Determination of the liver cytosolic proteins that bind to p-hydroxyacetophenone
The purpose of the present study was to determine the proteins that bind to acetophenones in the liver. Immobilized p‐hydroxyacetophenone (p‐HAP) was used as a ligand of affinity chromatography. Analysis using sodium dodesyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) demonstrated that five...
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| Veröffentlicht in: | Biomedical chromatography 2004-06, Vol.18 (5), p.335-340 |
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| creator | Negoro, Munetaka Wakabayashi, Ichiro |
| description | The purpose of the present study was to determine the proteins that bind to acetophenones in the liver. Immobilized p‐hydroxyacetophenone (p‐HAP) was used as a ligand of affinity chromatography. Analysis using sodium dodesyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) demonstrated that five polypeptides in the liver cytosolic fraction specifically bound to the p‐HAP matrix. These polypeptides were digested with Lys‐specific protease and used to generate peptide maps by reversed‐phase high‐performance liquid chromatography. Consequently, identification from a data base of protein sequences revealed that the five polypeptides were glycogen phosphorylase, cytosolic aldehyde dehydrogenase, adenosine kinase, class I alcohol dehydrogenase and glutathione S‐transferase A2. In addition to p‐HAP, acetylsalicylic acid also displayed a prominent ability to elute these five enzymes from the p‐HAP affinity column loaded with the cytosolic fraction of the liver. Thus, p‐HAP has affinities to the above liver enzymes and is a useful ligand for analysis of them. Copyright © 2004 John Wiley & Sons, Ltd. |
| doi_str_mv | 10.1002/bmc.340 |
| format | Article |
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Immobilized p‐hydroxyacetophenone (p‐HAP) was used as a ligand of affinity chromatography. Analysis using sodium dodesyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) demonstrated that five polypeptides in the liver cytosolic fraction specifically bound to the p‐HAP matrix. These polypeptides were digested with Lys‐specific protease and used to generate peptide maps by reversed‐phase high‐performance liquid chromatography. Consequently, identification from a data base of protein sequences revealed that the five polypeptides were glycogen phosphorylase, cytosolic aldehyde dehydrogenase, adenosine kinase, class I alcohol dehydrogenase and glutathione S‐transferase A2. In addition to p‐HAP, acetylsalicylic acid also displayed a prominent ability to elute these five enzymes from the p‐HAP affinity column loaded with the cytosolic fraction of the liver. Thus, p‐HAP has affinities to the above liver enzymes and is a useful ligand for analysis of them. Copyright © 2004 John Wiley & Sons, Ltd.</description><identifier>ISSN: 0269-3879</identifier><identifier>EISSN: 1099-0801</identifier><identifier>DOI: 10.1002/bmc.340</identifier><identifier>PMID: 15236443</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Acetophenones - metabolism ; acetylsalicylic acid ; adenosine kinase ; alcohol dehydrogenase ; aldehyde dehydrogenase ; Amino Acid Sequence ; Animals ; Chromatography, Affinity ; Cytosol - metabolism ; Electrophoresis, Polyacrylamide Gel ; glutathione S-transferase A2 ; glycogen phosphorylase ; Liver - metabolism ; Molecular Sequence Data ; p-hydroxyacetophenone ; Protein Binding ; Proteins - chemistry ; Proteins - metabolism ; Rabbits ; Sequence Homology, Amino Acid</subject><ispartof>Biomedical chromatography, 2004-06, Vol.18 (5), p.335-340</ispartof><rights>Copyright © 2004 John Wiley & Sons, Ltd.</rights><rights>Copyright 2004 John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3510-d91a75c2b8ef12e8922b9d9c0c1be7dc92022682cfd6afdf179b9694d576dcc3</citedby><cites>FETCH-LOGICAL-c3510-d91a75c2b8ef12e8922b9d9c0c1be7dc92022682cfd6afdf179b9694d576dcc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbmc.340$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbmc.340$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15236443$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Negoro, Munetaka</creatorcontrib><creatorcontrib>Wakabayashi, Ichiro</creatorcontrib><title>Determination of the liver cytosolic proteins that bind to p-hydroxyacetophenone</title><title>Biomedical chromatography</title><addtitle>Biomed. Chromatogr</addtitle><description>The purpose of the present study was to determine the proteins that bind to acetophenones in the liver. Immobilized p‐hydroxyacetophenone (p‐HAP) was used as a ligand of affinity chromatography. Analysis using sodium dodesyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) demonstrated that five polypeptides in the liver cytosolic fraction specifically bound to the p‐HAP matrix. These polypeptides were digested with Lys‐specific protease and used to generate peptide maps by reversed‐phase high‐performance liquid chromatography. Consequently, identification from a data base of protein sequences revealed that the five polypeptides were glycogen phosphorylase, cytosolic aldehyde dehydrogenase, adenosine kinase, class I alcohol dehydrogenase and glutathione S‐transferase A2. In addition to p‐HAP, acetylsalicylic acid also displayed a prominent ability to elute these five enzymes from the p‐HAP affinity column loaded with the cytosolic fraction of the liver. Thus, p‐HAP has affinities to the above liver enzymes and is a useful ligand for analysis of them. Copyright © 2004 John Wiley & Sons, Ltd.