Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1)
A cDNA clone, designated CeCPI, encoding a novel phytocystatin was isolated from taro corms (Colocasia esculenta) using both degenerated primers/RT-PCR amplification and 5'-/3'-RACE extension. The full-length cDNA gene is 1,008 bp in size, encodes 206 amino acid residues, with a deduced mo...
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| Veröffentlicht in: | Planta 2005-06, Vol.221 (4), p.493-501 |
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| description | A cDNA clone, designated CeCPI, encoding a novel phytocystatin was isolated from taro corms (Colocasia esculenta) using both degenerated primers/RT-PCR amplification and 5'-/3'-RACE extension. The full-length cDNA gene is 1,008 bp in size, encodes 206 amino acid residues, with a deduced molecular weight of 29 kDa. It contains a conserved reactive site motif Gln-Val-Val-Ser-Gly of cysteine protease inhibitors, and another consensus ARFAV sequence for phytocystatin. Sequence analysis revealed that CeCPI is phylogenetically closely related to Eudicots rather than to Monocots, despite taro belonging to Monocot. Recombinant GST-CeCPI fusion protein was overexpressed in Escherichia coli and its inhibitory activity against papain was identified on gelatin/SDS-PAGE. These results confirmed that recombinant CeCPI protein exhibited strong cysteine protease inhibitory activity. Investigation of its antifungal activity clearly revealed a toxic effect on the mycelium growth of phytopathogenic fungi, such as Sclerotium rolfsii Sacc. etc., at a concentration of 80 microgram recombinant CeCPI/ ml. Moreover, mycelium growth was completely inhibited and the sclerotia lysed at a concentration of 150-200 microgram/ml. Further studies have demonstrated that recombinant CeCPI is capable of acting against the endogenous cysteine proteinase in the fungal mycelium. |
| doi_str_mv | 10.1007/s00425-004-1462-8 |
| format | Article |
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Kaosiung no. 1)</title><source>MEDLINE</source><source>SpringerNature Journals</source><source>JSTOR</source><creator>Yang, A.H ; Yeh, K.W</creator><creatorcontrib>Yang, A.H ; Yeh, K.W</creatorcontrib><description>A cDNA clone, designated CeCPI, encoding a novel phytocystatin was isolated from taro corms (Colocasia esculenta) using both degenerated primers/RT-PCR amplification and 5'-/3'-RACE extension. The full-length cDNA gene is 1,008 bp in size, encodes 206 amino acid residues, with a deduced molecular weight of 29 kDa. It contains a conserved reactive site motif Gln-Val-Val-Ser-Gly of cysteine protease inhibitors, and another consensus ARFAV sequence for phytocystatin. Sequence analysis revealed that CeCPI is phylogenetically closely related to Eudicots rather than to Monocots, despite taro belonging to Monocot. Recombinant GST-CeCPI fusion protein was overexpressed in Escherichia coli and its inhibitory activity against papain was identified on gelatin/SDS-PAGE. These results confirmed that recombinant CeCPI protein exhibited strong cysteine protease inhibitory activity. Investigation of its antifungal activity clearly revealed a toxic effect on the mycelium growth of phytopathogenic fungi, such as Sclerotium rolfsii Sacc. etc., at a concentration of 80 microgram recombinant CeCPI/ ml. Moreover, mycelium growth was completely inhibited and the sclerotia lysed at a concentration of 150-200 microgram/ml. Further studies have demonstrated that recombinant CeCPI is capable of acting against the endogenous cysteine proteinase in the fungal mycelium.