Characterization of an Agrobacterium tumefaciens lectin.
Identifieur interne : 004C60 ( Main/Exploration ); précédent : 004C59; suivant : 004C61Characterization of an Agrobacterium tumefaciens lectin.
Auteurs : C. Depierreux [France] ; H C Kang ; B. Guérin ; M. Monsigny ; F. DelmotteSource :
- Glycobiology [ 0959-6658 ] ; 1991.
Descripteurs français
- KwdFr :
- Agrobacterium tumefaciens (immunologie), Animaux (MeSH), Arbres (MeSH), Chromatographie d'affinité (MeSH), Extraits de plantes (MeSH), Focalisation isoélectrique (MeSH), Glucides (analyse), Glycoprotéines (métabolisme), Humains (MeSH), Hémagglutination (effets des médicaments et des substances chimiques), Lectines (isolement et purification), Lectines végétales (MeSH), Masse moléculaire (MeSH), Polyosides (pharmacologie), Spectrométrie de fluorescence (MeSH), Suidae (MeSH), Tests d'inhibition de l'hémagglutination (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- analyse : Glucides.
- effets des médicaments et des substances chimiques : Hémagglutination.
- immunologie : Agrobacterium tumefaciens.
- isolement et purification : Lectines.
- métabolisme : Glycoprotéines.
- pharmacologie : Polyosides.
- Animaux, Arbres, Chromatographie d'affinité, Extraits de plantes, Focalisation isoélectrique, Humains, Lectines végétales, Masse moléculaire, Spectrométrie de fluorescence, Suidae, Tests d'inhibition de l'hémagglutination, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Agrobacterium tumefaciens (immunology), Animals (MeSH), Carbohydrates (analysis), Chromatography, Affinity (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Glycoproteins (metabolism), Hemagglutination (drug effects), Hemagglutination Inhibition Tests (MeSH), Humans (MeSH), Isoelectric Focusing (MeSH), Lectins (isolation & purification), Molecular Weight (MeSH), Plant Extracts (MeSH), Plant Lectins (MeSH), Polysaccharides (pharmacology), Spectrometry, Fluorescence (MeSH), Swine (MeSH), Trees (MeSH).
- MESH :
- chemical , analysis : Carbohydrates.
- drug effects : Hemagglutination.
- immunology : Agrobacterium tumefaciens.
- chemical , isolation & purification : Lectins.
- chemical , metabolism : Glycoproteins.
- chemical , pharmacology : Polysaccharides.
- Animals, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Hemagglutination Inhibition Tests, Humans, Isoelectric Focusing, Molecular Weight, Plant Extracts, Plant Lectins, Spectrometry, Fluorescence, Swine, Trees.
Abstract
An Agrobacterium tumefaciens suspension induces a strong agglutination of aldehyde-fixed pig erythrocytes at pH 5.0. The agglutination is inhibited by some polysaccharides, such as fucoidin, and also when the pH is raised to 7.0. Lectins (sugar-binding proteins) associated with the bacterial cell wall of A. tumefaciens strain 84.5 were directly evidenced by spectrofluorimetry using fluoresceinylated neoglycoproteins. The specific binding of the fluorescein-labelled neoglycoprotein bearing alpha-L-fucoside residues was also optimal at pH 5.0. A lectin was purified by affinity chromatography on agarose substituted with alpha-L-fucopyranoside. Furthermore, the haemagglutination activity of this lectin was inhibited by polysaccharides isolated from poplar leaves.
DOI: 10.1093/glycob/1.6.643
PubMed: 1822244
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Depierreux</name><affiliation wicri:level="3"><nlm:affiliation>Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans</wicri:regionArea><placeName><region type="region">Centre-Val de Loire</region><region type="old region">Région Centre</region><settlement type="city">Orléans</settlement></placeName></affiliation></author><author><name sortKey="Kang, H C" sort="Kang, H C" uniqKey="Kang H" first="H C" last="Kang">H C Kang</name></author><author><name sortKey="Guerin, B" sort="Guerin, B" uniqKey="Guerin B" first="B" last="Guérin">B. Guérin</name></author><author><name sortKey="Monsigny, M" sort="Monsigny, M" uniqKey="Monsigny M" first="M" last="Monsigny">M. 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Depierreux</name><affiliation wicri:level="3"><nlm:affiliation>Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans</wicri:regionArea><placeName><region type="region">Centre-Val de Loire</region><region type="old region">Région Centre</region><settlement type="city">Orléans</settlement></placeName></affiliation></author><author><name sortKey="Kang, H C" sort="Kang, H C" uniqKey="Kang H" first="H C" last="Kang">H C Kang</name></author><author><name sortKey="Guerin, B" sort="Guerin, B" uniqKey="Guerin B" first="B" last="Guérin">B. Guérin</name></author><author><name sortKey="Monsigny, M" sort="Monsigny, M" uniqKey="Monsigny M" first="M" last="Monsigny">M. 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Delmotte</name></author></analytic><series><title level="j">Glycobiology</title><idno type="ISSN">0959-6658</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agrobacterium tumefaciens (immunology)</term><term>Animals (MeSH)</term><term>Carbohydrates (analysis)</term><term>Chromatography, Affinity (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Glycoproteins (metabolism)</term><term>Hemagglutination (drug effects)</term><term>Hemagglutination Inhibition Tests (MeSH)</term><term>Humans (MeSH)</term><term>Isoelectric Focusing (MeSH)</term><term>Lectins (isolation & purification)</term><term>Molecular Weight (MeSH)</term><term>Plant Extracts (MeSH)</term><term>Plant Lectins (MeSH)</term><term>Polysaccharides (pharmacology)</term><term>Spectrometry, Fluorescence (MeSH)</term><term>Swine (MeSH)</term><term>Trees (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agrobacterium tumefaciens (immunologie)</term><term>Animaux (MeSH)</term><term>Arbres (MeSH)</term><term>Chromatographie d'affinité (MeSH)</term><term>Extraits de plantes (MeSH)</term><term>Focalisation isoélectrique (MeSH)</term><term>Glucides (analyse)</term><term>Glycoprotéines (métabolisme)</term><term>Humains (MeSH)</term><term>Hémagglutination (effets des médicaments et des substances chimiques)</term><term>Lectines (isolement et purification)</term><term>Lectines végétales (MeSH)</term><term>Masse moléculaire (MeSH)</term><term>Polyosides (pharmacologie)</term><term>Spectrométrie de fluorescence (MeSH)</term><term>Suidae (MeSH)</term><term>Tests d'inhibition de l'hémagglutination (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Carbohydrates</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Glucides</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Hemagglutination</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Hémagglutination</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Agrobacterium tumefaciens</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Agrobacterium tumefaciens</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Lectins</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Lectines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycoproteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Polyosides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Polysaccharides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chromatography, Affinity</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Hemagglutination Inhibition Tests</term><term>Humans</term><term>Isoelectric Focusing</term><term>Molecular Weight</term><term>Plant Extracts</term><term>Plant Lectins</term><term>Spectrometry, Fluorescence</term><term>Swine</term><term>Trees</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Arbres</term><term>Chromatographie d'affinité</term><term>Extraits de plantes</term><term>Focalisation isoélectrique</term><term>Humains</term><term>Lectines végétales</term><term>Masse moléculaire</term><term>Spectrométrie de fluorescence</term><term>Suidae</term><term>Tests d'inhibition de l'hémagglutination</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An Agrobacterium tumefaciens suspension induces a strong agglutination of aldehyde-fixed pig erythrocytes at pH 5.0. The agglutination is inhibited by some polysaccharides, such as fucoidin, and also when the pH is raised to 7.0. Lectins (sugar-binding proteins) associated with the bacterial cell wall of A. tumefaciens strain 84.5 were directly evidenced by spectrofluorimetry using fluoresceinylated neoglycoproteins. The specific binding of the fluorescein-labelled neoglycoprotein bearing alpha-L-fucoside residues was also optimal at pH 5.0. A lectin was purified by affinity chromatography on agarose substituted with alpha-L-fucopyranoside. Furthermore, the haemagglutination activity of this lectin was inhibited by polysaccharides isolated from poplar leaves.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1822244</PMID><DateCompleted><Year>1992</Year><Month>09</Month><Day>01</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0959-6658</ISSN><JournalIssue CitedMedium="Print"><Volume>1</Volume><Issue>6</Issue><PubDate><Year>1991</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Glycobiology</Title><ISOAbbreviation>Glycobiology</ISOAbbreviation></Journal><ArticleTitle>Characterization of an Agrobacterium tumefaciens lectin.</ArticleTitle><Pagination><MedlinePgn>643-9</MedlinePgn></Pagination><Abstract><AbstractText>An Agrobacterium tumefaciens suspension induces a strong agglutination of aldehyde-fixed pig erythrocytes at pH 5.0. The agglutination is inhibited by some polysaccharides, such as fucoidin, and also when the pH is raised to 7.0. Lectins (sugar-binding proteins) associated with the bacterial cell wall of A. tumefaciens strain 84.5 were directly evidenced by spectrofluorimetry using fluoresceinylated neoglycoproteins. The specific binding of the fluorescein-labelled neoglycoprotein bearing alpha-L-fucoside residues was also optimal at pH 5.0. A lectin was purified by affinity chromatography on agarose substituted with alpha-L-fucopyranoside. Furthermore, the haemagglutination activity of this lectin was inhibited by polysaccharides isolated from poplar leaves.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Depierreux</LastName><ForeName>C</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kang</LastName><ForeName>H C</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Guérin</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Monsigny</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Delmotte</LastName><ForeName>F</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Glycobiology</MedlineTA><NlmUniqueID>9104124</NlmUniqueID><ISSNLinking>0959-6658</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002241">Carbohydrates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006023">Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037102">Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010936">Plant Extracts</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037121">Plant Lectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016960" MajorTopicYN="N">Agrobacterium tumefaciens</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002241" MajorTopicYN="N">Carbohydrates</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002846" MajorTopicYN="N">Chromatography, Affinity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006023" MajorTopicYN="N">Glycoproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006384" MajorTopicYN="Y">Hemagglutination</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006385" MajorTopicYN="N">Hemagglutination Inhibition Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037102" MajorTopicYN="N">Lectins</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010936" MajorTopicYN="N">Plant Extracts</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037121" MajorTopicYN="N">Plant Lectins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>12</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>12</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>12</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1822244</ArticleId><ArticleId IdType="doi">10.1093/glycob/1.6.643</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Centre-Val de Loire</li><li>Région Centre</li></region><settlement><li>Orléans</li></settlement></list><tree><noCountry><name sortKey="Delmotte, F" sort="Delmotte, F" uniqKey="Delmotte F" first="F" last="Delmotte">F. Delmotte</name><name sortKey="Guerin, B" sort="Guerin, B" uniqKey="Guerin B" first="B" last="Guérin">B. Guérin</name><name sortKey="Kang, H C" sort="Kang, H C" uniqKey="Kang H" first="H C" last="Kang">H C Kang</name><name sortKey="Monsigny, M" sort="Monsigny, M" uniqKey="Monsigny M" first="M" last="Monsigny">M. Monsigny</name></noCountry><country name="France"><region name="Centre-Val de Loire"><name sortKey="Depierreux, C" sort="Depierreux, C" uniqKey="Depierreux C" first="C" last="Depierreux">C. Depierreux</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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