A metabolite of acetaminophen covalently binds to the 56 kDa selenium binding protein
Acetaminophen is metabolized by cytochrome P450 to a reactive metabolite that covalently binds to proteins and this binding correlates with the hepatotoxicity. The major protein adduct was previously reported to be a 55 kDa protein that was detected on Western blots using antisera specific for 3-(cy...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1992-02, Vol.182 (3), p.1348-1355 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Pumford, Neil R. Martin, Brian M. Hinson, Jack A. |
| description | Acetaminophen is metabolized by cytochrome P450 to a reactive metabolite that covalently binds to proteins and this binding correlates with the hepatotoxicity. The major protein adduct was previously reported to be a 55 kDa protein that was detected on Western blots using antisera specific for 3-(cystein-
S-yl)acetaminophen. In this study, the 55 kDa protein was isolated using a combination of ion exchange fast flow chromatography, hydroxyapatite HPLC and anion exchange HPLC. Amino acid sequences of 8 internal peptides from a trypsin digestion of the 55 kDa protein were found to have 97% homology with the deduced amino acid sequence from a cDNA that corresponds to a 56 kDa selenium binding protein. This is the first report of a specific protein to which a metabolite of acetaminophen covalently binds. |
| doi_str_mv | 10.1016/0006-291X(92)91881-P |
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S-yl)acetaminophen. In this study, the 55 kDa protein was isolated using a combination of ion exchange fast flow chromatography, hydroxyapatite HPLC and anion exchange HPLC. Amino acid sequences of 8 internal peptides from a trypsin digestion of the 55 kDa protein were found to have 97% homology with the deduced amino acid sequence from a cDNA that corresponds to a 56 kDa selenium binding protein. This is the first report of a specific protein to which a metabolite of acetaminophen covalently binds.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(92)91881-P</identifier><identifier>PMID: 1540179</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Acetaminophen - analogs & derivatives ; Acetaminophen - metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Biological and medical sciences ; Biotransformation ; Carrier Proteins - genetics ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Cell Fractionation ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Cytosol - metabolism ; Drug toxicity and drugs side effects treatment ; Immune Sera ; Liver - metabolism ; Male ; Medical sciences ; Mice ; Mice, Inbred Strains ; Molecular Sequence Data ; Molecular Weight ; Peptide Fragments - isolation & purification ; Pharmacology. Drug treatments ; Selenium - isolation & purification ; Selenium - metabolism ; Selenium-Binding Proteins ; Sequence Homology, Nucleic Acid ; Toxicity: digestive system ; Ultrafiltration</subject><ispartof>Biochemical and biophysical research communications, 1992-02, Vol.182 (3), p.1348-1355</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-218882a3c0acba02341933bfc7273f9829900569faf96a428f70a6cbdce9c1173</citedby><cites>FETCH-LOGICAL-c503t-218882a3c0acba02341933bfc7273f9829900569faf96a428f70a6cbdce9c1173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(92)91881-P$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5196728$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1540179$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pumford, Neil R.</creatorcontrib><creatorcontrib>Martin, Brian M.</creatorcontrib><creatorcontrib>Hinson, Jack A.</creatorcontrib><title>A metabolite of acetaminophen covalently binds to the 56 kDa selenium binding protein</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Acetaminophen is metabolized by cytochrome P450 to a reactive metabolite that covalently binds to proteins and this binding correlates with the hepatotoxicity. The major protein adduct was previously reported to be a 55 kDa protein that was detected on Western blots using antisera specific for 3-(cystein-
S-yl)acetaminophen. In this study, the 55 kDa protein was isolated using a combination of ion exchange fast flow chromatography, hydroxyapatite HPLC and anion exchange HPLC. Amino acid sequences of 8 internal peptides from a trypsin digestion of the 55 kDa protein were found to have 97% homology with the deduced amino acid sequence from a cDNA that corresponds to a 56 kDa selenium binding protein. This is the first report of a specific protein to which a metabolite of acetaminophen covalently binds.