Purification and characterization of two basic β-1,3-glucanases induced in Colletotrichum lindemuthianum-infected bean seedlings
Two β-1,3-glucanases which are rapidly induced in the incompatible interaction between bean (cv. Processor) and Colletotrichum, lindemuthianum race β were purified to homogeneity. Characterization of the two enzymes, GE1 and GE2, showed that they both had a basic isolectric point and a similar molec...
Gespeichert in:
| Veröffentlicht in: | Archives of biochemistry and biophysics 1992-02, Vol.292 (2), p.468-474 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 474 |
|---|---|
| container_issue | 2 |
| container_start_page | 468 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 292 |
| creator | Daugrois, Jean Heinrich Lafitte, Claude Barthe, Jean-Paul Faucher, Catherine Touze, André Esquerre-Tugaye, Marie-Thérèse |
| description | Two β-1,3-glucanases which are rapidly induced in the incompatible interaction between bean (cv. Processor) and
Colletotrichum, lindemuthianum race β were purified to homogeneity. Characterization of the two enzymes, GE1 and GE2, showed that they both had a basic isolectric point and a similar molecular weight (36,500 for GE1 and 36,000 for GE2), but differed in their pH optimum, thermal stability, and specific activity. GE2 was present in higher amounts but was shown to be less active than GE1 against laminarin and fungal cell walls isolated from race β of the fungus. Both enzymes were specific for β-1,3 linkages and showed a strict endolytic mode of action. Further characterization of GE2 was achieved by amino acid sequence analysis of tryptic peptides; the degree of homology shared with other basic β-1,3-glucanases depended on the plant source. A time-course study showed that GE1 and GE2 were increased during infection. They were also induced by fungal elicitors, thereby indicating that they originate from the host. |
| doi_str_mv | 10.1016/0003-9861(92)90017-Q |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_72784024</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>000398619290017Q</els_id><sourcerecordid>16208222</sourcerecordid><originalsourceid>FETCH-LOGICAL-c351t-f899eda91ef5b305256939fe047029e83a0ba19c1dbf2654cd04b5ead264ae6d3</originalsourceid><addsrcrecordid>eNqFkc2KFTEQhYMo43X0BUShFyIKtuanO93ZCHLxDwZ00FmH6qRyb6Q7GZNuRXe-kg_iM5lrX8adrgrqfHUoziHkHqNPGWXyGaVU1KqX7JHijxWlrKvPr5ENo0rWVPTNdbK5Qm6SWzl_KgxrJD8hJ6wTTDK-IT_eL8k7b2D2MVQQbGX2kMDMmPz3dRldNX-N1QDZm-rXz5o9EfVuXAwEyJgrH-xi0JZZbeM44hzn5M1-maqxSDgt895DWKbaB4fF11YDQqgyoi3ALt8mNxyMGe8c5ym5ePXy4_ZNffbu9dvti7PaiJbNteuVQguKoWsHQVveSiWUQ9p0lCvsBdABmDLMDo7LtjGWNkOLYLlsAKUVp-Th6nuZ4ucF86wnnw2OIwSMS9Yd7_qG8ua_IJOc9pzzAjYraFLMOaHTl8lPkL5pRvWhIn3IXx_y14rrPxXp83J2_-i_DBPav0drJ0V_cNQhGxhdgmB8vsJaLkTfi4LdXTEHUcMuFeTig2I9b9XB4_kqYkn0i8eks_EYSk8-lRK0jf7fT_4GaIO35A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16208222</pqid></control><display><type>article</type><title>Purification and characterization of two basic β-1,3-glucanases induced in Colletotrichum lindemuthianum-infected bean seedlings</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Daugrois, Jean Heinrich ; Lafitte, Claude ; Barthe, Jean-Paul ; Faucher, Catherine ; Touze, André ; Esquerre-Tugaye, Marie-Thérèse</creator><creatorcontrib>Daugrois, Jean Heinrich ; Lafitte, Claude ; Barthe, Jean-Paul ; Faucher, Catherine ; Touze, André ; Esquerre-Tugaye, Marie-Thérèse</creatorcontrib><description>Two β-1,3-glucanases which are rapidly induced in the incompatible interaction between bean (cv. Processor) and
