Covalent labeling of the beta-adrenergic ligand-binding site with para-(bromoacetamidyl)benzylcarazolol. A highly potent beta-adrenergic affinity label
para-(Bromoacetamidyl)benzylcarazolol (pBABC) was synthesized and found to be an extremely potent affinity label for beta-adrenergic receptors. Its interaction with mammalian (rabbit and hamster lung) and nonmammalian (turkey and frog erythrocyte) beta-adrenergic receptors was similar, displaying EC...
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| Veröffentlicht in: | Molecular pharmacology 1985-05, Vol.27 (5), p.499-506 |
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| creator | DICKINSON, K. E. J HEALD, S. L JEFFS, P. W LEFKOWITZ, R. J CARON, M. G |
| description | para-(Bromoacetamidyl)benzylcarazolol (pBABC) was synthesized and found to be an extremely potent affinity label for beta-adrenergic
receptors. Its interaction with mammalian (rabbit and hamster lung) and nonmammalian (turkey and frog erythrocyte) beta-adrenergic
receptors was similar, displaying EC50 values of 400-900 pM for inhibiting 125I-cyanopindolol binding to these receptors.
pBABC reduced the number of beta-adrenergic receptors in frog erythrocyte membranes, without any change in the affinity of
the remaining sites for [125I]iodocyanopindolol. pBABC has been radioiodinated. As assessed by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis, this affinity probe specifically labeled the beta-adrenergic peptide of a purified preparation of hamster
lung, with high efficiency (approximately 40%) and with a pharmacological specificity characteristic of an interaction at
the beta 2-adrenergic receptor ligand-binding site. Comparison of the proteolyzed products derived from purified receptor
labeled with [125I]pBABC and with the photoaffinity agent [125I]p-azidobenzylcarazolol suggested that covalent labeling of
the beta-adrenergic receptor by these probes occurs at similar domains of the beta-adrenergic receptor. Because of the much
higher level of incorporation of this affinity probe as opposed to photosensitive probes, pBABC should prove to be a useful
tool for structural studies of purified beta-adrenergic receptors. |
| format | Article |
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receptors. Its interaction with mammalian (rabbit and hamster lung) and nonmammalian (turkey and frog erythrocyte) beta-adrenergic
receptors was similar, displaying EC50 values of 400-900 pM for inhibiting 125I-cyanopindolol binding to these receptors.
pBABC reduced the number of beta-adrenergic receptors in frog erythrocyte membranes, without any change in the affinity of
the remaining sites for [125I]iodocyanopindolol. pBABC has been radioiodinated. As assessed by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis, this affinity probe specifically labeled the beta-adrenergic peptide of a purified preparation of hamster
lung, with high efficiency (approximately 40%) and with a pharmacological specificity characteristic of an interaction at
the beta 2-adrenergic receptor ligand-binding site. Comparison of the proteolyzed products derived from purified receptor
labeled with [125I]pBABC and with the photoaffinity agent [125I]p-azidobenzylcarazolol suggested that covalent labeling of
the beta-adrenergic receptor by these probes occurs at similar domains of the beta-adrenergic receptor. Because of the much
higher level of incorporation of this affinity probe as opposed to photosensitive probes, pBABC should prove to be a useful
tool for structural studies of purified beta-adrenergic receptors.</description><identifier>ISSN: 0026-895X</identifier><identifier>EISSN: 1521-0111</identifier><identifier>PMID: 2985948</identifier><identifier>CODEN: MOPMA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Pharmacology and Experimental Therapeutics</publisher><subject>Affinity Labels - metabolism ; Animals ; Biological and medical sciences ; Central nervous system ; Central neurotransmission. Neuromudulation. Pathways and receptors ; Cricetinae ; Fundamental and applied biological sciences. Psychology ; In Vitro Techniques ; Iodine Radioisotopes ; Iodocyanopindolol ; Ligands ; Lung - metabolism ; Pindolol - analogs & derivatives ; Pindolol - metabolism ; Propanolamines - metabolism ; Rabbits ; Receptors, Adrenergic, beta - drug effects ; Receptors, Adrenergic, beta - metabolism ; Vertebrates: nervous system and sense organs</subject><ispartof>Molecular pharmacology, 1985-05, Vol.27 (5), p.499-506</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8420473$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2985948$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>DICKINSON, K. E. J</creatorcontrib><creatorcontrib>HEALD, S. L</creatorcontrib><creatorcontrib>JEFFS, P. W</creatorcontrib><creatorcontrib>LEFKOWITZ, R. J</creatorcontrib><creatorcontrib>CARON, M. G</creatorcontrib><title>Covalent labeling of the beta-adrenergic ligand-binding site with para-(bromoacetamidyl)benzylcarazolol. A highly potent beta-adrenergic affinity label</title><title>Molecular pharmacology</title><addtitle>Mol Pharmacol</addtitle><description>para-(Bromoacetamidyl)benzylcarazolol (pBABC) was synthesized and found to be an extremely potent affinity label for beta-adrenergic
receptors. Its interaction with mammalian (rabbit and hamster lung) and nonmammalian (turkey and frog erythrocyte) beta-adrenergic
receptors was similar, displaying EC50 values of 400-900 pM for inhibiting 125I-cyanopindolol binding to these receptors.