</description><subject>Acetaminophen - analogs & derivatives</subject><subject>Acetaminophen - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Biotransformation</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Fractionation</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Ion Exchange</subject><subject>Cytosol - metabolism</subject><subject>Drug toxicity and drugs side effects treatment</subject><subject>Immune Sera</subject><subject>Liver - metabolism</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred Strains</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - isolation & purification</subject><subject>Pharmacology. Drug treatments</subject><subject>Selenium - isolation & purification</subject><subject>Selenium - metabolism</subject><subject>Selenium-Binding Proteins</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Toxicity: digestive system</subject><subject>Ultrafiltration</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtqHDEQRUVIcCZ2_sABLUJIFh1XqV_SxmCcJxjiRQzZCbW6ZMvulsYtjcF_H41ncHZZieKeKl0OY8cInxGwOwGArhIK_3xU4pNCKbG6fMFWCAoqgdC8ZKtn5DV7k9ItAGLTqQN2gG0D2KsVuzrjM2UzxMln4tFxY8s4-xDXNxS4jQ9mopCnRz74MCaeI883xNuO330xPFEJ_WZ-Cn245uslZvLhiL1yZkr0dv8esqtvX3-f_6gufn3_eX52UdkW6lxaSimFqS0YOxgQdYOqrgdne9HXTkmhFEDbKWec6kwjpOvBdHYYLSmL2NeH7MPubvn3fkMp69knS9NkAsVN0r2QAupWFrDZgXaJKS3k9Hrxs1keNYLe2tRbVXqrSiuhn2zqy7L2bn9_M8w0_lva6Sv5-31ukjWTW0ywPj1jLaquVCjY6Q6j4uLB06KT9RQsjX4hm_UY_f97_AXQHZBO</recordid><startdate>19920214</startdate><enddate>19920214</enddate><creator>Pumford, Neil R.</creator><creator>Martin, Brian M.</creator><creator>Hinson, Jack A.</creator><general>Elsevier Inc</general><general>Elsevier</general><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>7X8</scope></search><sort><creationdate>19920214</creationdate><title>A metabolite of acetaminophen covalently binds to the 56 kDa selenium binding protein</title><author>Pumford, Neil R. ; Martin, Brian M. ; Hinson, Jack A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-218882a3c0acba02341933bfc7273f9829900569faf96a428f70a6cbdce9c1173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Acetaminophen - analogs & derivatives</topic><topic>Acetaminophen - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Biotransformation</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Fractionation</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Ion Exchange</topic><topic>Cytosol - metabolism</topic><topic>Drug toxicity and drugs side effects treatment</topic><topic>Immune Sera</topic><topic>Liver - metabolism</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred Strains</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - isolation & purification</topic><topic>Pharmacology. Drug treatments</topic><topic>Selenium - isolation & purification</topic><topic>Selenium - metabolism</topic><topic>Selenium-Binding Proteins</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Toxicity: digestive system</topic><topic>Ultrafiltration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pumford, Neil R.</creatorcontrib><creatorcontrib>Martin, Brian M.</creatorcontrib><creatorcontrib>Hinson, Jack A.</creatorcontrib><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>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pumford, Neil R.</au><au>Martin, Brian M.</au><au>Hinson, Jack A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A metabolite of acetaminophen covalently binds to the 56 kDa selenium binding protein</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1992-02-14</date><risdate>1992</risdate><volume>182</volume><issue>3</issue><spage>1348</spage><epage>1355</epage><pages>1348-1355</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Acetaminophen is metabolized by cytochrome P450 to a reactive metabolite that covalently binds to proteins and this binding correlates with the hepatotoxicity. The major protein adduct was previously reported to be a 55 kDa protein that was detected on Western blots using antisera specific for 3-(cystein-
S-yl)acetaminophen. In this study, the 55 kDa protein was isolated using a combination of ion exchange fast flow chromatography, hydroxyapatite HPLC and anion exchange HPLC. Amino acid sequences of 8 internal peptides from a trypsin digestion of the 55 kDa protein were found to have 97% homology with the deduced amino acid sequence from a cDNA that corresponds to a 56 kDa selenium binding protein. This is the first report of a specific protein to which a metabolite of acetaminophen covalently binds.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1540179</pmid><doi>10.1016/0006-291X(92)91881-P</doi><tpages>8</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Acetaminophen - analogs & derivatives Acetaminophen - metabolism Amino Acid Sequence Animals Binding Sites Biological and medical sciences Biotransformation Carrier Proteins - genetics Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cell Fractionation Chromatography, High Pressure Liquid Chromatography, Ion Exchange Cytosol - metabolism Drug toxicity and drugs side effects treatment Immune Sera Liver - metabolism Male Medical sciences Mice Mice, Inbred Strains Molecular Sequence Data Molecular Weight Peptide Fragments - isolation & purification Pharmacology. Drug treatments Selenium - isolation & purification Selenium - metabolism Selenium-Binding Proteins Sequence Homology, Nucleic Acid Toxicity: digestive system Ultrafiltration |
| title | A metabolite of acetaminophen covalently binds to the 56 kDa selenium binding protein |
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