viral sialidase, Virology.
Abstract
Abstract: Synthetic thioglycoside-analogs of gangliosides such as Neu5Acα)2-S-6)Glcβ-(1-1)Ceramide (1) and the GM3 analog Neu5Acα(2-S-6)Galβ-(1–4)Glcβ(1-1)Ceramide (2), competitively inhibited GM3 hydrolysis by the sialidase of different subtypes of human and animal influenza viruses with an apparent Ki value of 2.8×10−6 and 1.5×10−5 M, respectively. The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-S-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (Ki =1.0×10−4 M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases fromClostridium perfringens andArthrobacter ureafaciens was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.
Url:
DOI: 10.1007/BF01073378
Links to Exploration step
ISTEX:1228478A7A2F7C329A7D1EEF343D51741C4185AFLe document en format XML
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The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-S-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (Ki =1.0×10−4 M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases fromClostridium perfringens andArthrobacter ureafaciens was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.</div></front></TEI><istex><corpusName>springer-journals</corpusName><keywords><teeft><json:string>sialidase</json:string><json:string>analog</json:string><json:string>sialidases</json:string><json:string>gangliosides</json:string><json:string>sialic</json:string><json:string>ganglioside</json:string><json:string>influenza virus sialidase</json:string><json:string>influenza virus</json:string><json:string>viral</json:string><json:string>influenza</json:string><json:string>virology</json:string><json:string>chem</json:string><json:string>matsumoto</json:string><json:string>nmol</json:string><json:string>thioglycoside</json:string><json:string>inhibitory activity</json:string><json:string>glycoprotein</json:string><json:string>inhibitor</json:string><json:string>active site</json:string><json:string>perfringens</json:string><json:string>thioglycoside analogs</json:string><json:string>ureafaciens</json:string><json:string>neu5ac</json:string><json:string>bacterial sialidases</json:string><json:string>final concentration</json:string><json:string>suzuki</json:string><json:string>sodium acetate buffer</json:string><json:string>enzyme activity</json:string><json:string>influenza viruses</json:string><json:string>sialic acid</json:string><json:string>newcastle disease virus</json:string><json:string>clostridium perfringens</json:string><json:string>biochim biophys acta</json:string><json:string>spike glycoprotein</json:string><json:string>arthrobacter ureafaciens</json:string><json:string>enzyme preparation</json:string><json:string>bacterial sialidase</json:string><json:string>same buffer</json:string><json:string>viral sialidase</json:string><json:string>sodium taurodeoxycholate</json:string><json:string>effective detergent</json:string><json:string>viral membranes</json:string><json:string>inhibitor concentration</json:string><json:string>dixon plot</json:string><json:string>reaction mixtures</json:string><json:string>potent inhibitor</json:string><json:string>several kinds</json:string><json:string>scientific research</json:string><json:string>ganglioside analogs</json:string><json:string>different subtypes</json:string><json:string>biol chem</json:string><json:string>sialidase inhibitor</json:string><json:string>carbohydr chem</json:string><json:string>biochemical nomenclature</json:string></teeft></keywords><author><json:item><name>Yasuo Suzuki</name><affiliations><json:string>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka, Japan</json:string></affiliations></json:item><json:item><name>Katsuhiko Sato</name><affiliations><json:string>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka, Japan</json:string></affiliations></json:item><json:item><name>Makoto Kiso</name><affiliations><json:string>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</json:string></affiliations></json:item><json:item><name>Akira Hasegawa</name><affiliations><json:string>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>sialidase inhibitor</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Thioglycoside-analog of ganglioside</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>influenza virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Cer : ceramide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>GM3 : Neu5Acα(2–3)Galβ(1–4)Glcβ(1-1)Cer</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>GM4 : Neu5Acα(2–3)Galβ(1-1)Cer</value></json:item></subject><articleId><json:string>BF01073378</json:string><json:string>Art9</json:string></articleId><arkIstex>ark:/67375/1BB-9N1XBGQH-Q</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: Synthetic thioglycoside-analogs of gangliosides such as Neu5Acα)2-S-6)Glcβ-(1-1)Ceramide (1) and the GM3 analog Neu5Acα(2-S-6)Galβ-(1–4)Glcβ(1-1)Ceramide (2), competitively inhibited GM3 hydrolysis by the sialidase of different subtypes of human and animal influenza viruses with an apparent Ki value of 2.8×10−6 and 1.5×10−5 M, respectively. The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-S-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (Ki =1.0×10−4 M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases fromClostridium perfringens andArthrobacter ureafaciens was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.