Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids
Identifieur interne : 003936 ( Istex/Corpus ); précédent : 003935; suivant : 003937Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids
Auteurs : Y. Fujii ; H. Higashi ; K. Ikuta ; S. Kato ; M. NaikiSource :
- Molecular Immunology [ 0161-5890 ] ; 1981.
Abstract
The precise specificities of human H-D antibodies and newly obtained avian antisera to the H-D antigen-active glycosphingolipids, N-glycolylneuraminyl(α2–3)lactosyl ceramide (hematoside) and N-glycolylneuraminyl(α2–3)lactoneotetraosyl ceramide (sialosylparagloboside) were compared by gel precipitation and hemagglutination inhibition using other gangliosides with a related structure and chemically modified hematoside derivatives and the oligosaccharides from both the antigenic glycosphingolipids. Human H-D antibodies were found to have the same affinity for both antigenic glycosphingolipids; however, the avian anti-hematoside or anti-sialosylparaglobosides showed a higher affinity for the homologous antigen. Human H-D antibodies were directed more exactly toward the terminal sialic acid residue and more roughly to the hydrophobic portion of both compounds; however, the two avian antibodies were directed more specifically to the whole structure of the homologous antigen glycosphingolipid.
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DOI: 10.1016/0161-5890(82)90250-4
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Ikuta</name><affiliation><mods:affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kato, S" sort="Kato, S" uniqKey="Kato S" first="S." last="Kato">S. Kato</name><affiliation><mods:affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</mods:affiliation></affiliation></author><author><name sortKey="Naiki, M" sort="Naiki, M" uniqKey="Naiki M" first="M." last="Naiki">M. Naiki</name><affiliation><mods:affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB</idno><date when="1982" year="1982">1982</date><idno type="doi">10.1016/0161-5890(82)90250-4</idno><idno type="url">https://api.istex.fr/document/95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">003936</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids</title><author><name sortKey="Fujii, Y" sort="Fujii, Y" uniqKey="Fujii Y" first="Y." last="Fujii">Y. Fujii</name><affiliation><mods:affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</mods:affiliation></affiliation></author><author><name sortKey="Higashi, H" sort="Higashi, H" uniqKey="Higashi H" first="H." last="Higashi">H. Higashi</name><affiliation><mods:affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</mods:affiliation></affiliation></author><author><name sortKey="Ikuta, K" sort="Ikuta, K" uniqKey="Ikuta K" first="K." last="Ikuta">K. Ikuta</name><affiliation><mods:affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</mods:affiliation></affiliation></author><author><name sortKey="Kato, S" sort="Kato, S" uniqKey="Kato S" first="S." last="Kato">S. Kato</name><affiliation><mods:affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</mods:affiliation></affiliation></author><author><name sortKey="Naiki, M" sort="Naiki, M" uniqKey="Naiki M" first="M." last="Naiki">M. Naiki</name><affiliation><mods:affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Immunology</title><title level="j" type="abbrev">MIMM</title><idno type="ISSN">0161-5890</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1981">1981</date><biblScope unit="volume">19</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="87">87</biblScope><biblScope unit="page" to="94">94</biblScope></imprint><idno type="ISSN">0161-5890</idno></series><idno type="istex">95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB</idno><idno type="DOI">10.1016/0161-5890(82)90250-4</idno><idno type="PII">0161-5890(82)90250-4</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0161-5890</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The precise specificities of human H-D antibodies and newly obtained avian antisera to the H-D antigen-active glycosphingolipids, N-glycolylneuraminyl(α2–3)lactosyl ceramide (hematoside) and N-glycolylneuraminyl(α2–3)lactoneotetraosyl ceramide (sialosylparagloboside) were compared by gel precipitation and hemagglutination inhibition using other gangliosides with a related structure and chemically modified hematoside derivatives and the oligosaccharides from both the antigenic glycosphingolipids. Human H-D antibodies were found to have the same affinity for both antigenic glycosphingolipids; however, the avian anti-hematoside or anti-sialosylparaglobosides showed a higher affinity for the homologous antigen. Human H-D antibodies were directed more exactly toward the terminal sialic acid residue and more roughly to the hydrophobic portion of both compounds; however, the two avian antibodies were directed more specifically to the whole structure of the homologous antigen glycosphingolipid.