Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium
A novel plant lectin has been isolated from the rhizomes of Calystegia sepium (hedge bindweed) and partially characterized. The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16 kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited b...
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| Veröffentlicht in: | Glycoconjugate journal 1997-02, Vol.14 (2), p.259-265 |
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| container_title | Glycoconjugate journal |
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| creator | Peumans, W J Winter, H C Bemer, V Van Leuven, F Goldstein, I J Truffa-Bachi, P Van Damme, E J |
| description | A novel plant lectin has been isolated from the rhizomes of Calystegia sepium (hedge bindweed) and partially characterized. The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16 kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited by maltose and mannose and hence exhibits a sugar binding specificity that differs in some respects from that of all previously isolated plant lectins. Mitogenicity tests have shown that the Calystegia lectin is a powerful T-cell mitogen. Affinity purification of human, plant and fungal glycoproteins on immobilized C. sepium lectin demonstrates that this novel lectin can be used for the isolation of glycoconjugates from various sources. Moreover, it can be expected that by virtue of its distinct specificity, the new lectin will become an important tool in glycobiology. |
| doi_str_mv | 10.1023/A:1018502107707 |
| format | Article |
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The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16 kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited by maltose and mannose and hence exhibits a sugar binding specificity that differs in some respects from that of all previously isolated plant lectins. Mitogenicity tests have shown that the Calystegia lectin is a powerful T-cell mitogen. Affinity purification of human, plant and fungal glycoproteins on immobilized C. sepium lectin demonstrates that this novel lectin can be used for the isolation of glycoconjugates from various sources. Moreover, it can be expected that by virtue of its distinct specificity, the new lectin will become an important tool in glycobiology.</description><identifier>ISSN: 0282-0080</identifier><identifier>EISSN: 1573-4986</identifier><identifier>DOI: 10.1023/A:1018502107707</identifier><identifier>PMID: 9111143</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Agglutination ; Agglutination Tests ; Amino Acid Sequence ; Amino Acids - analysis ; Animals ; Carbohydrate Metabolism ; Chromatography, Affinity - methods ; Dose-Response Relationship, Drug ; Erythrocytes - drug effects ; Erythrocytes - metabolism ; Fungal Proteins - chemistry ; Fungal Proteins - metabolism ; Glycoproteins - chemistry ; Glycoproteins - metabolism ; Hemagglutination ; Humans ; Lectins - isolation & purification ; Lectins - metabolism ; Lectins - pharmacology ; Lymphocytes - drug effects ; Mice ; Mice, Inbred BALB C ; Molecular biology ; Molecular Sequence Data ; Plant biology ; Plant Lectins ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plants - chemistry ; Proteins ; Rabbits ; Spleen - drug effects ; Substrate Specificity</subject><ispartof>Glycoconjugate journal, 1997-02, Vol.14 (2), p.259-265</ispartof><rights>Chapman and Hall 1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c320t-a2952fc822daa5150f39ef8348d29583d4d0b6a1b2a122e26a0793399f9c584c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9111143$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Peumans, W J</creatorcontrib><creatorcontrib>Winter, H C</creatorcontrib><creatorcontrib>Bemer, V</creatorcontrib><creatorcontrib>Van Leuven, F</creatorcontrib><creatorcontrib>Goldstein, I J</creatorcontrib><creatorcontrib>Truffa-Bachi, P</creatorcontrib><creatorcontrib>Van Damme, E J</creatorcontrib><title>Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium</title><title>Glycoconjugate journal</title><addtitle>Glycoconj J</addtitle><description>A novel plant lectin has been isolated from the rhizomes of Calystegia sepium (hedge bindweed) and partially characterized. The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16 kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited by maltose and mannose and hence exhibits a sugar binding specificity that differs in some respects from that of all previously isolated plant lectins. Mitogenicity tests have shown that the Calystegia lectin is a powerful T-cell mitogen. Affinity purification of human, plant and fungal glycoproteins on immobilized C. sepium lectin demonstrates that this novel lectin can be used for the isolation of glycoconjugates from various sources. Moreover, it can be expected that by virtue of its distinct specificity, the new lectin will become an important tool in glycobiology.