Isolation and characterization of hardening-induced proteins in Chlorella vulgaris C-27: Identification of late embryogenesis abundant proteins
Hardening-induced soluble proteins of chlorella vulgaris beijerink IAM C-27 (formerly Chlorella ellipsoidea Gerneck IAM C-27) were isolated and purified by two-dimensional high-performance liquid chromatography (2D-HPLC) on an anion-exchange column, with subsequent reversed-phase chromatography. Som...
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Veröffentlicht in: | Plant and cell physiology 1995-12, Vol.36 (8), p.1421-1430 |
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creator | Honjoh, K. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture) Yoshimoto, M Joh, T Kajiwara, T Miyamoto, T Hatano, S |
description | Hardening-induced soluble proteins of chlorella vulgaris beijerink IAM C-27 (formerly Chlorella ellipsoidea Gerneck IAM C-27) were isolated and purified by two-dimensional high-performance liquid chromatography (2D-HPLC) on an anion-exchange column, with subsequent reversed-phase chromatography. Some of the proteins were resolved by SDS-PAGE, characterized by amino-terminal sequencing and identified by searching for homologies in databases. Separation of the soluble proteins during the hardening of chlorella by a combination of 2D-HPLC and SDS-PAGE revealed that at least 31 proteins were induced or increased in abundance. Of particular interest was the induction after 12 h of a 10-kDa protein with the amino-terminal amino acid sequence AGNKPITEQISDAVGAAGQDVG and the induction after 6h of a 14-kDa protein with the amino-terminal sequence ALGEESLGDKAKNAFEDAKDAVKDAAGNVKEAV. The amino-terminal sequences of these proteins indicated that they were homologous to late embryogenesis abundant (LEA) proteins. Furthermore,the level of a 22-kDa protein also increased after 12 h. The amino-terminal sequence of this protein, AAPLVGGPAPDFTAAAVFD, indicated that it was homologous to thioredoxin peroxidase |
doi_str_mv | 10.1093/oxfordjournals.pcp.a078904 |
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(Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture) ; Yoshimoto, M ; Joh, T ; Kajiwara, T ; Miyamoto, T ; Hatano, S</creator><creatorcontrib>Honjoh, K. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture) ; Yoshimoto, M ; Joh, T ; Kajiwara, T ; Miyamoto, T ; Hatano, S</creatorcontrib><description>Hardening-induced soluble proteins of chlorella vulgaris beijerink IAM C-27 (formerly Chlorella ellipsoidea Gerneck IAM C-27) were isolated and purified by two-dimensional high-performance liquid chromatography (2D-HPLC) on an anion-exchange column, with subsequent reversed-phase chromatography. Some of the proteins were resolved by SDS-PAGE, characterized by amino-terminal sequencing and identified by searching for homologies in databases. Separation of the soluble proteins during the hardening of chlorella by a combination of 2D-HPLC and SDS-PAGE revealed that at least 31 proteins were induced or increased in abundance. Of particular interest was the induction after 12 h of a 10-kDa protein with the amino-terminal amino acid sequence AGNKPITEQISDAVGAAGQDVG and the induction after 6h of a 14-kDa protein with the amino-terminal sequence ALGEESLGDKAKNAFEDAKDAVKDAAGNVKEAV. The amino-terminal sequences of these proteins indicated that they were homologous to late embryogenesis abundant (LEA) proteins. Furthermore,the level of a 22-kDa protein also increased after 12 h. The amino-terminal sequence of this protein, AAPLVGGPAPDFTAAAVFD, indicated that it was homologous to thioredoxin peroxidase</description><identifier>ISSN: 0032-0781</identifier><identifier>ISSN: 1471-9053</identifier><identifier>EISSN: 1471-9053</identifier><identifier>DOI: 10.1093/oxfordjournals.pcp.a078904</identifier><identifier>PMID: 8589927</identifier><language>eng</language><publisher>Japan: Oxford University Press</publisher><subject>2D-HPLC ; Amino Acid Sequence ; Boiling-soluble protein ; Cells, Cultured ; Chlorella - chemistry ; CHLORELLA VULGARIS ; Chlorella vulgaris C-27 ; Chromatography, High Pressure Liquid ; DESARROLLO EMBRIONARIO ; DEVELOPPEMENT EMBRYONNAIRE ; DURCISSEMENT ; Electrophoresis, Polyacrylamide Gel ; ENDURECIMIENTO ; Freezing tolerance ; IDENTIFICACION ; IDENTIFICATION ; LEA protein ; Molecular Sequence Data ; Plant Proteins - chemistry ; Plant Proteins - isolation & purification ; POLIMORFISMO BIOQUIMICO ; POLYMORPHISME BIOCHIMIQUE ; PROTEINAS ; PROTEINE ; Solubility ; TECHNIQUE ANALYTIQUE ; TECNICAS ANALITICAS</subject><ispartof>Plant and cell physiology, 1995-12, Vol.36 (8), p.1421-1430</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8589927$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Honjoh, K. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Yoshimoto, M</creatorcontrib><creatorcontrib>Joh, T</creatorcontrib><creatorcontrib>Kajiwara, T</creatorcontrib><creatorcontrib>Miyamoto, T</creatorcontrib><creatorcontrib>Hatano, S</creatorcontrib><title>Isolation and characterization of hardening-induced proteins in Chlorella vulgaris C-27: Identification of late embryogenesis abundant proteins</title><title>Plant and cell physiology</title><addtitle>Plant Cell Physiol</addtitle><description>Hardening-induced soluble proteins of chlorella vulgaris beijerink IAM C-27 (formerly Chlorella ellipsoidea Gerneck IAM C-27) were isolated and purified by two-dimensional high-performance liquid chromatography (2D-HPLC) on an anion-exchange column, with subsequent reversed-phase chromatography. Some of the proteins were resolved by SDS-PAGE, characterized by amino-terminal sequencing and identified by searching for homologies in databases. Separation of the soluble proteins during the hardening of chlorella by a combination of 2D-HPLC and SDS-PAGE revealed that at least 31 proteins were induced or increased in abundance. Of particular interest was the induction after 12 h of a 10-kDa protein with the amino-terminal amino acid sequence AGNKPITEQISDAVGAAGQDVG and the induction after 6h of a 14-kDa protein with the amino-terminal sequence ALGEESLGDKAKNAFEDAKDAVKDAAGNVKEAV. The amino-terminal sequences of these proteins indicated that they were homologous to late embryogenesis abundant (LEA) proteins. Furthermore,the level of a 22-kDa protein also increased after 12 h. The amino-terminal sequence of this protein, AAPLVGGPAPDFTAAAVFD, indicated that it was homologous to thioredoxin peroxidase</description><subject>2D-HPLC</subject><subject>Amino Acid Sequence</subject><subject>Boiling-soluble protein</subject><subject>Cells, Cultured</subject><subject>Chlorella - chemistry</subject><subject>CHLORELLA VULGARIS</subject><subject>Chlorella vulgaris C-27</subject><subject>Chromatography, High Pressure Liquid</subject><subject>DESARROLLO EMBRIONARIO</subject><subject>DEVELOPPEMENT EMBRYONNAIRE</subject><subject>DURCISSEMENT</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>ENDURECIMIENTO</subject><subject>Freezing tolerance</subject><subject>IDENTIFICACION</subject><subject>IDENTIFICATION</subject><subject>LEA protein</subject><subject>Molecular Sequence Data</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - isolation & purification</subject><subject>POLIMORFISMO BIOQUIMICO</subject><subject>POLYMORPHISME BIOCHIMIQUE</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>Solubility</subject><subject>TECHNIQUE ANALYTIQUE</subject><subject>TECNICAS ANALITICAS</subject><issn>0032-0781</issn><issn>1471-9053</issn><issn>1471-9053</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUV1v1DAQtBCoHIU_gIRk8cBbDju-xHbf0AnooQKV-BDixdo466tLzr7aCWr5E_xlXOV0Ek-2dmZ3dmcIecnZkjMtXsdbF1N_HacUYMjLvd0vgUml2eoBWfCV5JVmjXhIFoyJuioIf0ye5HzNWPkLdkJOVKO0ruWC_N3kOMDoY6AQemqvIIEdMfk_czE6Wko9Bh-2lQ_9ZLGn-xRH9CFTH-j6aogJhwHo72nYQvKZrqtantFNaRq98_Y4qOggxV2X7uIWA-ZChW4KPYTxOPIpeeTKTfjs8J6Sb-_efl2fVxef32_Wby4qKxo1VlJ0zHIHTjoJVlq0K4EWXNuD5o1CaJhqBWtYDV2xjHMOjZNCSSHbUkVxSl7Nc4vwzYR5NDuf7f0dAeOUjZSqVm2tC_FsJtoUc07ozD75HaQ7w5m5T8P8n4YpaZhDGqX5xUFl6nbYH1sP9he8mnGfR7w9wpB-mbas2pjzHz_Nx--svvzyiRtW-M9nvoNoYFvMNh8udctaLWvxD7Bep8A</recordid><startdate>199512</startdate><enddate>199512</enddate><creator>Honjoh, K. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture)</creator><creator>Yoshimoto, M</creator><creator>Joh, T</creator><creator>Kajiwara, T</creator><creator>Miyamoto, T</creator><creator>Hatano, S</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</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>199512</creationdate><title>Isolation and characterization of hardening-induced proteins in Chlorella vulgaris C-27: Identification of late embryogenesis abundant proteins</title><author>Honjoh, K. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture) ; Yoshimoto, M ; Joh, T ; Kajiwara, T ; Miyamoto, T ; Hatano, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c358t-73b0c1faf7f7ac7cec43ecaf6da9158ea508630502ab109111a5f7387376050e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>2D-HPLC</topic><topic>Amino Acid Sequence</topic><topic>Boiling-soluble protein</topic><topic>Cells, Cultured</topic><topic>Chlorella - chemistry</topic><topic>CHLORELLA VULGARIS</topic><topic>Chlorella vulgaris C-27</topic><topic>Chromatography, High Pressure Liquid</topic><topic>DESARROLLO EMBRIONARIO</topic><topic>DEVELOPPEMENT EMBRYONNAIRE</topic><topic>DURCISSEMENT</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>ENDURECIMIENTO</topic><topic>Freezing tolerance</topic><topic>IDENTIFICACION</topic><topic>IDENTIFICATION</topic><topic>LEA protein</topic><topic>Molecular Sequence Data</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - isolation & purification</topic><topic>POLIMORFISMO BIOQUIMICO</topic><topic>POLYMORPHISME BIOCHIMIQUE</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>Solubility</topic><topic>TECHNIQUE ANALYTIQUE</topic><topic>TECNICAS ANALITICAS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Honjoh, K. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Yoshimoto, M</creatorcontrib><creatorcontrib>Joh, T</creatorcontrib><creatorcontrib>Kajiwara, T</creatorcontrib><creatorcontrib>Miyamoto, T</creatorcontrib><creatorcontrib>Hatano, S</creatorcontrib><collection>AGRIS</collection><collection>Istex</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>Plant and cell physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Honjoh, K. (Kyushu Univ., Fukuoka (Japan). Faculty of Agriculture)</au><au>Yoshimoto, M</au><au>Joh, T</au><au>Kajiwara, T</au><au>Miyamoto, T</au><au>Hatano, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of hardening-induced proteins in Chlorella vulgaris C-27: Identification of late embryogenesis abundant proteins</atitle><jtitle>Plant and cell physiology</jtitle><addtitle>Plant Cell Physiol</addtitle><date>1995-12</date><risdate>1995</risdate><volume>36</volume><issue>8</issue><spage>1421</spage><epage>1430</epage><pages>1421-1430</pages><issn>0032-0781</issn><issn>1471-9053</issn><eissn>1471-9053</eissn><abstract>Hardening-induced soluble proteins of chlorella vulgaris beijerink IAM C-27 (formerly Chlorella ellipsoidea Gerneck IAM C-27) were isolated and purified by two-dimensional high-performance liquid chromatography (2D-HPLC) on an anion-exchange column, with subsequent reversed-phase chromatography. Some of the proteins were resolved by SDS-PAGE, characterized by amino-terminal sequencing and identified by searching for homologies in databases. Separation of the soluble proteins during the hardening of chlorella by a combination of 2D-HPLC and SDS-PAGE revealed that at least 31 proteins were induced or increased in abundance. Of particular interest was the induction after 12 h of a 10-kDa protein with the amino-terminal amino acid sequence AGNKPITEQISDAVGAAGQDVG and the induction after 6h of a 14-kDa protein with the amino-terminal sequence ALGEESLGDKAKNAFEDAKDAVKDAAGNVKEAV. The amino-terminal sequences of these proteins indicated that they were homologous to late embryogenesis abundant (LEA) proteins. Furthermore,the level of a 22-kDa protein also increased after 12 h. The amino-terminal sequence of this protein, AAPLVGGPAPDFTAAAVFD, indicated that it was homologous to thioredoxin peroxidase</abstract><cop>Japan</cop><pub>Oxford University Press</pub><pmid>8589927</pmid><doi>10.1093/oxfordjournals.pcp.a078904</doi><tpages>10</tpages></addata></record> |
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subjects | 2D-HPLC Amino Acid Sequence Boiling-soluble protein Cells, Cultured Chlorella - chemistry CHLORELLA VULGARIS Chlorella vulgaris C-27 Chromatography, High Pressure Liquid DESARROLLO EMBRIONARIO DEVELOPPEMENT EMBRYONNAIRE DURCISSEMENT Electrophoresis, Polyacrylamide Gel ENDURECIMIENTO Freezing tolerance IDENTIFICACION IDENTIFICATION LEA protein Molecular Sequence Data Plant Proteins - chemistry Plant Proteins - isolation & purification POLIMORFISMO BIOQUIMICO POLYMORPHISME BIOCHIMIQUE PROTEINAS PROTEINE Solubility TECHNIQUE ANALYTIQUE TECNICAS ANALITICAS |
title | Isolation and characterization of hardening-induced proteins in Chlorella vulgaris C-27: Identification of late embryogenesis abundant proteins |
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