Characterization of an Agrobacterium tumefaciens lectin.
Identifieur interne : 004C34 ( Main/Corpus ); précédent : 004C33; suivant : 004C35Characterization of an Agrobacterium tumefaciens lectin.
Auteurs : C. Depierreux ; H C Kang ; B. Guérin ; M. Monsigny ; F. DelmotteSource :
- Glycobiology [ 0959-6658 ] ; 1991.
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
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pubmed:1822244Le document en format XML
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<author><name sortKey="Depierreux, C" sort="Depierreux, C" uniqKey="Depierreux C" first="C" last="Depierreux">C. Depierreux</name>
<affiliation><nlm:affiliation>Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans, France.</nlm:affiliation>
</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. Monsigny</name>
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<author><name sortKey="Delmotte, F" sort="Delmotte, F" uniqKey="Delmotte F" first="F" last="Delmotte">F. Delmotte</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Characterization of an Agrobacterium tumefaciens lectin.</title>
<author><name sortKey="Depierreux, C" sort="Depierreux, C" uniqKey="Depierreux C" first="C" last="Depierreux">C. Depierreux</name>
<affiliation><nlm:affiliation>Département de Biochimie des Glycoconjugués et Lectines Endogènes, Centre de Biophysique Moléculaire, C.N.R.S., Orléans, France.</nlm:affiliation>
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<author><name sortKey="Kang, H C" sort="Kang, H C" uniqKey="Kang H" first="H C" last="Kang">H C Kang</name>
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<author><name sortKey="Guerin, B" sort="Guerin, B" uniqKey="Guerin B" first="B" last="Guérin">B. Guérin</name>
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<author><name sortKey="Monsigny, M" sort="Monsigny, M" uniqKey="Monsigny M" first="M" last="Monsigny">M. Monsigny</name>
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<author><name sortKey="Delmotte, F" sort="Delmotte, F" uniqKey="Delmotte F" first="F" last="Delmotte">F. Delmotte</name>
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<series><title level="j">Glycobiology</title>
<idno type="ISSN">0959-6658</idno>
<imprint><date when="1991" type="published">1991</date>
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<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="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Carbohydrates</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Hemagglutination</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" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycoproteins</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>
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<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>
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<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1822244</PMID>
<DateCompleted><Year>1992</Year>
<Month>09</Month>
<Day>01</Day>
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<DateRevised><Year>2019</Year>
<Month>05</Month>
<Day>10</Day>
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<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>
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<Title>Glycobiology</Title>
<ISOAbbreviation>Glycobiology</ISOAbbreviation>
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<ArticleTitle>Characterization of an Agrobacterium tumefaciens lectin.</ArticleTitle>
<Pagination><MedlinePgn>643-9</MedlinePgn>
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<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>
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