Primary structures of concanavalin a-like lectins from seeds of two species of Canavalia
The amino acid sequences of two lectins from the seeds of Canavalia lineata and C. virosa have been determined by the manual Edman degradation method. Both proteins were found to be highly homologous to concanavalin A, a lectin from C. ensiformis. All the residues suggested to participate in binding...
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| Veröffentlicht in: | Phytochemistry (Oxford) 1993-07, Vol.33 (5), p.985-987 |
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| container_end_page | 987 |
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| container_title | Phytochemistry (Oxford) |
| container_volume | 33 |
| creator | Fujimura, S. Terada, S. Jayavardhanan, K.K. Panikkar, K.R. Kimoto, E. |
| description | The amino acid sequences of two lectins from the seeds of
Canavalia lineata and
C. virosa have been determined by the manual Edman degradation method. Both proteins were found to be highly homologous to concanavalin A, a lectin from
C. ensiformis. All the residues suggested to participate in binding to carbohydrates and metal ions are completely conserved in the proteins. |
| doi_str_mv | 10.1016/0031-9422(93)85008-F |
| format | Article |
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Canavalia lineata and
C. virosa have been determined by the manual Edman degradation method. Both proteins were found to be highly homologous to concanavalin A, a lectin from
C. ensiformis. All the residues suggested to participate in binding to carbohydrates and metal ions are completely conserved in the proteins.</description><identifier>ISSN: 0031-9422</identifier><identifier>EISSN: 1873-3700</identifier><identifier>DOI: 10.1016/0031-9422(93)85008-F</identifier><identifier>PMID: 7764031</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Analytical, structural and metabolic biochemistry ; binding sites ; Biological and medical sciences ; Biotechnology ; C. virosa ; Canavalia ; Canavalia cathartica ; Canavalia lineata ; Cell biochemistry ; Cell physiology ; comparisons ; concanavalin A ; Concanavalin A - chemistry ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; lectins ; Lectins - chemistry ; Lectins - isolation & purification ; Leguminosae ; Molecular Sequence Data ; Plant Lectins ; Plant physiology and development ; Proteins ; seeds ; Seeds - chemistry</subject><ispartof>Phytochemistry (Oxford), 1993-07, Vol.33 (5), p.985-987</ispartof><rights>1993</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c325t-41a7717de55cddddcab466f1c4dec757bf93c65e1d841c90aad03285f31890753</citedby><cites>FETCH-LOGICAL-c325t-41a7717de55cddddcab466f1c4dec757bf93c65e1d841c90aad03285f31890753</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/003194229385008F$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3764197$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7764031$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fujimura, S.</creatorcontrib><creatorcontrib>Terada, S.</creatorcontrib><creatorcontrib>Jayavardhanan, K.K.</creatorcontrib><creatorcontrib>Panikkar, K.R.</creatorcontrib><creatorcontrib>Kimoto, E.</creatorcontrib><title>Primary structures of concanavalin a-like lectins from seeds of two species of Canavalia</title><title>Phytochemistry (Oxford)</title><addtitle>Phytochemistry</addtitle><description>The amino acid sequences of two lectins from the seeds of
Canavalia lineata and
C. virosa have been determined by the manual Edman degradation method. Both proteins were found to be highly homologous to concanavalin A, a lectin from
C. ensiformis. All the residues suggested to participate in binding to carbohydrates and metal ions are completely conserved in the proteins.