A mitogenic agglutinin from the red alga Carpopeltis flabellata
Identifieur interne : 002C00 ( Istex/Corpus ); précédent : 002B99; suivant : 002C01A mitogenic agglutinin from the red alga Carpopeltis flabellata
Auteurs : Kanji Hori ; Haruo Matsuda ; Keisuke Miyazawa ; Keiji ItoSource :
- Phytochemistry [ 0031-9422 ] ; 1986.
Abstract
An agglutinin has been isolated from the marine red alga Carpopeltis flabellata by ammonium sulphate fractionation, affinity chromatography on a yeast mannan-Sepharose 4B column and gel permeation HPLC. This new protein, designated carnin, is a monomeric glycoprotein with a Mr of 25 000, and it contains large amounts of Gly and Asx. It strongly agglutinated untreated rabbit, mouse and horse erythrocytes, and very weakly untreated human erythrocytes, whereas it did not agglutinate untreated sheep and chicken erythrocytes. Treatment of the erythrocytes with trypsin affected their sensitivity to haemagglutination by the agglutinin. The haemagglutinating activity was inhibited only by glycoproteins with N-glycosidic sugar chains. The activity was not affected by divalent cations. Carnin also showed mitogenic activity for T lymphocytes from mouse spleen. It inhibited the normal embryonic development of marine invertebrates.
Url:
DOI: 10.1016/S0031-9422(00)81807-5
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This new protein, designated carnin, is a monomeric glycoprotein with a Mr of 25 000, and it contains large amounts of Gly and Asx. It strongly agglutinated untreated rabbit, mouse and horse erythrocytes, and very weakly untreated human erythrocytes, whereas it did not agglutinate untreated sheep and chicken erythrocytes. Treatment of the erythrocytes with trypsin affected their sensitivity to haemagglutination by the agglutinin. The haemagglutinating activity was inhibited only by glycoproteins with N-glycosidic sugar chains. The activity was not affected by divalent cations. Carnin also showed mitogenic activity for T lymphocytes from mouse spleen. It inhibited the normal embryonic development of marine invertebrates.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Kanji Hori</name><affiliations><json:string>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</json:string></affiliations></json:item><json:item><name>Haruo Matsuda</name><affiliations><json:string>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</json:string></affiliations></json:item><json:item><name>Keisuke Miyazawa</name><affiliations><json:string>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</json:string></affiliations></json:item><json:item><name>Keiji Ito</name><affiliations><json:string>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Carpopeltis flabellata</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>grateloupiaceae</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>agglutinin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>mitogen</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>glycoprotein</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>isolation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>sugar-binding specificity</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>biological activity.</value></json:item></subject><language><json:string>eng</json:string></language><abstract>An agglutinin has been isolated from the marine red alga Carpopeltis flabellata by ammonium sulphate fractionation, affinity chromatography on a yeast mannan-Sepharose 4B column and gel permeation HPLC. This new protein, designated carnin, is a monomeric glycoprotein with a Mr of 25 000, and it contains large amounts of Gly and Asx. It strongly agglutinated untreated rabbit, mouse and horse erythrocytes, and very weakly untreated human erythrocytes, whereas it did not agglutinate untreated sheep and chicken erythrocytes. Treatment of the erythrocytes with trypsin affected their sensitivity to haemagglutination by the agglutinin. The haemagglutinating activity was inhibited only by glycoproteins with N-glycosidic sugar chains. The activity was not affected by divalent cations. Carnin also showed mitogenic activity for T lymphocytes from mouse spleen. 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This new protein, designated carnin, is a monomeric glycoprotein with a Mr of 25 000, and it contains large amounts of Gly and Asx. It strongly agglutinated untreated rabbit, mouse and horse erythrocytes, and very weakly untreated human erythrocytes, whereas it did not agglutinate untreated sheep and chicken erythrocytes. Treatment of the erythrocytes with trypsin affected their sensitivity to haemagglutination by the agglutinin. The haemagglutinating activity was inhibited only by glycoproteins with N-glycosidic sugar chains. The activity was not affected by divalent cations. Carnin also showed mitogenic activity for T lymphocytes from mouse spleen. It inhibited the normal embryonic development of marine invertebrates.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Carpopeltis flabellata</term></item><item><term>grateloupiaceae</term></item><item><term>agglutinin</term></item><item><term>mitogen</term></item><item><term>glycoprotein</term></item><item><term>isolation</term></item><item><term>sugar-binding specificity</term></item><item><term>biological activity.