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Y. Fujii</name><affiliations><json:string>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</json:string></affiliations></json:item><json:item><name>H. Higashi</name><affiliations><json:string>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</json:string></affiliations></json:item><json:item><name>K. Ikuta</name><affiliations><json:string>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</json:string></affiliations></json:item><json:item><name>S. Kato</name><affiliations><json:string>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</json:string></affiliations></json:item><json:item><name>M. Naiki</name><affiliations><json:string>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</json:string></affiliations></json:item></author><language><json:string>eng</json:string></language><abstract>The precise specificities of human H-D antibodies and newly obtained avian antisera to the H-D antigen-active glycosphingolipids, N-glycolylneuraminyl(α2–3)lactosyl ceramide (hematoside) and N-glycolylneuraminyl(α2–3)lactoneotetraosyl ceramide (sialosylparagloboside) were compared by gel precipitation and hemagglutination inhibition using other gangliosides with a related structure and chemically modified hematoside derivatives and the oligosaccharides from both the antigenic glycosphingolipids. Human H-D antibodies were found to have the same affinity for both antigenic glycosphingolipids; however, the avian anti-hematoside or anti-sialosylparaglobosides showed a higher affinity for the homologous antigen. Human H-D antibodies were directed more exactly toward the terminal sialic acid residue and more roughly to the hydrophobic portion of both compounds; however, the two avian antibodies were directed more specifically to the whole structure of the homologous antigen glycosphingolipid.</abstract><qualityIndicators><score>4.999</score><pdfVersion>1.4</pdfVersion><pdfPageSize>504 x 756 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>1001</abstractCharCount><pdfWordCount>3047</pdfWordCount><pdfCharCount>28510</pdfCharCount><pdfPageCount>8</pdfPageCount><abstractWordCount>121</abstractWordCount></qualityIndicators><title>Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids</title><pii><json:string>0161-5890(82)90250-4</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>19</volume><pii><json:string>S0161-5890(00)X0139-3</json:string></pii><pages><last>94</last><first>87</first></pages><issn><json:string>0161-5890</json:string></issn><issue>1</issue><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><title>Molecular Immunology</title><publicationDate>1982</publicationDate></host><categories><wos><json:string>IMMUNOLOGY</json:string><json:string>BIOCHEMISTRY & MOLECULAR BIOLOGY</json:string></wos></categories><publicationDate>1981</publicationDate><copyrightDate>1982</copyrightDate><doi><json:string>10.1016/0161-5890(82)90250-4</json:string></doi><id>95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB/fulltext/pdf</uri></json:item><json:item><original>true</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB/fulltext/txt</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1982</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids</title><author><persName><forename type="first">Y.</forename><surname>Fujii</surname></persName><affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</affiliation></author><author><persName><forename type="first">H.</forename><surname>Higashi</surname></persName><affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</affiliation></author><author><persName><forename type="first">K.</forename><surname>Ikuta</surname></persName><affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</affiliation></author><author><persName><forename type="first">S.</forename><surname>Kato</surname></persName><affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</affiliation></author><author><persName><forename type="first">M.</forename><surname>Naiki</surname></persName><affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</affiliation></author></analytic><monogr><title level="j">Molecular Immunology</title><title level="j" type="abbrev">MIMM</title><idno type="pISSN">0161-5890</idno><idno type="PII">S0161-5890(00)X0139-3</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1981"></date><biblScope unit="volume">19</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="87">87</biblScope><biblScope unit="page" to="94">94</biblScope></imprint></monogr><idno type="istex">95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB</idno><idno type="DOI">10.1016/0161-5890(82)90250-4</idno><idno type="PII">0161-5890(82)90250-4</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1982</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The precise specificities of human H-D antibodies and newly obtained avian antisera to the H-D antigen-active glycosphingolipids, N-glycolylneuraminyl(α2–3)lactosyl ceramide (hematoside) and N-glycolylneuraminyl(α2–3)lactoneotetraosyl ceramide (sialosylparagloboside) were compared by gel precipitation and hemagglutination inhibition using other gangliosides with a related structure and chemically modified hematoside derivatives and the oligosaccharides from both the antigenic glycosphingolipids. Human H-D antibodies were found to have the same affinity for both antigenic glycosphingolipids; however, the avian anti-hematoside or anti-sialosylparaglobosides showed a higher affinity for the homologous antigen. Human H-D antibodies were directed more exactly toward the terminal sialic acid residue and more roughly to the hydrophobic portion of both compounds; however, the two avian antibodies were directed more specifically to the whole structure of the homologous antigen glycosphingolipid.