</description><subject>Agglutination</subject><subject>Agglutination Tests</subject><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Carbohydrate Metabolism</subject><subject>Chromatography, Affinity - methods</subject><subject>Dose-Response Relationship, Drug</subject><subject>Erythrocytes - drug effects</subject><subject>Erythrocytes - metabolism</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - metabolism</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - metabolism</subject><subject>Hemagglutination</subject><subject>Humans</subject><subject>Lectins - isolation & purification</subject><subject>Lectins - metabolism</subject><subject>Lectins - pharmacology</subject><subject>Lymphocytes - drug effects</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Plant biology</subject><subject>Plant Lectins</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plants - chemistry</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Spleen - drug effects</subject><subject>Substrate Specificity</subject><issn>0282-0080</issn><issn>1573-4986</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNpdkD1PwzAYhC0EKqUwMyFZDGyB13YS22xVxUelSixljlzHBldOHGIb1H9PJDpxyw336HQ6hK4J3BOg7GH5SICICigBzoGfoDmpOCtKKepTNAcqaAEg4BxdxLgHAF5SMUMzSSaVbI626xi8Si70OFiscB--jceDV33C3ujkevzj0idWPc59jll5HAejnXXapQO2Y-jwSvlDTObDKRzN4HJ3ic6s8tFcHX2B3p-ftqvXYvP2sl4tN4VmFFKhqKyo1YLSVqmKVGCZNFawUrRTIlhbtrCrFdlRRSg1tFbAJWNSWqkrUWq2QHd_vcMYvrKJqelc1MZP603IseFC1hyEnMDbf-A-5LGftjW8ZkQQqMkE3RyhvOtM2wyj69R4aI5fsV9yMGou</recordid><startdate>19970201</startdate><enddate>19970201</enddate><creator>Peumans, W J</creator><creator>Winter, H C</creator><creator>Bemer, V</creator><creator>Van Leuven, F</creator><creator>Goldstein, I J</creator><creator>Truffa-Bachi, P</creator><creator>Van Damme, E J</creator><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>19970201</creationdate><title>Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium</title><author>Peumans, W J ; Winter, H C ; Bemer, V ; Van Leuven, F ; Goldstein, I J ; Truffa-Bachi, P ; Van Damme, E J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c320t-a2952fc822daa5150f39ef8348d29583d4d0b6a1b2a122e26a0793399f9c584c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Agglutination</topic><topic>Agglutination Tests</topic><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Carbohydrate Metabolism</topic><topic>Chromatography, Affinity - methods</topic><topic>Dose-Response Relationship, Drug</topic><topic>Erythrocytes - drug effects</topic><topic>Erythrocytes - metabolism</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - metabolism</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - metabolism</topic><topic>Hemagglutination</topic><topic>Humans</topic><topic>Lectins - isolation & purification</topic><topic>Lectins - metabolism</topic><topic>Lectins - pharmacology</topic><topic>Lymphocytes - drug effects</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Plant biology</topic><topic>Plant Lectins</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Plants - chemistry</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Spleen - drug effects</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Peumans, W J</creatorcontrib><creatorcontrib>Winter, H C</creatorcontrib><creatorcontrib>Bemer, V</creatorcontrib><creatorcontrib>Van Leuven, F</creatorcontrib><creatorcontrib>Goldstein, I J</creatorcontrib><creatorcontrib>Truffa-Bachi, P</creatorcontrib><creatorcontrib>Van Damme, E J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Glycoconjugate journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Peumans, W J</au><au>Winter, H C</au><au>Bemer, V</au><au>Van Leuven, F</au><au>Goldstein, I J</au><au>Truffa-Bachi, P</au><au>Van Damme, E J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium</atitle><jtitle>Glycoconjugate journal</jtitle><addtitle>Glycoconj J</addtitle><date>1997-02-01</date><risdate>1997</risdate><volume>14</volume><issue>2</issue><spage>259</spage><epage>265</epage><pages>259-265</pages><issn>0282-0080</issn><eissn>1573-4986</eissn><abstract>A novel plant lectin has been isolated from the rhizomes of Calystegia sepium (hedge bindweed) and partially characterized. The lectin is a dimeric protein composed of two identical non-covalently linked subunits of 16 kDa. Hapten inhibition studies indicate that the novel lectin is best inhibited by maltose and mannose and hence exhibits a sugar binding specificity that differs in some respects from that of all previously isolated plant lectins. Mitogenicity tests have shown that the Calystegia lectin is a powerful T-cell mitogen. Affinity purification of human, plant and fungal glycoproteins on immobilized C. sepium lectin demonstrates that this novel lectin can be used for the isolation of glycoconjugates from various sources. Moreover, it can be expected that by virtue of its distinct specificity, the new lectin will become an important tool in glycobiology.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>9111143</pmid><doi>10.1023/A:1018502107707</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Agglutination Agglutination Tests Amino Acid Sequence Amino Acids - analysis Animals Carbohydrate Metabolism Chromatography, Affinity - methods Dose-Response Relationship, Drug Erythrocytes - drug effects Erythrocytes - metabolism Fungal Proteins - chemistry Fungal Proteins - metabolism Glycoproteins - chemistry Glycoproteins - metabolism Hemagglutination Humans Lectins - isolation & purification Lectins - metabolism Lectins - pharmacology Lymphocytes - drug effects Mice Mice, Inbred BALB C Molecular biology Molecular Sequence Data Plant biology Plant Lectins Plant Proteins - chemistry Plant Proteins - metabolism Plants - chemistry Proteins Rabbits Spleen - drug effects Substrate Specificity |
| title | Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium |
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