pBABC reduced the number of beta-adrenergic receptors in frog erythrocyte membranes, without any change in the affinity of
the remaining sites for [125I]iodocyanopindolol. pBABC has been radioiodinated. As assessed by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis, this affinity probe specifically labeled the beta-adrenergic peptide of a purified preparation of hamster
lung, with high efficiency (approximately 40%) and with a pharmacological specificity characteristic of an interaction at
the beta 2-adrenergic receptor ligand-binding site. Comparison of the proteolyzed products derived from purified receptor
labeled with [125I]pBABC and with the photoaffinity agent [125I]p-azidobenzylcarazolol suggested that covalent labeling of
the beta-adrenergic receptor by these probes occurs at similar domains of the beta-adrenergic receptor. Because of the much
higher level of incorporation of this affinity probe as opposed to photosensitive probes, pBABC should prove to be a useful
tool for structural studies of purified beta-adrenergic receptors.</description><subject>Affinity Labels - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Central nervous system</subject><subject>Central neurotransmission. Neuromudulation. Pathways and receptors</subject><subject>Cricetinae</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>In Vitro Techniques</subject><subject>Iodine Radioisotopes</subject><subject>Iodocyanopindolol</subject><subject>Ligands</subject><subject>Lung - metabolism</subject><subject>Pindolol - analogs & derivatives</subject><subject>Pindolol - metabolism</subject><subject>Propanolamines - metabolism</subject><subject>Rabbits</subject><subject>Receptors, Adrenergic, beta - drug effects</subject><subject>Receptors, Adrenergic, beta - metabolism</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>0026-895X</issn><issn>1521-0111</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkM1q3DAURk1oSSdpHyGgRRqShYNkS7a0DEPzA4FuWujOXMmyrSJLjqRpcF4kr1sNM3TR1V185557-U6KDWEVKTEh5EOxwbhqSi7Yr0_FWYy_MSaUcXxanFaCM0H5pnjf-j9gtUvIgtTWuBH5AaVJI6kTlNAH7XQYjULWjOD6UhrX76lokkavJk1ogQDltQx-9qDy0mz61d5I7d5Wq3L25q23t-gOTWac7IoWn_b3_vfDMBhn0np45HPxcQAb9ZfjPC9-3n_7sX0sn78_PG3vnsupalgqe1zhRlDZKMWo4LTFtRKcUNm2ZBiEFFUra1VTaCTVGaO5jJbWjNe8aYiE-ry4OniX4F92OqZuNlFpa8Fpv4td22BOK8oyeHEEd3LWfbcEM0NYu2OTOb885hAV2CGAUyb-w7IE07bO2NcDti_j1QTdLROEGVQuacy2tmMdFaL-C34mjGE</recordid><startdate>198505</startdate><enddate>198505</enddate><creator>DICKINSON, K. E. J</creator><creator>HEALD, S. L</creator><creator>JEFFS, P. W</creator><creator>LEFKOWITZ, R. J</creator><creator>CARON, M. G</creator><general>American Society for Pharmacology and Experimental Therapeutics</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>198505</creationdate><title>Covalent labeling of the beta-adrenergic ligand-binding site with para-(bromoacetamidyl)benzylcarazolol. A highly potent beta-adrenergic affinity label</title><author>DICKINSON, K. E. J ; HEALD, S. L ; JEFFS, P. W ; LEFKOWITZ, R. J ; CARON, M. G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h265t-d020694b6cc54984703c9814b771ff9b927b3c34a6b4e4b648957435838661ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Affinity Labels - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Central nervous system</topic><topic>Central neurotransmission. Neuromudulation. Pathways and receptors</topic><topic>Cricetinae</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>In Vitro Techniques</topic><topic>Iodine Radioisotopes</topic><topic>Iodocyanopindolol</topic><topic>Ligands</topic><topic>Lung - metabolism</topic><topic>Pindolol - analogs & derivatives</topic><topic>Pindolol - metabolism</topic><topic>Propanolamines - metabolism</topic><topic>Rabbits</topic><topic>Receptors, Adrenergic, beta - drug effects</topic><topic>Receptors, Adrenergic, beta - metabolism</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>DICKINSON, K. E. J</creatorcontrib><creatorcontrib>HEALD, S. L</creatorcontrib><creatorcontrib>JEFFS, P. W</creatorcontrib><creatorcontrib>LEFKOWITZ, R. J</creatorcontrib><creatorcontrib>CARON, M. G</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>MEDLINE - Academic</collection><jtitle>Molecular pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>DICKINSON, K. E. J</au><au>HEALD, S. L</au><au>JEFFS, P. W</au><au>LEFKOWITZ, R. J</au><au>CARON, M. G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Covalent labeling of the beta-adrenergic ligand-binding site with para-(bromoacetamidyl)benzylcarazolol. A highly potent beta-adrenergic affinity label</atitle><jtitle>Molecular pharmacology</jtitle><addtitle>Mol Pharmacol</addtitle><date>1985-05</date><risdate>1985</risdate><volume>27</volume><issue>5</issue><spage>499</spage><epage>506</epage><pages>499-506</pages><issn>0026-895X</issn><eissn>1521-0111</eissn><coden>MOPMA3</coden><abstract>para-(Bromoacetamidyl)benzylcarazolol (pBABC) was synthesized and found to be an extremely potent affinity label for beta-adrenergic
receptors. Its interaction with mammalian (rabbit and hamster lung) and nonmammalian (turkey and frog erythrocyte) beta-adrenergic
receptors was similar, displaying EC50 values of 400-900 pM for inhibiting 125I-cyanopindolol binding to these receptors.
pBABC reduced the number of beta-adrenergic receptors in frog erythrocyte membranes, without any change in the affinity of
the remaining sites for [125I]iodocyanopindolol. pBABC has been radioiodinated. As assessed by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis, this affinity probe specifically labeled the beta-adrenergic peptide of a purified preparation of hamster
lung, with high efficiency (approximately 40%) and with a pharmacological specificity characteristic of an interaction at
the beta 2-adrenergic receptor ligand-binding site. Comparison of the proteolyzed products derived from purified receptor
labeled with [125I]pBABC and with the photoaffinity agent [125I]p-azidobenzylcarazolol suggested that covalent labeling of
the beta-adrenergic receptor by these probes occurs at similar domains of the beta-adrenergic receptor. Because of the much
higher level of incorporation of this affinity probe as opposed to photosensitive probes, pBABC should prove to be a useful
tool for structural studies of purified beta-adrenergic receptors.</abstract><cop>Bethesda, MD</cop><pub>American Society for Pharmacology and Experimental Therapeutics</pub><pmid>2985948</pmid><tpages>8</tpages></addata></record> |
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| ispartof | Molecular pharmacology, 1985-05, Vol.27 (5), p.499-506 |
| issn | 0026-895X 1521-0111 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | Affinity Labels - metabolism Animals Biological and medical sciences Central nervous system Central neurotransmission. Neuromudulation. Pathways and receptors Cricetinae Fundamental and applied biological sciences. Psychology In Vitro Techniques Iodine Radioisotopes Iodocyanopindolol Ligands Lung - metabolism Pindolol - analogs & derivatives Pindolol - metabolism Propanolamines - metabolism Rabbits Receptors, Adrenergic, beta - drug effects Receptors, Adrenergic, beta - metabolism Vertebrates: nervous system and sense organs |
| title | Covalent labeling of the beta-adrenergic ligand-binding site with para-(bromoacetamidyl)benzylcarazolol. A highly potent beta-adrenergic affinity label |
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