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/s00425-004-1462-8</identifier><identifier>PMID: 15647900</identifier><identifier>CODEN: PLANAB</identifier><language>eng</language><publisher>Berlin: Springer-Verlag</publisher><subject>Agronomy. Soil science and plant productions ; Amino Acid Sequence ; amino acid sequences ; Amino acids ; Antifungal Agents ; antifungal properties ; Antifungals ; Bacteria ; Base Sequence ; Biological and medical sciences ; Classical and quantitative genetics. Population genetics. Molecular genetics ; Cloning ; Cloning, Molecular ; Colocasia - metabolism ; Colocasia esculenta ; Complementary DNA ; cystatin ; Cystatins ; Cystatins - biosynthesis ; Cystatins - pharmacology ; Cysteine proteinase inhibitors ; cysteine proteinases ; E coli ; enzyme activity ; Escherichia coli ; Fundamental and applied biological sciences. Psychology ; fungal antagonists ; Gene Expression ; Generalities. Genetics. Plant material ; Genetics and breeding of economic plants ; host-pathogen relationships ; Molecular genetics ; Molecular Sequence Data ; Molecular weight ; Mycelium ; nucleotide sequences ; Pathogens ; plant biochemistry ; plant pathogenic fungi ; plant proteins ; Plant Proteins - biosynthesis ; Plant Proteins - pharmacology ; Plants ; Protease inhibitors ; Proteinase inhibitors ; Proteins ; recombinant fusion proteins ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - pharmacology ; Sclerotium rolfsii ; sequence analysis ; Sequence Homology, Amino Acid ; Taro ; thermal stability</subject><ispartof>Planta, 2005-06, Vol.221 (4), p.493-501</ispartof><rights>Springer-Verlag Berlin Heidelberg 2005</rights><rights>2005 INIST-CNRS</rights><rights>Springer-Verlag 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c476t-5bd64d29484f4b1bbe2216e3c325356cb41990f6d6355b0a2b7baa12cccb62d3</citedby><cites>FETCH-LOGICAL-c476t-5bd64d29484f4b1bbe2216e3c325356cb41990f6d6355b0a2b7baa12cccb62d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23388909$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23388909$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>315,782,786,805,27933,27934,58026,58259</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16892394$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15647900$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, A.H</creatorcontrib><creatorcontrib>Yeh, K.W</creatorcontrib><title>Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1)</title><title>Planta</title><addtitle>Planta</addtitle><description>A cDNA clone, designated CeCPI, encoding a novel phytocystatin was isolated from taro corms (Colocasia esculenta) using both degenerated primers/RT-PCR amplification and 5'-/3'-RACE extension. The full-length cDNA gene is 1,008 bp in size, encodes 206 amino acid residues, with a deduced molecular weight of 29 kDa. It contains a conserved reactive site motif Gln-Val-Val-Ser-Gly of cysteine protease inhibitors, and another consensus ARFAV sequence for phytocystatin. Sequence analysis revealed that CeCPI is phylogenetically closely related to Eudicots rather than to Monocots, despite taro belonging to Monocot. Recombinant GST-CeCPI fusion protein was overexpressed in Escherichia coli and its inhibitory activity against papain was identified on gelatin/SDS-PAGE. These results confirmed that recombinant CeCPI protein exhibited strong cysteine protease inhibitory activity. Investigation of its antifungal activity clearly revealed a toxic effect on the mycelium growth of phytopathogenic fungi, such as Sclerotium rolfsii Sacc. etc., at a concentration of 80 microgram recombinant CeCPI/ ml. Moreover, mycelium growth was completely inhibited and the sclerotia lysed at a concentration of 150-200 microgram/ml. Further studies have demonstrated that recombinant CeCPI is capable of acting against the endogenous cysteine proteinase in the fungal mycelium.