Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts
Concanavalin A, the lectin from Canavalia ensiformis, develops arginase activity depending on Mn 2+. The cation cannot be substituted by Ca 2+ which, in addition, inhibits Mn 2+-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated f...
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| Veröffentlicht in: | Plant physiology and biochemistry 2004-12, Vol.42 (10), p.773-779 |
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| container_title | Plant physiology and biochemistry |
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| creator | Fontaniella, Blanca Millanes, Ana-María Vicente, Carlos Legaz, María-Estrella |
| description | Concanavalin A, the lectin from
Canavalia ensiformis, develops arginase activity depending on Mn
2+. The cation cannot be substituted by Ca
2+ which, in addition, inhibits Mn
2+-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated from
Evernia prunastri and
Xanthoria parietina thalli. This binding involves a ligand, probably a glycoprotein containing mannose, which can be isolated by affinity chromatography. Analysis by SDS-PAGE reveals that the ligand is a dimeric protein composed by two monomers of 54 and 48 kDa. This ligand shows to be different from the receptor for natural lichen lectins, previously identified as a polygalactosylated urease. |
| doi_str_mv | 10.1016/j.plaphy.2004.09.003 |
| format | Article |
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Canavalia ensiformis, develops arginase activity depending on Mn
2+. The cation cannot be substituted by Ca
2+ which, in addition, inhibits Mn
2+-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated from
Evernia prunastri and
Xanthoria parietina thalli. This binding involves a ligand, probably a glycoprotein containing mannose, which can be isolated by affinity chromatography. Analysis by SDS-PAGE reveals that the ligand is a dimeric protein composed by two monomers of 54 and 48 kDa. This ligand shows to be different from the receptor for natural lichen lectins, previously identified as a polygalactosylated urease.</description><identifier>ISSN: 0981-9428</identifier><identifier>EISSN: 1873-2690</identifier><identifier>DOI: 10.1016/j.plaphy.2004.09.003</identifier><identifier>PMID: 15596096</identifier><identifier>CODEN: PPBIEX</identifier><language>eng</language><publisher>Paris: Elsevier Masson SAS</publisher><subject>Biological and medical sciences ; Canavalia ensiformis ; Cell biochemistry ; Cell physiology ; Cell wall ; Cell Wall - metabolism ; Chromatography, Affinity ; Concanavalin A ; Concanavalin A - metabolism ; Electrophoresis, Polyacrylamide Gel ; Evernia prunastri ; Fundamental and applied biological sciences. Psychology ; Lectin ligand ; Lichens - metabolism ; Ligands ; Mannose - metabolism ; Phycobiont ; Plant physiology and development ; Plant Proteins - metabolism ; Protein Binding ; Xanthoria parietina</subject><ispartof>Plant physiology and biochemistry, 2004-12, Vol.42 (10), p.773-779</ispartof><rights>2004 Elsevier SAS</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-77440c2554bd02d5a4c381a8ac996f881cf2f5172e2e96cc17ec7c20e2b9e283</citedby><cites>FETCH-LOGICAL-c421t-77440c2554bd02d5a4c381a8ac996f881cf2f5172e2e96cc17ec7c20e2b9e283</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.plaphy.2004.09.003$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16338751$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15596096$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fontaniella, Blanca</creatorcontrib><creatorcontrib>Millanes, Ana-María</creatorcontrib><creatorcontrib>Vicente, Carlos</creatorcontrib><creatorcontrib>Legaz, María-Estrella</creatorcontrib><title>Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts</title><title>Plant physiology and biochemistry</title><addtitle>Plant Physiol Biochem</addtitle><description>Concanavalin A, the lectin from
Canavalia ensiformis, develops arginase activity depending on Mn
2+. The cation cannot be substituted by Ca
2+ which, in addition, inhibits Mn
2+-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated from
Evernia prunastri and