</description><subject>Acetophenones - metabolism</subject><subject>acetylsalicylic acid</subject><subject>adenosine kinase</subject><subject>alcohol dehydrogenase</subject><subject>aldehyde dehydrogenase</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Chromatography, Affinity</subject><subject>Cytosol - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>glutathione S-transferase A2</subject><subject>glycogen phosphorylase</subject><subject>Liver - metabolism</subject><subject>Molecular Sequence Data</subject><subject>p-hydroxyacetophenone</subject><subject>Protein Binding</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Rabbits</subject><subject>Sequence Homology, Amino Acid</subject><issn>0269-3879</issn><issn>1099-0801</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10EuP0zAUhmELMaKdgvgHKCtmgdLxJbHjJXToXFQuEhUsLcc-UQ1JHGx3ZvLvCUoFq1l54Uevjj6EXhO8JhjTy7oza1bgZ2hJsJQ5rjB5jpaYcpmzSsgFOo_xJ8ZYcipeoAUpKeNFwZbo6xUkCJ3rdXK-z3yTpQNkrbuHkJkx-ehbZ7Ih-ASuj9OnTlntepslnw35YbTBP47aQPLDAXrfw0t01ug2wqvTu0L77cf95ibffbm-3bzf5YaVBOdWEi1KQ-sKGkKhkpTW0kqDDalBWCMpppRX1DSW68Y2RMhaclnYUnBrDFuht3N2Ou33EWJSnYsG2lb34I9Rcc4FxyWf4MUMTfAxBmjUEFynw6gIVn-3U9N2atpukm9OyWPdgf3vTmNN4N0MHlwL41Md9eHTZs7ls3YxweM_rcMvxQUTpfrx-VqV228338V2r-7YHx_xiAA</recordid><startdate>200406</startdate><enddate>200406</enddate><creator>Negoro, Munetaka</creator><creator>Wakabayashi, Ichiro</creator><general>John Wiley & Sons, Ltd</general><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>200406</creationdate><title>Determination of the liver cytosolic proteins that bind to p-hydroxyacetophenone</title><author>Negoro, Munetaka ; Wakabayashi, Ichiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3510-d91a75c2b8ef12e8922b9d9c0c1be7dc92022682cfd6afdf179b9694d576dcc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acetophenones - metabolism</topic><topic>acetylsalicylic acid</topic><topic>adenosine kinase</topic><topic>alcohol dehydrogenase</topic><topic>aldehyde dehydrogenase</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Chromatography, Affinity</topic><topic>Cytosol - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>glutathione S-transferase A2</topic><topic>glycogen phosphorylase</topic><topic>Liver - metabolism</topic><topic>Molecular Sequence Data</topic><topic>p-hydroxyacetophenone</topic><topic>Protein Binding</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Rabbits</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Negoro, Munetaka</creatorcontrib><creatorcontrib>Wakabayashi, Ichiro</creatorcontrib><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>Biomedical chromatography</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Negoro, Munetaka</au><au>Wakabayashi, Ichiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Determination of the liver cytosolic proteins that bind to p-hydroxyacetophenone</atitle><jtitle>Biomedical chromatography</jtitle><addtitle>Biomed. Chromatogr</addtitle><date>2004-06</date><risdate>2004</risdate><volume>18</volume><issue>5</issue><spage>335</spage><epage>340</epage><pages>335-340</pages><issn>0269-3879</issn><eissn>1099-0801</eissn><abstract>The purpose of the present study was to determine the proteins that bind to acetophenones in the liver. Immobilized p‐hydroxyacetophenone (p‐HAP) was used as a ligand of affinity chromatography. Analysis using sodium dodesyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) demonstrated that five polypeptides in the liver cytosolic fraction specifically bound to the p‐HAP matrix. These polypeptides were digested with Lys‐specific protease and used to generate peptide maps by reversed‐phase high‐performance liquid chromatography. Consequently, identification from a data base of protein sequences revealed that the five polypeptides were glycogen phosphorylase, cytosolic aldehyde dehydrogenase, adenosine kinase, class I alcohol dehydrogenase and glutathione S‐transferase A2. 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| ispartof | Biomedical chromatography, 2004-06, Vol.18 (5), p.335-340 |
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| source | MEDLINE; Wiley Online Library All Journals |
| subjects | Acetophenones - metabolism acetylsalicylic acid adenosine kinase alcohol dehydrogenase aldehyde dehydrogenase Amino Acid Sequence Animals Chromatography, Affinity Cytosol - metabolism Electrophoresis, Polyacrylamide Gel glutathione S-transferase A2 glycogen phosphorylase Liver - metabolism Molecular Sequence Data p-hydroxyacetophenone Protein Binding Proteins - chemistry Proteins - metabolism Rabbits Sequence Homology, Amino Acid |
| title | Determination of the liver cytosolic proteins that bind to p-hydroxyacetophenone |
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