Colletotrichum, lindemuthianum race β were purified to homogeneity. Characterization of the two enzymes, GE1 and GE2, showed that they both had a basic isolectric point and a similar molecular weight (36,500 for GE1 and 36,000 for GE2), but differed in their pH optimum, thermal stability, and specific activity. GE2 was present in higher amounts but was shown to be less active than GE1 against laminarin and fungal cell walls isolated from race β of the fungus. Both enzymes were specific for β-1,3 linkages and showed a strict endolytic mode of action. Further characterization of GE2 was achieved by amino acid sequence analysis of tryptic peptides; the degree of homology shared with other basic β-1,3-glucanases depended on the plant source. A time-course study showed that GE1 and GE2 were increased during infection. They were also induced by fungal elicitors, thereby indicating that they originate from the host.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(92)90017-Q</identifier><identifier>PMID: 1731612</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; beta -1,3-glucanase ; beta-Glucosidase - biosynthesis ; beta-Glucosidase - isolation & purification ; beta-Glucosidase - metabolism ; Biological and medical sciences ; characterization ; Chromatography, Gel ; COLLETOTRICHUM ; Colletotrichum lindemuthianum ; Enzyme Induction ; Enzyme Stability ; Enzymes and enzyme inhibitors ; Fabaceae - enzymology ; Fabaceae - microbiology ; Fundamental and applied biological sciences. Psychology ; GLICOSIDASAS ; Glucan 1,3-beta-Glucosidase ; GLYCOSIDASE ; Hydrolases ; infection ; ISOENZIMAS ; ISOENZYME ; Kinetics ; Mitosporic Fungi - pathogenicity ; Molecular Sequence Data ; Molecular Weight ; PESO MOLECULAR ; PHASEOLUS VULGARIS ; Plants, Medicinal ; PLANTULAS ; PLANTULE ; POIDS MOLECULAIRE ; PROPIEDADES FISICO-QUIMICAS ; PROPRIETE PHYSICOCHIMIQUE ; PURIFICACION ; PURIFICATION ; Sequence Homology, Nucleic Acid</subject><ispartof>Archives of biochemistry and biophysics, 1992-02, Vol.292 (2), p.468-474</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-f899eda91ef5b305256939fe047029e83a0ba19c1dbf2654cd04b5ead264ae6d3</citedby><cites>FETCH-LOGICAL-c351t-f899eda91ef5b305256939fe047029e83a0ba19c1dbf2654cd04b5ead264ae6d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(92)90017-Q$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5233883$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1731612$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Daugrois, Jean Heinrich</creatorcontrib><creatorcontrib>Lafitte, Claude</creatorcontrib><creatorcontrib>Barthe, Jean-Paul</creatorcontrib><creatorcontrib>Faucher, Catherine</creatorcontrib><creatorcontrib>Touze, André</creatorcontrib><creatorcontrib>Esquerre-Tugaye, Marie-Thérèse</creatorcontrib><title>Purification and characterization of two basic β-1,3-glucanases induced in Colletotrichum lindemuthianum-infected bean seedlings</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Two β-1,3-glucanases which are rapidly induced in the incompatible interaction between bean (cv. Processor) and
Colletotrichum, lindemuthianum race β were purified to homogeneity. Characterization of the two enzymes, GE1 and GE2, showed that they both had a basic isolectric point and a similar molecular weight (36,500 for GE1 and 36,000 for GE2), but differed in their pH optimum, thermal stability, and specific activity. GE2 was present in higher amounts but was shown to be less active than GE1 against laminarin and fungal cell walls isolated from race β of the fungus. Both enzymes were specific for β-1,3 linkages and showed a strict endolytic mode of action. Further characterization of GE2 was achieved by amino acid sequence analysis of tryptic peptides; the degree of homology shared with other basic β-1,3-glucanases depended on the plant source. A time-course study showed that GE1 and GE2 were increased during infection. They were also induced by fungal elicitors, thereby indicating that they originate from the host.