The Dipeptide, γ-Glutamylcysteine, Is Recognized by the Anti-glutathione Antibody Single Chain Fv Fragment 20C9
The anti-glutathione antibody scFv 20C9, which we previously isolated from a human synthetic phage antibody scFv library [Hirose, M., Hayano, T., Shirai, H., Nakamura, H., and Kikuchi, M. (1998) Protein Eng. 11, 243–248], was expressed in the E. coli pET system and purified by sequential chromatogra...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2001-03, Vol.281 (5), p.1321-1324 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Horibe, Tomohisa Furuya, Rie Iwai, Akiyoshi Yosho, Chieko Tujimoto, Yoshiyuki Kikuchi, Masakazu |
| description | The anti-glutathione antibody scFv 20C9, which we previously isolated from a human synthetic phage antibody scFv library [Hirose, M., Hayano, T., Shirai, H., Nakamura, H., and Kikuchi, M. (1998) Protein Eng. 11, 243–248], was expressed in the E. coli pET system and purified by sequential chromatography on Ni and glutathione-conjugated affinity resins. The purified scFv 20C9 antibody was characterized for its binding affinity for several glutathione derivatives by the BIACORE system. Although GSH, GSSG, and γ-Glu-Cys could bind to the immobilized antibody, this was not the case for Cys-Gly, l-Glu, l-Cys, l-Gly, or several other glutathione derivatives such as γ-Glu-Ser-Gly. The results suggest that a γ-glutamic acid and sulfur atom are important for scFv 20C9 antibody recognition of glutathione. This is the first report to indicate that an scFv antibody can recognize a region as small as a dipeptide. |
| doi_str_mv | 10.1006/bbrc.2001.4491 |
| format | Article |
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(1998) Protein Eng. 11, 243–248], was expressed in the E. coli pET system and purified by sequential chromatography on Ni and glutathione-conjugated affinity resins. The purified scFv 20C9 antibody was characterized for its binding affinity for several glutathione derivatives by the BIACORE system. Although GSH, GSSG, and γ-Glu-Cys could bind to the immobilized antibody, this was not the case for Cys-Gly, l-Glu, l-Cys, l-Gly, or several other glutathione derivatives such as γ-Glu-Ser-Gly. The results suggest that a γ-glutamic acid and sulfur atom are important for scFv 20C9 antibody recognition of glutathione. This is the first report to indicate that an scFv antibody can recognize a region as small as a dipeptide.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2001.4491</identifier><identifier>PMID: 11243880</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>anti-glutathione antibody ; Antibodies, Monoclonal - genetics ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - metabolism ; Antibody Specificity ; BIACORE system ; Biosensing Techniques ; dipeptide ; Dipeptides - immunology ; Escherichia coli ; Glutathione - analogs & derivatives ; Glutathione - immunology ; Humans ; Immunoglobulin Fragments - genetics ; Immunoglobulin Fragments - immunology ; Immunoglobulin Fragments - metabolism ; Kinetics ; phage antibody scFv library ; Transfection</subject><ispartof>Biochemical and biophysical research communications, 2001-03, Vol.281 (5), p.1321-1324</ispartof><rights>2001 Academic Press</rights><rights>Copyright 2001 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-d5399520cc577ba1266d9c6be04c5c8a2538a664e75bdf18738e4006e193b56f3</citedby><cites>FETCH-LOGICAL-c340t-d5399520cc577ba1266d9c6be04c5c8a2538a664e75bdf18738e4006e193b56f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2001.4491$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11243880$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Horibe, Tomohisa</creatorcontrib><creatorcontrib>Furuya, Rie</creatorcontrib><creatorcontrib>Iwai, Akiyoshi</creatorcontrib><creatorcontrib>Yosho, Chieko</creatorcontrib><creatorcontrib>Tujimoto, Yoshiyuki</creatorcontrib><creatorcontrib>Kikuchi, Masakazu</creatorcontrib><title>The Dipeptide, γ-Glutamylcysteine, Is Recognized by the Anti-glutathione Antibody Single Chain Fv Fragment 20C9</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The anti-glutathione antibody scFv 20C9, which we previously isolated from a human synthetic phage antibody scFv library [Hirose, M., Hayano, T., Shirai, H., Nakamura, H., and Kikuchi, M. (1998) Protein Eng. 11, 243–248], was expressed in the E. coli pET system and purified by sequential chromatography on Ni and glutathione-conjugated affinity resins. The purified scFv 20C9 antibody was characterized for its binding affinity for several glutathione derivatives by the BIACORE system. Although GSH, GSSG, and γ-Glu-Cys could bind to the immobilized antibody, this was not the case for Cys-Gly, l-Glu, l-Cys, l-Gly, or several other glutathione derivatives such as γ-Glu-Ser-Gly. The results suggest that a γ-glutamic acid and sulfur atom are important for scFv 20C9 antibody recognition of glutathione. This is the first report to indicate that an scFv antibody can recognize a region as small as a dipeptide.