Fluorescein-labeled glutathione to study protein S-glutathionylation
Numerous studies of S-glutathionylation of cysteine thiols indicate that this protein modification plays a key role in redox regulation of proteins. To facilitate the study of protein S-glutathionylation, we developed a synthesis and purification to produce milligram quantities of fluorescein-labele...
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| Veröffentlicht in: | Analytical biochemistry 2010-07, Vol.402 (1), p.102-104 |
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| container_title | Analytical biochemistry |
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| creator | Landino, Lisa M. Brown, Carolyn M. Edson, Carolyn A. Gilbert, Laura J. Grega-Larson, Nathan Wirth, Anna Jean Lane, Kelly C. |
| description | Numerous studies of S-glutathionylation of cysteine thiols indicate that this protein modification plays a key role in redox regulation of proteins. To facilitate the study of protein S-glutathionylation, we developed a synthesis and purification to produce milligram quantities of fluorescein-labeled glutathione. The amino terminus of the glutathione tripeptide reacted with fluorescein isothiocyanate readily in ammonium bicarbonate. Purification by solid phase extraction on C8 and C18 columns separated excess reactants from desired products. Both oxidized and reduced fluorescein-labeled glutathione reacted with a variety of thiol-containing proteins to yield fluorescent proteins. |
| doi_str_mv | 10.1016/j.ab.2010.02.006 |
| format | Article |
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To facilitate the study of protein S-glutathionylation, we developed a synthesis and purification to produce milligram quantities of fluorescein-labeled glutathione. The amino terminus of the glutathione tripeptide reacted with fluorescein isothiocyanate readily in ammonium bicarbonate. Purification by solid phase extraction on C8 and C18 columns separated excess reactants from desired products. Both oxidized and reduced fluorescein-labeled glutathione reacted with a variety of thiol-containing proteins to yield fluorescent proteins.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/j.ab.2010.02.006</identifier><identifier>PMID: 20156418</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Fluorescein - chemistry ; Fluorescent Dyes - chemistry ; Glutathione - chemistry ; Glutathione - metabolism ; Oxidation-Reduction ; Proteins - metabolism ; Sulfhydryl Compounds - metabolism</subject><ispartof>Analytical biochemistry, 2010-07, Vol.402 (1), p.102-104</ispartof><rights>2010 Elsevier Inc.</rights><rights>2010 Elsevier Inc. 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To facilitate the study of protein S-glutathionylation, we developed a synthesis and purification to produce milligram quantities of fluorescein-labeled glutathione. The amino terminus of the glutathione tripeptide reacted with fluorescein isothiocyanate readily in ammonium bicarbonate. Purification by solid phase extraction on C8 and C18 columns separated excess reactants from desired products. Both oxidized and reduced fluorescein-labeled glutathione reacted with a variety of thiol-containing proteins to yield fluorescent proteins.</description><subject>Fluorescein - chemistry</subject><subject>Fluorescent Dyes - chemistry</subject><subject>Glutathione - chemistry</subject><subject>Glutathione - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Proteins - metabolism</subject><subject>Sulfhydryl Compounds - metabolism</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v3CAURVHUKpmk2XdVedeVJw-DMe6iUjX5qhSpi6RrhOE5YcSYKeBI8-9DNEnaLLp6Qu_cCxxCPlNYUqDibL3Uw7KBcoRmCSAOyIJCL2pg0H8gCwBgdSP67ogcp7QGoJS34pAclUgrOJULcn7p5xAxGXRT7fWAHm117-es84MLE1Y5VCnPdldtY8gFqm7rv-ud17mMT-TjqH3C05d5Qn5fXtytruubX1c_Vz9uasO5yLUe29H2LQy8lSCohaa1hknNNcNu6CwgSku5FZRrOY4SmAWujeiphLFDy07I933vdh42aA1OOWqvttFtdNypoJ16v5ncg7oPj6qRknWdLAVfXwpi-DNjymrjyte91xOGOamOMcapaPpCwp40MaQUcXy7hYJ6dq_WSg_q2b2CRhX3JfLl39e9BV5lF-DbHsDi6NFhVMk4nAxaF9FkZYP7f_sTDlGV1Q</recordid><startdate>20100701</startdate><enddate>20100701</enddate><creator>Landino, Lisa M.</creator><creator>Brown, Carolyn M.</creator><creator>Edson, Carolyn A.</creator><creator>Gilbert, Laura J.</creator><creator>Grega-Larson, Nathan</creator><creator>Wirth, Anna Jean</creator><creator>Lane, Kelly C.</creator><general>Elsevier Inc</general><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><scope>5PM</scope></search><sort><creationdate>20100701</creationdate><title>Fluorescein-labeled glutathione to study protein S-glutathionylation</title><author>Landino, Lisa M. ; Brown, Carolyn M. ; Edson, Carolyn A. ; Gilbert, Laura J. ; Grega-Larson, Nathan ; Wirth, Anna Jean ; Lane, Kelly C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-af5fd950b458061d025dc38a4a3e7b7d0ee8d14d614a8ff803d04ac69180f7ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Fluorescein - chemistry</topic><topic>Fluorescent Dyes - chemistry</topic><topic>Glutathione - chemistry</topic><topic>Glutathione - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Proteins - metabolism</topic><topic>Sulfhydryl Compounds - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Landino, Lisa M.</creatorcontrib><creatorcontrib>Brown, Carolyn M.</creatorcontrib><creatorcontrib>Edson, Carolyn A.</creatorcontrib><creatorcontrib>Gilbert, Laura J.</creatorcontrib><creatorcontrib>Grega-Larson, Nathan</creatorcontrib><creatorcontrib>Wirth, Anna Jean</creatorcontrib><creatorcontrib>Lane, Kelly C.</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Landino, Lisa M.</au><au>Brown, Carolyn M.</au><au>Edson, Carolyn A.</au><au>Gilbert, Laura J.</au><au>Grega-Larson, Nathan</au><au>Wirth, Anna Jean</au><au>Lane, Kelly C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fluorescein-labeled glutathione to study protein S-glutathionylation</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>2010-07-01</date><risdate>2010</risdate><volume>402</volume><issue>1</issue><spage>102</spage><epage>104</epage><pages>102-104</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>Numerous studies of S-glutathionylation of cysteine thiols indicate that this protein modification plays a key role in redox regulation of proteins. To facilitate the study of protein S-glutathionylation, we developed a synthesis and purification to produce milligram quantities of fluorescein-labeled glutathione. The amino terminus of the glutathione tripeptide reacted with fluorescein isothiocyanate readily in ammonium bicarbonate. Purification by solid phase extraction on C8 and C18 columns separated excess reactants from desired products. Both oxidized and reduced fluorescein-labeled glutathione reacted with a variety of thiol-containing proteins to yield fluorescent proteins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20156418</pmid><doi>10.1016/j.ab.2010.02.006</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0003-2697 |
| ispartof | Analytical biochemistry, 2010-07, Vol.402 (1), p.102-104 |
| issn | 0003-2697 1096-0309 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Fluorescein - chemistry Fluorescent Dyes - chemistry Glutathione - chemistry Glutathione - metabolism Oxidation-Reduction Proteins - metabolism Sulfhydryl Compounds - metabolism |
| title | Fluorescein-labeled glutathione to study protein S-glutathionylation |
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