Design, Expression, and Crystallization of Recombinant Lectin from the Garden Pea (Pisum sativum)
The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1989-04, Vol.264 (12), p.6793-6796 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 6796 |
|---|---|
| container_issue | 12 |
| container_start_page | 6793 |
| container_title | The Journal of biological chemistry |
| container_volume | 264 |
| creator | Prasthofer, T Phillips, S R Suddath, F L Engler, J A |
| description | The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent assay, the resulting propeptide molecule is virtually indistinguishable from the mature proteolytically processed lectin isolated from peas. Preliminary crystallization experiments using the recombinant propeptide lectin yield crystals in space group P212121 with a = 64.8 Å, b = 73.8 Å, and c = 109.0 Å (1 Å = 0.1 nm) that diffract to 2.8-Å resolution. This unit cell size is quite similar to the unit cell determined for native pea lectin, suggesting that the overall structure of the recombinant prolectin is virtually identical. |
| doi_str_mv | 10.1016/S0021-9258(18)83499-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_78954844</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925818834998</els_id><sourcerecordid>15360442</sourcerecordid><originalsourceid>FETCH-LOGICAL-c514t-f81ff7362b15a8a8b7380e0954732a48ab9f2e67f879f3f0c2c127f79e312a183</originalsourceid><addsrcrecordid>eNqFkV9rFDEUxYModV39AkIhoEgLjuYmmUnmSWStVViwWAu-hUz2Zjcyf9Zkplo_vdnusq8NhITc3z1JziHkFNg7YFC9v2aMQ1HzUp-BPtdC1nWhH5EZMC0KUcLPx2R2RJ6SZyn9YnnIGk7ICVeZknJG7CdMYd2_pRd_txFTCkPe235FF_EujbZtwz875kM6ePod3dA1obf9SJfoxtBTH4eOjhuklzausKdXaOnZVUhTR1Puu5268-fkibdtwheHdU5uPl_8WHwplt8uvy4-LgtXghwLr8F7JSreQGm11Y0SmiGrS6kEt1LbpvYcK-W1qr3wzHEHXHlVowBuQYs5ebPX3cbh94RpNF1IDtvW9jhMySidtbSUD4JQiopJyTNY7kEXh5QierONobPxzgAzuwzMfQZmZ7ABbe4zMLuXnB4umJoOV8eug-m5_vpQt8nZ1kfbu5COmBIAZbmTebXHNmG9-RMimiYMboOd4ZU0wE2lapGpl3vK28HYdcxCN9e6BrGbc_JhX8Rs_G3AaJIL2DtcZTk3mtUQHvjLfy8ktZI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15360442</pqid></control><display><type>article</type><title>Design, Expression, and Crystallization of Recombinant Lectin from the Garden Pea (Pisum sativum)</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Prasthofer, T ; Phillips, S R ; Suddath, F L ; Engler, J A</creator><creatorcontrib>Prasthofer, T ; Phillips, S R ; Suddath, F L ; Engler, J A</creatorcontrib><description>The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent assay, the resulting propeptide molecule is virtually indistinguishable from the mature proteolytically processed lectin isolated from peas. Preliminary crystallization experiments using the recombinant propeptide lectin yield crystals in space group P212121 with a = 64.8 Å, b = 73.8 Å, and c = 109.0 Å (1 Å = 0.1 nm) that diffract to 2.8-Å resolution. This unit cell size is quite similar to the unit cell determined for native pea lectin, suggesting that the overall structure of the recombinant prolectin is virtually identical.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)83499-8</identifier><identifier>PMID: 2708344</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Biological and medical sciences ; Biotechnology ; Blotting, Western ; Chromatography, Gel ; Cloning, Molecular ; CRISTALIZACION ; CRISTALLISATION ; CRYSTALLIZATION ; Enzyme-Linked Immunosorbent Assay ; EPREUVE D'HEMAGGLUTINATION ; Fundamental and applied biological sciences. Psychology ; Genetic engineering ; Genetic technics ; HAEMAGGLUTINATION TESTS ; Hemagglutinins ; LECTINA ; LECTINE ; LECTINS ; Lectins - genetics ; Methods. Procedures. Technologies ; Molecular Sequence Data ; PISUM SATIVUM ; Plant Lectins ; Promoter Regions, Genetic ; PRUEBA DE HEMAGLUTINACION ; RECOMBINACION ; RECOMBINAISON ; Recombinant Proteins - ultrastructure ; RECOMBINATION</subject><ispartof>The Journal of biological chemistry, 1989-04, Vol.264 (12), p.6793-6796</ispartof><rights>1989 © 1989 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-f81ff7362b15a8a8b7380e0954732a48ab9f2e67f879f3f0c2c127f79e312a183</citedby><cites>FETCH-LOGICAL-c514t-f81ff7362b15a8a8b7380e0954732a48ab9f2e67f879f3f0c2c127f79e312a183</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7311558$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2708344$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Prasthofer, T</creatorcontrib><creatorcontrib>Phillips, S R</creatorcontrib><creatorcontrib>Suddath, F L</creatorcontrib><creatorcontrib>Engler, J A</creatorcontrib><title>Design, Expression, and Crystallization of Recombinant Lectin from the Garden Pea (Pisum sativum)</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent assay, the resulting propeptide molecule is virtually indistinguishable from the mature proteolytically processed lectin isolated from peas. Preliminary crystallization experiments using the recombinant propeptide lectin yield crystals in space group P212121 with a = 64.8 Å, b = 73.8 Å, and c = 109.0 Å (1 Å = 0.1 nm) that diffract to 2.8-Å resolution. This unit cell size is quite similar to the unit cell determined for native pea lectin, suggesting that the overall structure of the recombinant prolectin is virtually identical.</description><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Blotting, Western</subject><subject>Chromatography, Gel</subject><subject>Cloning, Molecular</subject><subject>CRISTALIZACION</subject><subject>CRISTALLISATION</subject><subject>CRYSTALLIZATION</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>EPREUVE D'HEMAGGLUTINATION</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>HAEMAGGLUTINATION TESTS</subject><subject>Hemagglutinins</subject><subject>LECTINA</subject><subject>LECTINE</subject><subject>LECTINS</subject><subject>Lectins - genetics</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular Sequence Data</subject><subject>PISUM SATIVUM</subject><subject>Plant Lectins</subject><subject>Promoter Regions, Genetic</subject><subject>PRUEBA DE HEMAGLUTINACION</subject><subject>RECOMBINACION</subject><subject>RECOMBINAISON</subject><subject>Recombinant Proteins - ultrastructure</subject><subject>RECOMBINATION</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV9rFDEUxYModV39AkIhoEgLjuYmmUnmSWStVViwWAu-hUz2Zjcyf9Zkplo_vdnusq8NhITc3z1JziHkFNg7YFC9v2aMQ1HzUp-BPtdC1nWhH5EZMC0KUcLPx2R2RJ6SZyn9YnnIGk7ICVeZknJG7CdMYd2_pRd_txFTCkPe235FF_EujbZtwz875kM6ePod3dA1obf9SJfoxtBTH4eOjhuklzausKdXaOnZVUhTR1Puu5268-fkibdtwheHdU5uPl_8WHwplt8uvy4-LgtXghwLr8F7JSreQGm11Y0SmiGrS6kEt1LbpvYcK-W1qr3wzHEHXHlVowBuQYs5ebPX3cbh94RpNF1IDtvW9jhMySidtbSUD4JQiopJyTNY7kEXh5QierONobPxzgAzuwzMfQZmZ7ABbe4zMLuXnB4umJoOV8eug-m5_vpQt8nZ1kfbu5COmBIAZbmTebXHNmG9-RMimiYMboOd4ZU0wE2lapGpl3vK28HYdcxCN9e6BrGbc_JhX8Rs_G3AaJIL2DtcZTk3mtUQHvjLfy8ktZI</recordid><startdate>19890425</startdate><enddate>19890425</enddate><creator>Prasthofer, T</creator><creator>Phillips, S R</creator><creator>Suddath, F L</creator><creator>Engler, J A</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890425</creationdate><title>Design, Expression, and Crystallization of Recombinant Lectin from the Garden Pea (Pisum sativum)</title><author>Prasthofer, T ; Phillips, S R ; Suddath, F L ; Engler, J