</description><subject>anti-glutathione antibody</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Antibody Specificity</subject><subject>BIACORE system</subject><subject>Biosensing Techniques</subject><subject>dipeptide</subject><subject>Dipeptides - immunology</subject><subject>Escherichia coli</subject><subject>Glutathione - analogs & derivatives</subject><subject>Glutathione - immunology</subject><subject>Humans</subject><subject>Immunoglobulin Fragments - genetics</subject><subject>Immunoglobulin Fragments - immunology</subject><subject>Immunoglobulin Fragments - metabolism</subject><subject>Kinetics</subject><subject>phage antibody scFv library</subject><subject>Transfection</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM2KFDEUhYM4OO3o1qVk5WqqTaqSVGU5tPY4MCCMI7gL-bndHalKlUl6oHyteQ-fyRTd4MrVhcN3DtwPoXeUrCkh4qMx0a5rQuiaMUlfoBUlklQ1JewlWpFCVLWkPy7R65R-FooyIV-hS0pr1nQdWaHp8QD4k59gyt7BNf7zXN32x6yHubdzyuBDCe8SfgA77oP_DQ6bGedSugnZV_uFzQc_hlNgRjfjbz7se8Cbg_YBb5_wNur9ACHjmmzkG3Sx032Ct-d7hb5vPz9uvlT3X2_vNjf3lW0YyZXjjZS8JtbytjWa1kI4aYUBwiy3na5502khGLTcuB3t2qYDVt4FKhvDxa65Qh9Ou1Mcfx0hZTX4ZKHvdYDxmFQrJOdM8gKuT6CNY0oRdmqKftBxVpSoxbFaHKvFsVocl8L78_LRDOD-4WepBehOAJT_njxElayHYMH5CDYrN_r_bf8FiACKrg</recordid><startdate>200103</startdate><enddate>200103</enddate><creator>Horibe, Tomohisa</creator><creator>Furuya, Rie</creator><creator>Iwai, Akiyoshi</creator><creator>Yosho, Chieko</creator><creator>Tujimoto, Yoshiyuki</creator><creator>Kikuchi, Masakazu</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></search><sort><creationdate>200103</creationdate><title>The Dipeptide, γ-Glutamylcysteine, Is Recognized by the Anti-glutathione Antibody Single Chain Fv Fragment 20C9</title><author>Horibe, Tomohisa ; Furuya, Rie ; Iwai, Akiyoshi ; Yosho, Chieko ; Tujimoto, Yoshiyuki ; Kikuchi, Masakazu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-d5399520cc577ba1266d9c6be04c5c8a2538a664e75bdf18738e4006e193b56f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>anti-glutathione antibody</topic><topic>Antibodies, Monoclonal - genetics</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Antibody Specificity</topic><topic>BIACORE system</topic><topic>Biosensing Techniques</topic><topic>dipeptide</topic><topic>Dipeptides - immunology</topic><topic>Escherichia coli</topic><topic>Glutathione - analogs & derivatives</topic><topic>Glutathione - immunology</topic><topic>Humans</topic><topic>Immunoglobulin Fragments - genetics</topic><topic>Immunoglobulin Fragments - immunology</topic><topic>Immunoglobulin Fragments - metabolism</topic><topic>Kinetics</topic><topic>phage antibody scFv library</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Horibe, Tomohisa</creatorcontrib><creatorcontrib>Furuya, Rie</creatorcontrib><creatorcontrib>Iwai, Akiyoshi</creatorcontrib><creatorcontrib>Yosho, Chieko</creatorcontrib><creatorcontrib>Tujimoto, Yoshiyuki</creatorcontrib><creatorcontrib>Kikuchi, Masakazu</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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Horibe, Tomohisa</au><au>Furuya, Rie</au><au>Iwai, Akiyoshi</au><au>Yosho, Chieko</au><au>Tujimoto, Yoshiyuki</au><au>Kikuchi, Masakazu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Dipeptide, γ-Glutamylcysteine, Is Recognized by the Anti-glutathione Antibody Single Chain Fv Fragment 20C9</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2001-03</date><risdate>2001</risdate><volume>281</volume><issue>5</issue><spage>1321</spage><epage>1324</epage><pages>1321-1324</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The anti-glutathione antibody scFv 20C9, which we previously isolated from a human synthetic phage antibody scFv library [Hirose, M., Hayano, T., Shirai, H., Nakamura, H., and Kikuchi, M. (1998) Protein Eng. 11, 243–248], was expressed in the E. coli pET system and purified by sequential chromatography on Ni and glutathione-conjugated affinity resins. The purified scFv 20C9 antibody was characterized for its binding affinity for several glutathione derivatives by the BIACORE system. Although GSH, GSSG, and γ-Glu-Cys could bind to the immobilized antibody, this was not the case for Cys-Gly, l-Glu, l-Cys, l-Gly, or several other glutathione derivatives such as γ-Glu-Ser-Gly. The results suggest that a γ-glutamic acid and sulfur atom are important for scFv 20C9 antibody recognition of glutathione. This is the first report to indicate that an scFv antibody can recognize a region as small as a dipeptide.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11243880</pmid><doi>10.1006/bbrc.2001.4491</doi><tpages>4</tpages></addata></record> |
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| subjects | anti-glutathione antibody Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antibodies, Monoclonal - metabolism Antibody Specificity BIACORE system Biosensing Techniques dipeptide Dipeptides - immunology Escherichia coli Glutathione - analogs & derivatives Glutathione - immunology Humans Immunoglobulin Fragments - genetics Immunoglobulin Fragments - immunology Immunoglobulin Fragments - metabolism Kinetics phage antibody scFv library Transfection |
| title | The Dipeptide, γ-Glutamylcysteine, Is Recognized by the Anti-glutathione Antibody Single Chain Fv Fragment 20C9 |
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