Identification and localization of the first glutaredoxin in leaves of a higher plant
Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a si...
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| Veröffentlicht in: | FEBS letters 1995-08, Vol.369 (2), p.149-152 |
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| creator | Morell, S. Follmann, H. Häberlein, I. |
| description | Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a significant crossreactivity with antibodies raised against
E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the
E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm). |
| doi_str_mv | 10.1016/0014-5793(95)00690-B |
| format | Article |
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E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the
E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm).</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)00690-B</identifier><identifier>PMID: 7649248</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>alpha-Amylases - antagonists & inhibitors ; Amino Acid Sequence ; Bacterial Proteins - metabolism ; Chloroplasts - enzymology ; Cross Reactions ; Enzyme Inhibitors - metabolism ; Escherichia coli - chemistry ; Glutaredoxin ; Glutaredoxins ; Localization ; Molecular Sequence Data ; Molecular Weight ; Oxidoreductases - chemistry ; Oxidoreductases - immunology ; Oxidoreductases - isolation & purification ; Oxidoreductases - metabolism ; Plant Leaves - enzymology ; Plant Proteins - chemistry ; Plant Proteins - immunology ; Plant Proteins - isolation & purification ; Plant Proteins - metabolism ; Protein Disulfide Reductase (Glutathione) ; Proteins - immunology ; Proteins - metabolism ; Spinach leave ; Spinacia oleracea - enzymology ; Thioredoxin ; Trypsin Inhibitors</subject><ispartof>FEBS letters, 1995-08, Vol.369 (2), p.149-152</ispartof><rights>1995</rights><rights>FEBS Letters 369 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c466B-e89a37cb5a7e0f4f20527434801a196134409eae09271437213e473e7205ed663</citedby><cites>FETCH-LOGICAL-c466B-e89a37cb5a7e0f4f20527434801a196134409eae09271437213e473e7205ed663</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(95)00690-B$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7649248$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Morell, S.</creatorcontrib><creatorcontrib>Follmann, H.</creatorcontrib><creatorcontrib>Häberlein, I.</creatorcontrib><title>Identification and localization of the first glutaredoxin in leaves of a higher plant</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a significant crossreactivity with antibodies raised against
E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the
E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm).</description><subject>alpha-Amylases - antagonists & inhibitors</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - metabolism</subject><subject>Chloroplasts - enzymology</subject><subject>Cross Reactions</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Escherichia coli - chemistry</subject><subject>Glutaredoxin</subject><subject>Glutaredoxins</subject><subject>Localization</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - immunology</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Oxidoreductases - metabolism</subject><subject>Plant Leaves - enzymology</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - immunology</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plant Proteins - metabolism</subject><subject>Protein Disulfide Reductase (Glutathione)</subject><subject>Proteins - immunology</subject><subject>Proteins - metabolism</subject><subject>Spinach leave</subject><subject>Spinacia oleracea - enzymology</subject><subject>Thioredoxin</subject><subject>Trypsin Inhibitors</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkF9LwzAUxYMoOqffQKFPog_VpEmT5kVwsqkw8MU9hyy9dZGsnUk3_3x603X4KEIg5J5zz735IXRG8DXBhN9gTFiaC0kvZX6FMZc4He2hASkETSnjxT4a_FqO0HEIbzi-CyIP0aHgTGasGKDZUwl1aytrdGubOtF1mbjGaGe_-0JTJe0Cksr60Cavbt1qD2XzaeskHgd6A6Hz6GRhXxfgk5XTdXuCDirtApzu7iGaTcYv94_p9Pnh6f5umhrG-SiFQmoqzDzXAnDFqgznmWCUFZhoIjmhjGEJGrDMBGFUZIQCExRENELJOR2iiz535Zv3NYRWLW0w4OIO0KyDEoLlPH40GllvNL4JwUOlVt4utf9SBKuOpupQqQ6Vkrna0lSj2Ha-y1_Pl1D-Nu3wRX3S6x_Wwde_MtVkPMo6oavLfFvtBt32QRBpbSx4FYyF2kBpPZhWlY39e9MfkTyV6A</recordid><startdate>19950807</startdate><enddate>19950807</enddate><creator>Morell, S.</creator><creator>Follmann, H.</creator><creator>Häberlein, I.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19950807</creationdate><title>Identification and localization of the first glutaredoxin in leaves of a higher plant</title><author>Morell, S. ; Follmann, H. ; Häberlein, I.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c466B-e89a37cb5a7e0f4f20527434801a196134409eae09271437213e473e7205ed663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>alpha-Amylases - antagonists & inhibitors</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - metabolism</topic><topic>Chloroplasts - enzymology</topic><topic>Cross Reactions</topic><topic>Enzyme Inhibitors - metabolism</topic><topic>Escherichia coli - chemistry</topic><topic>Glutaredoxin</topic><topic>Glutaredoxins</topic><topic>Localization</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxidoreductases - immunology</topic><topic>Oxidoreductases - isolation & purification</topic><topic>Oxidoreductases - metabolism</topic><topic>Plant Leaves - enzymology</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - immunology</topic><topic>Plant Proteins - isolation & purification</topic><topic>Plant Proteins - metabolism</topic><topic>Protein Disulfide Reductase (Glutathione)</topic><topic>Proteins - immunology</topic><topic>Proteins - metabolism</topic><topic>Spinach leave</topic><topic>Spinacia oleracea - enzymology</topic><topic>Thioredoxin</topic><topic>Trypsin Inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Morell, S.</creatorcontrib><creatorcontrib>Follmann, H.</creatorcontrib><creatorcontrib>Häberlein, I.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Morell, S.</au><au>Follmann, H.</au><au>Häberlein, I.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and localization of the first glutaredoxin in leaves of a higher plant</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-08-07</date><risdate>1995</risdate><volume>369</volume><issue>2</issue><spage>149</spage><epage>152</epage><pages>149-152</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a significant crossreactivity with antibodies raised against
E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the
E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm).</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7649248</pmid><doi>10.1016/0014-5793(95)00690-B</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | FEBS letters, 1995-08, Vol.369 (2), p.149-152 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77456924 |
| source | MEDLINE; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | alpha-Amylases - antagonists & inhibitors Amino Acid Sequence Bacterial Proteins - metabolism Chloroplasts - enzymology Cross Reactions Enzyme Inhibitors - metabolism Escherichia coli - chemistry Glutaredoxin Glutaredoxins Localization Molecular Sequence Data Molecular Weight Oxidoreductases - chemistry Oxidoreductases - immunology Oxidoreductases - isolation & purification Oxidoreductases - metabolism Plant Leaves - enzymology Plant Proteins - chemistry Plant Proteins - immunology Plant Proteins - isolation & purification Plant Proteins - metabolism Protein Disulfide Reductase (Glutathione) Proteins - immunology Proteins - metabolism Spinach leave Spinacia oleracea - enzymology Thioredoxin Trypsin Inhibitors |
| title | Identification and localization of the first glutaredoxin in leaves of a higher plant |
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