Xanthoria parietina thalli. This binding involves a ligand, probably a glycoprotein containing mannose, which can be isolated by affinity chromatography. Analysis by SDS-PAGE reveals that the ligand is a dimeric protein composed by two monomers of 54 and 48 kDa. This ligand shows to be different from the receptor for natural lichen lectins, previously identified as a polygalactosylated urease.</description><subject>Biological and medical sciences</subject><subject>Canavalia ensiformis</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>Cell wall</subject><subject>Cell Wall - metabolism</subject><subject>Chromatography, Affinity</subject><subject>Concanavalin A</subject><subject>Concanavalin A - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Evernia prunastri</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Lectin ligand</subject><subject>Lichens - metabolism</subject><subject>Ligands</subject><subject>Mannose - metabolism</subject><subject>Phycobiont</subject><subject>Plant physiology and development</subject><subject>Plant Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Xanthoria parietina</subject><issn>0981-9428</issn><issn>1873-2690</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v1DAQxS0EotvCN0DIF7gl2E7iPxekagUUqRKX3q3JZNL1KrGXOFvUb49Xu1JvcJk5zO-Nnt5j7IMUtRRSf9nXhwkOu-daCdHWwtVCNK_YRlrTVEo78ZpthLOycq2yV-w6570QQrWmecuuZNc5LZzeML9NESHCE0wh8lvehzhkviYOfIYYU6YKU1whxBAf-RQeIQ68kOuOONI08T9QRhp5TjOVO-4o8uIKUx-KLr9jb0aYMr2_7Bv28P3bw_auuv_14-f29r7CVsm1MqZtBaqua_tBqKGDFhsrwQI6p0drJY5q7KRRpMhpRGkIDSpBqnekbHPDPp_fHpb0-0h59XPIJ38QKR2z10aapjPyv6A0VhVWF7A9g7iknBca_WEJMyzPXgp_KsDv_bkAfyrAC-dLAUX28fL_2M80vIguiRfg0wWAjDCNC0QM-YXTTWNNdzL69cxRSe0p0OIzBopIQ1gIVz-k8G8nfwHmsKW9</recordid><startdate>20041201</startdate><enddate>20041201</enddate><creator>Fontaniella, Blanca</creator><creator>Millanes, Ana-María</creator><creator>Vicente, Carlos</creator><creator>Legaz, María-Estrella</creator><general>Elsevier Masson SAS</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20041201</creationdate><title>Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts</title><author>Fontaniella, Blanca ; Millanes, Ana-María ; Vicente, Carlos ; Legaz, María-Estrella</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c421t-77440c2554bd02d5a4c381a8ac996f881cf2f5172e2e96cc17ec7c20e2b9e283</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Biological and medical sciences</topic><topic>Canavalia ensiformis</topic><topic>Cell biochemistry</topic><topic>Cell physiology</topic><topic>Cell wall</topic><topic>Cell Wall - metabolism</topic><topic>Chromatography, Affinity</topic><topic>Concanavalin A</topic><topic>Concanavalin A - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Evernia prunastri</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Lectin ligand</topic><topic>Lichens - metabolism</topic><topic>Ligands</topic><topic>Mannose - metabolism</topic><topic>Phycobiont</topic><topic>Plant physiology and development</topic><topic>Plant Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Xanthoria parietina</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fontaniella, Blanca</creatorcontrib><creatorcontrib>Millanes, Ana-María</creatorcontrib><creatorcontrib>Vicente, Carlos</creatorcontrib><creatorcontrib>Legaz, María-Estrella</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>Plant physiology and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fontaniella, Blanca</au><au>Millanes, Ana-María</au><au>Vicente, Carlos</au><au>Legaz, María-Estrella</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts</atitle><jtitle>Plant physiology and biochemistry</jtitle><addtitle>Plant Physiol Biochem</addtitle><date>2004-12-01</date><risdate>2004</risdate><volume>42</volume><issue>10</issue><spage>773</spage><epage>779</epage><pages>773-779</pages><issn>0981-9428</issn><eissn>1873-2690</eissn><coden>PPBIEX</coden><abstract>Concanavalin A, the lectin from
Canavalia ensiformis, develops arginase activity depending on Mn
2+. The cation cannot be substituted by Ca
2+ which, in addition, inhibits Mn
2+-supported activity. Fluorescein-labeled Concanavalin A is able to bind to the cell wall of algal cells recently isolated from
Evernia prunastri and
Xanthoria parietina thalli. This binding involves a ligand, probably a glycoprotein containing mannose, which can be isolated by affinity chromatography. Analysis by SDS-PAGE reveals that the ligand is a dimeric protein composed by two monomers of 54 and 48 kDa. This ligand shows to be different from the receptor for natural lichen lectins, previously identified as a polygalactosylated urease.</abstract><cop>Paris</cop><pub>Elsevier Masson SAS</pub><pmid>15596096</pmid><doi>10.1016/j.plaphy.2004.09.003</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0981-9428 |
| ispartof | Plant physiology and biochemistry, 2004-12, Vol.42 (10), p.773-779 |
| issn | 0981-9428 1873-2690 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Biological and medical sciences Canavalia ensiformis Cell biochemistry Cell physiology Cell wall Cell Wall - metabolism Chromatography, Affinity Concanavalin A Concanavalin A - metabolism Electrophoresis, Polyacrylamide Gel Evernia prunastri Fundamental and applied biological sciences. Psychology Lectin ligand Lichens - metabolism Ligands Mannose - metabolism Phycobiont Plant physiology and development Plant Proteins - metabolism Protein Binding Xanthoria parietina |
| title | Concanavalin A binds to a mannose-containing ligand in the cell wall of some lichen phycobionts |
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