</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>beta -1,3-glucanase</subject><subject>beta-Glucosidase - biosynthesis</subject><subject>beta-Glucosidase - isolation & purification</subject><subject>beta-Glucosidase - metabolism</subject><subject>Biological and medical sciences</subject><subject>characterization</subject><subject>Chromatography, Gel</subject><subject>COLLETOTRICHUM</subject><subject>Colletotrichum lindemuthianum</subject><subject>Enzyme Induction</subject><subject>Enzyme Stability</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fabaceae - enzymology</subject><subject>Fabaceae - microbiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GLICOSIDASAS</subject><subject>Glucan 1,3-beta-Glucosidase</subject><subject>GLYCOSIDASE</subject><subject>Hydrolases</subject><subject>infection</subject><subject>ISOENZIMAS</subject><subject>ISOENZYME</subject><subject>Kinetics</subject><subject>Mitosporic Fungi - pathogenicity</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>PESO MOLECULAR</subject><subject>PHASEOLUS VULGARIS</subject><subject>Plants, Medicinal</subject><subject>PLANTULAS</subject><subject>PLANTULE</subject><subject>POIDS MOLECULAIRE</subject><subject>PROPIEDADES FISICO-QUIMICAS</subject><subject>PROPRIETE PHYSICOCHIMIQUE</subject><subject>PURIFICACION</subject><subject>PURIFICATION</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2KFTEQhYMo43X0BUShFyIKtuanO93ZCHLxDwZ00FmH6qRyb6Q7GZNuRXe-kg_iM5lrX8adrgrqfHUoziHkHqNPGWXyGaVU1KqX7JHijxWlrKvPr5ENo0rWVPTNdbK5Qm6SWzl_KgxrJD8hJ6wTTDK-IT_eL8k7b2D2MVQQbGX2kMDMmPz3dRldNX-N1QDZm-rXz5o9EfVuXAwEyJgrH-xi0JZZbeM44hzn5M1-maqxSDgt895DWKbaB4fF11YDQqgyoi3ALt8mNxyMGe8c5ym5ePXy4_ZNffbu9dvti7PaiJbNteuVQguKoWsHQVveSiWUQ9p0lCvsBdABmDLMDo7LtjGWNkOLYLlsAKUVp-Th6nuZ4ucF86wnnw2OIwSMS9Yd7_qG8ua_IJOc9pzzAjYraFLMOaHTl8lPkL5pRvWhIn3IXx_y14rrPxXp83J2_-i_DBPav0drJ0V_cNQhGxhdgmB8vsJaLkTfi4LdXTEHUcMuFeTig2I9b9XB4_kqYkn0i8eks_EYSk8-lRK0jf7fT_4GaIO35A</recordid><startdate>19920201</startdate><enddate>19920201</enddate><creator>Daugrois, Jean Heinrich</creator><creator>Lafitte, Claude</creator><creator>Barthe, Jean-Paul</creator><creator>Faucher, Catherine</creator><creator>Touze, André</creator><creator>Esquerre-Tugaye, Marie-Thérèse</creator><general>Elsevier Inc</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19920201</creationdate><title>Purification and characterization of two basic β-1,3-glucanases induced in Colletotrichum lindemuthianum-infected bean seedlings</title><author>Daugrois, Jean Heinrich ; Lafitte, Claude ; Barthe, Jean-Paul ; Faucher, Catherine ; Touze, André ; Esquerre-Tugaye, Marie-Thérèse</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-f899eda91ef5b305256939fe047029e83a0ba19c1dbf2654cd04b5ead264ae6d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>beta -1,3-glucanase</topic><topic>beta-Glucosidase - biosynthesis</topic><topic>beta-Glucosidase - isolation & purification</topic><topic>beta-Glucosidase - metabolism</topic><topic>Biological and medical sciences</topic><topic>characterization</topic><topic>Chromatography, Gel</topic><topic>COLLETOTRICHUM</topic><topic>Colletotrichum lindemuthianum</topic><topic>Enzyme Induction</topic><topic>Enzyme Stability</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fabaceae - enzymology</topic><topic>Fabaceae - microbiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GLICOSIDASAS</topic><topic>Glucan 1,3-beta-Glucosidase</topic><topic>GLYCOSIDASE</topic><topic>Hydrolases</topic><topic>infection</topic><topic>ISOENZIMAS</topic><topic>ISOENZYME</topic><topic>Kinetics</topic><topic>Mitosporic Fungi - pathogenicity</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>PESO MOLECULAR</topic><topic>PHASEOLUS VULGARIS</topic><topic>Plants, Medicinal</topic><topic>PLANTULAS</topic><topic>PLANTULE</topic><topic>POIDS MOLECULAIRE</topic><topic>PROPIEDADES FISICO-QUIMICAS</topic><topic>PROPRIETE PHYSICOCHIMIQUE</topic><topic>PURIFICACION</topic><topic>PURIFICATION</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Daugrois, Jean