A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-f81ff7362b15a8a8b7380e0954732a48ab9f2e67f879f3f0c2c127f79e312a183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Blotting, Western</topic><topic>Chromatography, Gel</topic><topic>Cloning, Molecular</topic><topic>CRISTALIZACION</topic><topic>CRISTALLISATION</topic><topic>CRYSTALLIZATION</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>EPREUVE D'HEMAGGLUTINATION</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>HAEMAGGLUTINATION TESTS</topic><topic>Hemagglutinins</topic><topic>LECTINA</topic><topic>LECTINE</topic><topic>LECTINS</topic><topic>Lectins - genetics</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular Sequence Data</topic><topic>PISUM SATIVUM</topic><topic>Plant Lectins</topic><topic>Promoter Regions, Genetic</topic><topic>PRUEBA DE HEMAGLUTINACION</topic><topic>RECOMBINACION</topic><topic>RECOMBINAISON</topic><topic>Recombinant Proteins - ultrastructure</topic><topic>RECOMBINATION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prasthofer, T</creatorcontrib><creatorcontrib>Phillips, S R</creatorcontrib><creatorcontrib>Suddath, F L</creatorcontrib><creatorcontrib>Engler, J A</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Prasthofer, T</au><au>Phillips, S R</au><au>Suddath, F L</au><au>Engler, J A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Design, Expression, and Crystallization of Recombinant Lectin from the Garden Pea (Pisum sativum)</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-04-25</date><risdate>1989</risdate><volume>264</volume><issue>12</issue><spage>6793</spage><epage>6796</epage><pages>6793-6796</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent assay, the resulting propeptide molecule is virtually indistinguishable from the mature proteolytically processed lectin isolated from peas. Preliminary crystallization experiments using the recombinant propeptide lectin yield crystals in space group P212121 with a = 64.8 Å, b = 73.8 Å, and c = 109.0 Å (1 Å = 0.1 nm) that diffract to 2.8-Å resolution. This unit cell size is quite similar to the unit cell determined for native pea lectin, suggesting that the overall structure of the recombinant prolectin is virtually identical.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2708344</pmid><doi>10.1016/S0021-9258(18)83499-8</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1989-04, Vol.264 (12), p.6793-6796 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78954844 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Biological and medical sciences Biotechnology Blotting, Western Chromatography, Gel Cloning, Molecular CRISTALIZACION CRISTALLISATION CRYSTALLIZATION Enzyme-Linked Immunosorbent Assay EPREUVE D'HEMAGGLUTINATION Fundamental and applied biological sciences. Psychology Genetic engineering Genetic technics HAEMAGGLUTINATION TESTS Hemagglutinins LECTINA LECTINE LECTINS Lectins - genetics Methods. Procedures. Technologies Molecular Sequence Data PISUM SATIVUM Plant Lectins Promoter Regions, Genetic PRUEBA DE HEMAGLUTINACION RECOMBINACION RECOMBINAISON Recombinant Proteins - ultrastructure RECOMBINATION |
| title | Design, Expression, and Crystallization of Recombinant Lectin from the Garden Pea (Pisum sativum) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T12%3A12%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Design,%20Expression,%20and%20Crystallization%20of%20Recombinant%20Lectin%20from%20the%20Garden%20Pea%20(Pisum%20sativum)&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Prasthofer,%20T&rft.date=1989-04-25&rft.volume=264&rft.issue=12&rft.spage=6793&rft.epage=6796&rft.pages=6793-6796&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(18)83499-8&rft_dat=%3Cproquest_cross%3E15360442%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15360442&rft_id=info:pmid/2708344&rft_els_id=S0021925818834998&rfr_iscdi=true |