</p></abstract></profileDesc><revisionDesc><change when="1981-05-05">Registration</change><change when="1981">Published</change></revisionDesc></teiHeader></istex:fulltextTEI></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"><item-info><jid>MIMM</jid><aid>82902504</aid><ce:pii>0161-5890(82)90250-4</ce:pii><ce:doi>10.1016/0161-5890(82)90250-4</ce:doi><ce:copyright type="unknown" year="1982"></ce:copyright></item-info><head><ce:title>Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids</ce:title><ce:author-group><ce:author><ce:given-name>Y.</ce:given-name><ce:surname>Fujii</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>H.</ce:given-name><ce:surname>Higashi</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>K.</ce:given-name><ce:surname>Ikuta</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>S.</ce:given-name><ce:surname>Kato</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Naiki</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>∗</ce:label><ce:textfn>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>†</ce:label><ce:textfn>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="9" month="12" year="1980"></ce:date-received><ce:date-accepted day="5" month="5" year="1981"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The precise specificities of human H-D antibodies and newly obtained avian antisera to the H-D antigen-active glycosphingolipids, <ce:italic>N</ce:italic>-glycolylneuraminyl(α2–3)lactosyl ceramide (hematoside) and <ce:italic>N</ce:italic>-glycolylneuraminyl(α2–3)lactoneotetraosyl ceramide (sialosylparagloboside) were compared by gel precipitation and hemagglutination inhibition using other gangliosides with a related structure and chemically modified hematoside derivatives and the oligosaccharides from both the antigenic glycosphingolipids. Human H-D antibodies were found to have the same affinity for both antigenic glycosphingolipids; however, the avian anti-hematoside or anti-sialosylparaglobosides showed a higher affinity for the homologous antigen. Human H-D antibodies were directed more exactly toward the terminal sialic acid residue and more roughly to the hydrophobic portion of both compounds; however, the two avian antibodies were directed more specifically to the whole structure of the homologous antigen glycosphingolipid.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Specificities of human heterophilic Hanganutziu and Deicher (H-D) antibodies and avian antisera against H-D antigen-active glycosphingolipids</title></titleInfo><name type="personal"><namePart type="given">Y.</namePart><namePart type="family">Fujii</namePart><affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Higashi</namePart><affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">K.</namePart><namePart type="family">Ikuta</namePart><affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Kato</namePart><affiliation>Department of Pathology, Research Institute for Microbiol Disease, Osaka University. Osaka 565, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Naiki</namePart><affiliation>Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan</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">1981</dateIssued><dateValid encoding="w3cdtf">1981-05-05</dateValid><copyrightDate encoding="w3cdtf">1982</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">The precise specificities of human H-D antibodies and newly obtained avian antisera to the H-D antigen-active glycosphingolipids, N-glycolylneuraminyl(α2–3)lactosyl ceramide (hematoside) and N-glycolylneuraminyl(α2–3)lactoneotetraosyl ceramide (sialosylparagloboside) were compared by gel precipitation and hemagglutination inhibition using other gangliosides with a related structure and chemically modified hematoside derivatives and the oligosaccharides from both the antigenic glycosphingolipids. Human H-D antibodies were found to have the same affinity for both antigenic glycosphingolipids; however, the avian anti-hematoside or anti-sialosylparaglobosides showed a higher affinity for the homologous antigen. Human H-D antibodies were directed more exactly toward the terminal sialic acid residue and more roughly to the hydrophobic portion of both compounds; however, the two avian antibodies were directed more specifically to the whole structure of the homologous antigen glycosphingolipid.</abstract><relatedItem type="host"><titleInfo><title>Molecular Immunology</title></titleInfo><titleInfo type="abbreviated"><title>MIMM</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">198201</dateIssued></originInfo><identifier type="ISSN">0161-5890</identifier><identifier type="PII">S0161-5890(00)X0139-3</identifier><part><date>198201</date><detail type="volume"><number>19</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>191</end></extent><extent unit="pages"><start>87</start><end>94</end></extent></part></relatedItem><identifier type="istex">95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB</identifier><identifier type="DOI">10.1016/0161-5890(82)90250-4</identifier><identifier type="PII">0161-5890(82)90250-4</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/95B29D1CBEDAA8C007A804DA6E8535A8FF0643BB/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">IMMUNOLOGY</classCode><classCode scheme="WOS">BIOCHEMISTRY & MOLECULAR BIOLOGY</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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