Heinrich</creatorcontrib><creatorcontrib>Lafitte, Claude</creatorcontrib><creatorcontrib>Barthe, Jean-Paul</creatorcontrib><creatorcontrib>Faucher, Catherine</creatorcontrib><creatorcontrib>Touze, André</creatorcontrib><creatorcontrib>Esquerre-Tugaye, Marie-Thérèse</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Daugrois, Jean Heinrich</au><au>Lafitte, Claude</au><au>Barthe, Jean-Paul</au><au>Faucher, Catherine</au><au>Touze, André</au><au>Esquerre-Tugaye, Marie-Thérèse</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of two basic β-1,3-glucanases induced in Colletotrichum lindemuthianum-infected bean seedlings</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1992-02-01</date><risdate>1992</risdate><volume>292</volume><issue>2</issue><spage>468</spage><epage>474</epage><pages>468-474</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>Two β-1,3-glucanases which are rapidly induced in the incompatible interaction between bean (cv. Processor) and
Colletotrichum, lindemuthianum race β were purified to homogeneity. Characterization of the two enzymes, GE1 and GE2, showed that they both had a basic isolectric point and a similar molecular weight (36,500 for GE1 and 36,000 for GE2), but differed in their pH optimum, thermal stability, and specific activity. GE2 was present in higher amounts but was shown to be less active than GE1 against laminarin and fungal cell walls isolated from race β of the fungus. Both enzymes were specific for β-1,3 linkages and showed a strict endolytic mode of action. Further characterization of GE2 was achieved by amino acid sequence analysis of tryptic peptides; the degree of homology shared with other basic β-1,3-glucanases depended on the plant source. A time-course study showed that GE1 and GE2 were increased during infection. They were also induced by fungal elicitors, thereby indicating that they originate from the host.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1731612</pmid><doi>10.1016/0003-9861(92)90017-Q</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1992-02, Vol.292 (2), p.468-474 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72784024 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino Acid Sequence Analytical, structural and metabolic biochemistry beta -1,3-glucanase beta-Glucosidase - biosynthesis beta-Glucosidase - isolation & purification beta-Glucosidase - metabolism Biological and medical sciences characterization Chromatography, Gel COLLETOTRICHUM Colletotrichum lindemuthianum Enzyme Induction Enzyme Stability Enzymes and enzyme inhibitors Fabaceae - enzymology Fabaceae - microbiology Fundamental and applied biological sciences. Psychology GLICOSIDASAS Glucan 1,3-beta-Glucosidase GLYCOSIDASE Hydrolases infection ISOENZIMAS ISOENZYME Kinetics Mitosporic Fungi - pathogenicity Molecular Sequence Data Molecular Weight PESO MOLECULAR PHASEOLUS VULGARIS Plants, Medicinal PLANTULAS PLANTULE POIDS MOLECULAIRE PROPIEDADES FISICO-QUIMICAS PROPRIETE PHYSICOCHIMIQUE PURIFICACION PURIFICATION Sequence Homology, Nucleic Acid |
| title | Purification and characterization of two basic β-1,3-glucanases induced in Colletotrichum lindemuthianum-infected bean seedlings |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T00%3A16%3A07IST&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=Purification%20and%20characterization%20of%20two%20basic%20%CE%B2-1,3-glucanases%20induced%20in%20Colletotrichum%20lindemuthianum-infected%20bean%20seedlings&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Daugrois,%20Jean%20Heinrich&rft.date=1992-02-01&rft.volume=292&rft.issue=2&rft.spage=468&rft.epage=474&rft.pages=468-474&rft.issn=0003-9861&rft.eissn=1096-0384&rft.coden=ABBIA4&rft_id=info:doi/10.1016/0003-9861(92)90017-Q&rft_dat=%3Cproquest_cross%3E16208222%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=16208222&rft_id=info:pmid/1731612&rft_els_id=000398619290017Q&rfr_iscdi=true |