</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1986-08-05">Received</change><change when="1986">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>PHYTO</jid><aid>00818075</aid><ce:pii>S0031-9422(00)81807-5</ce:pii><ce:doi>10.1016/S0031-9422(00)81807-5</ce:doi><ce:copyright type="unknown" year="1987"></ce:copyright></item-info><head><ce:title>A mitogenic agglutinin from the red alga <ce:italic>Carpopeltis flabellata</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>Kanji</ce:given-name><ce:surname>Hori</ce:surname></ce:author><ce:author><ce:given-name>Haruo</ce:given-name><ce:surname>Matsuda</ce:surname></ce:author><ce:author><ce:given-name>Keisuke</ce:given-name><ce:surname>Miyazawa</ce:surname></ce:author><ce:author><ce:given-name>Keiji</ce:given-name><ce:surname>Ito</ce:surname></ce:author><ce:affiliation><ce:textfn>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="5" month="8" year="1986"></ce:date-received><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>An agglutinin has been isolated from the marine red alga <ce:italic>Carpopeltis flabellata</ce:italic> by ammonium sulphate fractionation, affinity chromatography on a yeast mannan-Sepharose 4B column and gel permeation HPLC. This new protein, designated carnin, is a monomeric glycoprotein with a <ce:italic>M<ce:inf>r</ce:inf></ce:italic> of 25 000, and it contains large amounts of Gly and Asx. It strongly agglutinated untreated rabbit, mouse and horse erythrocytes, and very weakly untreated human erythrocytes, whereas it did not agglutinate untreated sheep and chicken erythrocytes. Treatment of the erythrocytes with trypsin affected their sensitivity to haemagglutination by the agglutinin. The haemagglutinating activity was inhibited only by glycoproteins with <ce:italic>N</ce:italic>-glycosidic sugar chains. The activity was not affected by divalent cations. Carnin also showed mitogenic activity for T lymphocytes from mouse spleen. It inhibited the normal embryonic development of marine invertebrates.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text><ce:italic>Carpopeltis flabellata</ce:italic></ce:text></ce:keyword><ce:keyword><ce:text>grateloupiaceae</ce:text></ce:keyword><ce:keyword><ce:text>agglutinin</ce:text></ce:keyword><ce:keyword><ce:text>mitogen</ce:text></ce:keyword><ce:keyword><ce:text>glycoprotein</ce:text></ce:keyword><ce:keyword><ce:text>isolation</ce:text></ce:keyword><ce:keyword><ce:text>sugar-binding specificity</ce:text></ce:keyword><ce:keyword><ce:text>biological activity.</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>A mitogenic agglutinin from the red alga Carpopeltis flabellata</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>A mitogenic agglutinin from the red alga</title></titleInfo><name type="personal"><namePart type="given">Kanji</namePart><namePart type="family">Hori</namePart><affiliation>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Haruo</namePart><namePart type="family">Matsuda</namePart><affiliation>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Keisuke</namePart><namePart type="family">Miyazawa</namePart><affiliation>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Keiji</namePart><namePart type="family">Ito</namePart><affiliation>Faculty of Applied Biological Science, Hiroshima University, 2-17 Midorimachi, Fukuyama 720, 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">1986</dateIssued><dateCaptured encoding="w3cdtf">1986-08-05</dateCaptured><copyrightDate encoding="w3cdtf">1987</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">An agglutinin has been isolated from the marine red alga Carpopeltis flabellata by ammonium sulphate fractionation, affinity chromatography on a yeast mannan-Sepharose 4B column and gel permeation HPLC. This new protein, designated carnin, is a monomeric glycoprotein with a Mr of 25 000, and it contains large amounts of Gly and Asx. It strongly agglutinated untreated rabbit, mouse and horse erythrocytes, and very weakly untreated human erythrocytes, whereas it did not agglutinate untreated sheep and chicken erythrocytes. Treatment of the erythrocytes with trypsin affected their sensitivity to haemagglutination by the agglutinin. The haemagglutinating activity was inhibited only by glycoproteins with N-glycosidic sugar chains. The activity was not affected by divalent cations. Carnin also showed mitogenic activity for T lymphocytes from mouse spleen. It inhibited the normal embryonic development of marine invertebrates.</abstract><subject><genre>Keywords</genre><topic>Carpopeltis flabellata</topic><topic>grateloupiaceae</topic><topic>agglutinin</topic><topic>mitogen</topic><topic>glycoprotein</topic><topic>isolation</topic><topic>sugar-binding specificity</topic><topic>biological activity.</topic></subject><relatedItem type="host"><titleInfo><title>Phytochemistry</title></titleInfo><titleInfo type="abbreviated"><title>PHYTO</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19870423</dateIssued></originInfo><identifier type="ISSN">0031-9422</identifier><identifier type="PII">S0031-9422(00)X0149-5</identifier><part><date>19870423</date><detail type="volume"><number>26</number><caption>vol.</caption></detail><detail type="issue"><number>5</number><caption>no.</caption></detail><extent unit="issue pages"><start>1237</start><end>1555</end></extent><extent unit="pages"><start>1335</start><end>1338</end></extent></part></relatedItem><identifier type="istex">E0FD9A51CC3F8A14A88AC77C19B95CCD70EA3D04</identifier><identifier type="DOI">10.1016/S0031-9422(00)81807-5</identifier><identifier type="PII">S0031-9422(00)81807-5</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/E0FD9A51CC3F8A14A88AC77C19B95CCD70EA3D04/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">BIOCHEMISTRY & MOLECULAR BIOLOGY</classCode><classCode scheme="WOS">PLANT SCIENCES</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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