</abstract><qualityIndicators><score>5.89</score><pdfWordCount>2126</pdfWordCount><pdfCharCount>14340</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>8</pdfPageCount><pdfPageSize>482.28 x 677 pts</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>147</abstractWordCount><abstractCharCount>1089</abstractCharCount><keywordCount>6</keywordCount></qualityIndicators><title>New ganglioside analogs that inhibit influenze virus sialidase</title><pmid><json:string>2136350</json:string></pmid><genre><json:string>research-article</json:string></genre><host><title>Glycoconjugate Journal</title><language><json:string>unknown</json:string></language><publicationDate>1990</publicationDate><copyrightDate>1990</copyrightDate><issn><json:string>0282-0080</json:string></issn><eissn><json:string>1573-4986</json:string></eissn><journalId><json:string>10719</json:string></journalId><volume>7</volume><issue>4</issue><pages><first>349</first><last>356</last></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Pathology</value></json:item><json:item><value>Biochemistry, general</value></json:item></subject></host><namedEntities><unitex><date></date><geogName></geogName><orgName></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName></persName><placeName></placeName><ref_url></ref_url><ref_bibl></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/1BB-9N1XBGQH-Q</json:string></ark><categories><wos><json:string>1 - 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The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-S-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (Ki =1.0×10−4 M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases fromClostridium perfringens andArthrobacter ureafaciens was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Key words</head><item><term>sialidase inhibitor</term></item><item><term>Thioglycoside-analog of ganglioside</term></item><item><term>influenza virus</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>Cer</term><term>ceramide</term></item><item><term>GM3</term><term>Neu5Acα(2–3)Galβ(1–4)Glcβ(1-1)Cer</term></item><item><term>GM4</term><term>Neu5Acα(2–3)Galβ(1-1)Cer</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Pathology</term></item><item><term>Biochemistry, general</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1990-05-28">Created</change><change when="1990-07-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-9N1XBGQH-Q/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType 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general</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>7</VolumeIDStart><VolumeIDEnd>7</VolumeIDEnd><VolumeIssueCount>6</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>4</IssueIDStart><IssueIDEnd>4</IssueIDEnd><IssueArticleCount>9</IssueArticleCount><IssueHistory><CoverDate><DateString>1990</DateString><Year>1990</Year><Month>7</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Glycoconjugate Journal AB</CopyrightHolderName><CopyrightYear>1990</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art9"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF01073378</ArticleID><ArticleDOI>10.1007/BF01073378</ArticleDOI><ArticleSequenceNumber>9</ArticleSequenceNumber><ArticleTitle Language="En">New ganglioside analogs that inhibit influenze virus sialidase</ArticleTitle><ArticleFirstPage>349</ArticleFirstPage><ArticleLastPage>356</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2005</Year><Month>1</Month><Day>15</Day></RegistrationDate><Received><Year>1990</Year><Month>5</Month><Day>28</Day></Received></ArticleHistory><ArticleCopyright><CopyrightHolderName>Glycoconjugate Journal AB</CopyrightHolderName><CopyrightYear>1990</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>10719</JournalID><VolumeIDStart>7</VolumeIDStart><VolumeIDEnd>7</VolumeIDEnd><IssueIDStart>4</IssueIDStart><IssueIDEnd>4</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Yasuo</GivenName><FamilyName>Suzuki</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Katsuhiko</GivenName><FamilyName>Sato</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Makoto</GivenName><FamilyName>Kiso</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Akira</GivenName><FamilyName>Hasegawa</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Department of Biochemistry</OrgDivision><OrgName>University of Shizuoka, School of Pharmaceutical Science</OrgName><OrgAddress><Street>395 Yada</Street><Postcode>422</Postcode><City>Shizuoka</City><Country>Japan</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Department of Applied Bio-organic Chemistry</OrgDivision><OrgName>Gifu University</OrgName><OrgAddress><Postcode>501-11</Postcode><City>Gifu</City><Country>Japan</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>Synthetic thioglycoside-analogs of gangliosides such as Neu5Acα)2-<Emphasis Type="Italic">S</Emphasis>-6)Glcβ-(1-1)Ceramide (1) and the GM3 analog Neu5Acα(2-<Emphasis Type="Italic">S</Emphasis>-6)Galβ-(1–4)Glcβ(1-1)Ceramide (2), competitively inhibited GM3 hydrolysis by the sialidase of different subtypes of human and animal influenza viruses with an apparent K<Subscript>i</Subscript> value of 2.8×10<Superscript>−6</Superscript> and 1.5×10<Superscript>−5</Superscript> M, respectively. The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-<Emphasis Type="Italic">S</Emphasis>-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (K<Subscript>i</Subscript> =1.0×10<Superscript>−4</Superscript> M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases from<Emphasis Type="Italic">Clostridium perfringens</Emphasis> and<Emphasis Type="Italic">Arthrobacter ureafaciens</Emphasis> was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.