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>binding sites</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>C. virosa</subject><subject>Canavalia</subject><subject>Canavalia cathartica</subject><subject>Canavalia lineata</subject><subject>Cell biochemistry</subject><subject>Cell physiology</subject><subject>comparisons</subject><subject>concanavalin A</subject><subject>Concanavalin A - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>lectins</subject><subject>Lectins - chemistry</subject><subject>Lectins - isolation & purification</subject><subject>Leguminosae</subject><subject>Molecular Sequence Data</subject><subject>Plant Lectins</subject><subject>Plant physiology and development</subject><subject>Proteins</subject><subject>seeds</subject><subject>Seeds - chemistry</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFu1DAQhq0KVJbSNygihwrBIWUcx3FyqYRWLCBVohJU4mbN2uPKkI23dlLE2-Ntoj0yFx_-7x-NP8YuOFxx4M0HAMHLrq6qd51430qAttycsBVvlSiFAnjGVkfkBXuZ0i8AkLJpTtmpUk2dsxX7eRv9DuPfIo1xMuMUKRXBFSYMBgd8xN4PBZa9_01FT2b0QypcDLsiEdkncvwTirQn4-fiemnhK_bcYZ_ofHnP2N3m04_1l_Lm2-ev6483pRGVHMuao1JcWZLS2DwGt3XTOG5qS0ZJtXWdMI0kbtuamw4QLYiqlU7wtgMlxRl7O-_dx_AwURr1zidDfY8DhSlpJbtaqEpksJ5BE0NKkZzez1_XHPRBqD7Y0gdbuhP6Saje5NrrZf-03ZE9lhaDOb9cckwGexdxMD4dMZEx3qmMvZkxh0HjfczI3fcKuACuWlm1TSauZ4KyrUdPUacsdTBkfczmtQ3-_5f-A7Vwmxo</recordid><startdate>199307</startdate><enddate>199307</enddate><creator>Fujimura, S.</creator><creator>Terada, S.</creator><creator>Jayavardhanan, K.K.</creator><creator>Panikkar, K.R.</creator><creator>Kimoto, E.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><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>7X8</scope></search><sort><creationdate>199307</creationdate><title>Primary structures of concanavalin a-like lectins from seeds of two species of Canavalia</title><author>Fujimura, S. ; Terada, S. ; Jayavardhanan, K.K. ; Panikkar, K.R. ; Kimoto, E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c325t-41a7717de55cddddcab466f1c4dec757bf93c65e1d841c90aad03285f31890753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>binding sites</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>C. virosa</topic><topic>Canavalia</topic><topic>Canavalia cathartica</topic><topic>Canavalia lineata</topic><topic>Cell biochemistry</topic><topic>Cell physiology</topic><topic>comparisons</topic><topic>concanavalin A</topic><topic>Concanavalin A - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>lectins</topic><topic>Lectins - chemistry</topic><topic>Lectins - isolation & purification</topic><topic>Leguminosae</topic><topic>Molecular Sequence Data</topic><topic>Plant Lectins</topic><topic>Plant physiology and development</topic><topic>Proteins</topic><topic>seeds</topic><topic>Seeds - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fujimura, S.</creatorcontrib><creatorcontrib>Terada, S.</creatorcontrib><creatorcontrib>Jayavardhanan, K.K.</creatorcontrib><creatorcontrib>Panikkar, K.R.</creatorcontrib><creatorcontrib>Kimoto, E.</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fujimura, S.</au><au>Terada, S.</au><au>Jayavardhanan, K.K.</au><au>Panikkar, K.R.</au><au>Kimoto, E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Primary structures of concanavalin a-like lectins from seeds of two species of Canavalia</atitle><jtitle>Phytochemistry (Oxford)</jtitle><addtitle>Phytochemistry</addtitle><date>1993-07</date><risdate>1993</risdate><volume>33</volume><issue>5</issue><spage>985</spage><epage>987</epage><pages>985-987</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><abstract>The amino acid sequences of two lectins from the seeds of
Canavalia lineata and
C. virosa have been determined by the manual Edman degradation method. Both proteins were found to be highly homologous to concanavalin A, a lectin from
C. ensiformis. All the residues suggested to participate in binding to carbohydrates and metal ions are completely conserved in the proteins.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>7764031</pmid><doi>10.1016/0031-9422(93)85008-F</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0031-9422 |
| ispartof | Phytochemistry (Oxford), 1993-07, Vol.33 (5), p.985-987 |
| issn | 0031-9422 1873-3700 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence amino acid sequences Analytical, structural and metabolic biochemistry binding sites Biological and medical sciences Biotechnology C. virosa Canavalia Canavalia cathartica Canavalia lineata Cell biochemistry Cell physiology comparisons concanavalin A Concanavalin A - chemistry Fundamental and applied biological sciences. Psychology Glycoproteins lectins Lectins - chemistry Lectins - isolation & purification Leguminosae Molecular Sequence Data Plant Lectins Plant physiology and development Proteins seeds Seeds - chemistry |
| title | Primary structures of concanavalin a-like lectins from seeds of two species of Canavalia |
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