</description><subject>Agronomy. Soil science and plant productions</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino acids</subject><subject>Antifungal Agents</subject><subject>antifungal properties</subject><subject>Antifungals</subject><subject>Bacteria</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Classical and quantitative genetics. Population genetics. Molecular genetics</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Colocasia - metabolism</subject><subject>Colocasia esculenta</subject><subject>Complementary DNA</subject><subject>cystatin</subject><subject>Cystatins</subject><subject>Cystatins - biosynthesis</subject><subject>Cystatins - pharmacology</subject><subject>Cysteine proteinase inhibitors</subject><subject>cysteine proteinases</subject><subject>E coli</subject><subject>enzyme activity</subject><subject>Escherichia coli</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>fungal antagonists</subject><subject>Gene Expression</subject><subject>Generalities. Genetics. Plant material</subject><subject>Genetics and breeding of economic plants</subject><subject>host-pathogen relationships</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>Molecular weight</subject><subject>Mycelium</subject><subject>nucleotide sequences</subject><subject>Pathogens</subject><subject>plant biochemistry</subject><subject>plant pathogenic fungi</subject><subject>plant proteins</subject><subject>Plant Proteins - biosynthesis</subject><subject>Plant Proteins - pharmacology</subject><subject>Plants</subject><subject>Protease inhibitors</subject><subject>Proteinase inhibitors</subject><subject>Proteins</subject><subject>recombinant fusion proteins</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Sclerotium rolfsii</subject><subject>sequence analysis</subject><subject>Sequence Homology, Amino Acid</subject><subject>Taro</subject><subject>thermal stability</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkd2KFDEQhYMo7jj6AF6oQVAUtsf8dTp9KYN_uOKF63WopNNDhp5kTNKL8wI-t1l6cMGLqgqcr04FDkJPKdlQQrp3mRDB2qb2hgrJGnUPrajgrGFEqPtoRUh9k563F-hRzntCqth1D9EFbaXoekJW6M-3ODk7T5CwnWLwYXeJk7PxYHyAUPDOBYfd72NyOfsYLjGEoVbx4xx2MGGwxd_4csJxxPaUCxQf8JjiARdIEb_ZxilayB6wy_WMCwWwvdngrxCzrxY4xA2mbx-jByNM2T05zzW6_vjhevu5ufr-6cv2_VVjRSdL05pBioH1QolRGGqMY4xKxy1nLW-lNYL2PRnlIHnbGgLMdAaAMmutkWzga_R6sT2m-Gt2ueiDz9ZNEwQX56xprxhRqqvgy__AfZxTqF_TiirV9pTKCtEFsinmnNyoj8kfIJ00Jfo2IL0EpGvXtwFpVXeen41nc3DD3cY5kQq8OgOQLUxjgmB9vuOk6hnvReWeLdw-l5j-6Yxzpfqa-Rq9WPQRooZdqh4_fzBCOaFEUioo_wtxOavB</recordid><startdate>20050601</startdate><enddate>20050601</enddate><creator>Yang, A.H</creator><creator>Yeh, K.W</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7QL</scope><scope>7T7</scope><scope>C1K</scope><scope>M7N</scope></search><sort><creationdate>20050601</creationdate><title>Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1)</title><author>Yang, A.H ; Yeh, K.W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-5bd64d29484f4b1bbe2216e3c325356cb41990f6d6355b0a2b7baa12cccb62d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Agronomy. Soil science and plant productions</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Amino acids</topic><topic>Antifungal Agents</topic><topic>antifungal properties</topic><topic>Antifungals</topic><topic>Bacteria</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Classical and quantitative genetics. Population genetics. Molecular genetics</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>Colocasia - metabolism</topic><topic>Colocasia esculenta</topic><topic>Complementary DNA</topic><topic>cystatin</topic><topic>Cystatins</topic><topic>Cystatins - biosynthesis</topic><topic>Cystatins - pharmacology</topic><topic>Cysteine proteinase inhibitors</topic><topic>cysteine proteinases</topic><topic>E coli</topic><topic>enzyme activity</topic><topic>Escherichia coli</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>fungal antagonists</topic><topic>Gene Expression</topic><topic>Generalities. Genetics. Plant material</topic><topic>Genetics and breeding of economic plants</topic><topic>host-pathogen relationships</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>Molecular weight</topic><topic>Mycelium</topic><topic>nucleotide sequences</topic><topic>Pathogens</topic><topic>plant biochemistry</topic><topic>plant pathogenic fungi</topic><topic>plant proteins</topic><topic>Plant Proteins - biosynthesis</topic><topic>Plant Proteins - pharmacology</topic><topic>Plants</topic><topic>Protease