</Para></Abstract><KeywordGroup Language="En"><Heading>Key words</Heading><Keyword><Emphasis Type="Italic">sialidase inhibitor</Emphasis></Keyword><Keyword><Emphasis Type="Italic">Thioglycoside-analog of ganglioside</Emphasis></Keyword><Keyword><Emphasis Type="Italic">influenza virus</Emphasis></Keyword></KeywordGroup><AbbreviationGroup><Heading>Abbreviations</Heading><DefinitionList><DefinitionListEntry><Term>Cer</Term><Description><Para>ceramide</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>GM3</Term><Description><Para>Neu5Acα(2–3)Galβ(1–4)Glcβ(1-1)Cer</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>GM4</Term><Description><Para>Neu5Acα(2–3)Galβ(1-1)Cer</Para></Description></DefinitionListEntry></DefinitionList></AbbreviationGroup><ArticleNote Type="Misc"><SimplePara>Gangliosides were abbreviated according to Svennerholm [1] and the recommendation of the IUPAC-IUB Commission on Biochemical Nomenclature [2].</SimplePara></ArticleNote></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>New ganglioside analogs that inhibit influenze virus sialidase</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>New ganglioside analogs that inhibit influenze virus sialidase</title></titleInfo><name type="personal" displayLabel="corresp"><namePart type="given">Yasuo</namePart><namePart type="family">Suzuki</namePart><affiliation>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Katsuhiko</namePart><namePart type="family">Sato</namePart><affiliation>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, 395 Yada, 422, Shizuoka, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Makoto</namePart><namePart type="family">Kiso</namePart><affiliation>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Akira</namePart><namePart type="family">Hasegawa</namePart><affiliation>Department of Applied Bio-organic Chemistry, Gifu University, 501-11, Gifu, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" 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>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateCreated encoding="w3cdtf">1990-05-28</dateCreated><dateIssued encoding="w3cdtf">1990-07-01</dateIssued><copyrightDate encoding="w3cdtf">1990</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Synthetic thioglycoside-analogs of gangliosides such as Neu5Acα)2-S-6)Glcβ-(1-1)Ceramide (1) and the GM3 analog Neu5Acα(2-S-6)Galβ-(1–4)Glcβ(1-1)Ceramide (2), competitively inhibited GM3 hydrolysis by the sialidase of different subtypes of human and animal influenza viruses with an apparent Ki value of 2.8×10−6 and 1.5×10−5 M, respectively. The inhibitory activity of the ganglioside GM4 analog [Neu5Acα-(2-S-6)Galβ-(1-1)Ceramide (3)], in which the glucose of 1 was substituted by galactose, was lower than that of 1 (Ki =1.0×10−4 M). The thioglycoside-analogs (1, 2, 3) of the gangliosides were nonhydrolyzable substrates for influenza virus sialidase. The inhibitory activity of 1 to bacterial sialidases fromClostridium perfringens andArthrobacter ureafaciens was considerably lower than that to influenza virus sialidase, indicating that the structure of the active site in bacterial and influenza virus sialidase may be different and the analogs may be useful to determine the orientation of the substrate to the active site of sialidases, especially of influenza viruses.</abstract><subject lang="en"><genre>Key words</genre><topic>sialidase inhibitor</topic><topic>Thioglycoside-analog of ganglioside</topic><topic>influenza virus</topic></subject><subject><genre>Abbreviations</genre><topic>Cer : ceramide</topic><topic>GM3 : Neu5Acα(2–3)Galβ(1–4)Glcβ(1-1)Cer</topic><topic>GM4 : Neu5Acα(2–3)Galβ(1-1)Cer</topic></subject><relatedItem type="host"><titleInfo><title>Glycoconjugate Journal</title><subTitle>Official Journal of the International Glycoconjugate Organization</subTitle></titleInfo><titleInfo type="abbreviated"><title>Glycoconjugate J</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>Springer</publisher><dateIssued encoding="w3cdtf">1990-07-01</dateIssued><copyrightDate encoding="w3cdtf">1990</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Pathology</topic><topic>Biochemistry, general</topic></subject><identifier type="ISSN">0282-0080</identifier><identifier type="eISSN">1573-4986</identifier><identifier type="JournalID">10719</identifier><identifier type="IssueArticleCount">9</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>1990</date><detail type="volume"><number>7</number><caption>vol.</caption></detail><detail type="issue"><number>4</number><caption>no.</caption></detail><extent unit="pages"><start>349</start><end>356</end></extent></part><recordInfo><recordOrigin>Glycoconjugate Journal AB, 1990</recordOrigin></recordInfo></relatedItem><identifier type="istex">1228478A7A2F7C329A7D1EEF343D51741C4185AF</identifier><identifier type="ark">ark:/67375/1BB-9N1XBGQH-Q</identifier><identifier type="DOI">10.1007/BF01073378</identifier><identifier type="ArticleID">BF01073378</identifier><identifier type="ArticleID">Art9</identifier><accessCondition type="use and reproduction" contentType="copyright">Glycoconjugate Journal AB, 1990</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Glycoconjugate Journal AB, 1990</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-9N1XBGQH-Q/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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