inhibitors</topic><topic>Proteinase inhibitors</topic><topic>Proteins</topic><topic>recombinant fusion proteins</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Sclerotium rolfsii</topic><topic>sequence analysis</topic><topic>Sequence Homology, Amino Acid</topic><topic>Taro</topic><topic>thermal stability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, A.H</creatorcontrib><creatorcontrib>Yeh, K.W</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>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>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>ProQuest Pharma Collection</collection><collection>Technology Research Database</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 Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Planta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, A.H</au><au>Yeh, K.W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1)</atitle><jtitle>Planta</jtitle><addtitle>Planta</addtitle><date>2005-06-01</date><risdate>2005</risdate><volume>221</volume><issue>4</issue><spage>493</spage><epage>501</epage><pages>493-501</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><coden>PLANAB</coden><abstract>A cDNA clone, designated CeCPI, encoding a novel phytocystatin was isolated from taro corms (Colocasia esculenta) using both degenerated primers/RT-PCR amplification and 5'-/3'-RACE extension. The full-length cDNA gene is 1,008 bp in size, encodes 206 amino acid residues, with a deduced molecular weight of 29 kDa. It contains a conserved reactive site motif Gln-Val-Val-Ser-Gly of cysteine protease inhibitors, and another consensus ARFAV sequence for phytocystatin. Sequence analysis revealed that CeCPI is phylogenetically closely related to Eudicots rather than to Monocots, despite taro belonging to Monocot. Recombinant GST-CeCPI fusion protein was overexpressed in Escherichia coli and its inhibitory activity against papain was identified on gelatin/SDS-PAGE. These results confirmed that recombinant CeCPI protein exhibited strong cysteine protease inhibitory activity. Investigation of its antifungal activity clearly revealed a toxic effect on the mycelium growth of phytopathogenic fungi, such as Sclerotium rolfsii Sacc. etc., at a concentration of 80 microgram recombinant CeCPI/ ml. Moreover, mycelium growth was completely inhibited and the sclerotia lysed at a concentration of 150-200 microgram/ml. Further studies have demonstrated that recombinant CeCPI is capable of acting against the endogenous cysteine proteinase in the fungal mycelium.</abstract><cop>Berlin</cop><pub>Springer-Verlag</pub><pmid>15647900</pmid><doi>10.1007/s00425-004-1462-8</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Agronomy. Soil science and plant productions Amino Acid Sequence amino acid sequences Amino acids Antifungal Agents antifungal properties Antifungals Bacteria Base Sequence Biological and medical sciences Classical and quantitative genetics. Population genetics. Molecular genetics Cloning Cloning, Molecular Colocasia - metabolism Colocasia esculenta Complementary DNA cystatin Cystatins Cystatins - biosynthesis Cystatins - pharmacology Cysteine proteinase inhibitors cysteine proteinases E coli enzyme activity Escherichia coli Fundamental and applied biological sciences. Psychology fungal antagonists Gene Expression Generalities. Genetics. Plant material Genetics and breeding of economic plants host-pathogen relationships Molecular genetics Molecular Sequence Data Molecular weight Mycelium nucleotide sequences Pathogens plant biochemistry plant pathogenic fungi plant proteins Plant Proteins - biosynthesis Plant Proteins - pharmacology Plants Protease inhibitors Proteinase inhibitors Proteins recombinant fusion proteins Recombinant Proteins - biosynthesis Recombinant Proteins - pharmacology Sclerotium rolfsii sequence analysis Sequence Homology, Amino Acid Taro thermal stability |
| title | Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1) |
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