Identification of a receptor for atrial natriuretic factor in rabbit aorta membranes by affinity cross-linking
Binding sites in rabbit aorta membranes for atrial natriuretic factor (ANF) have been specifically and covalently labeled by two methods. In the first, the photoreactive analog of ANF, 125I-azidobenzoyl-ANF, was synthesized and used to photoaffinity label ANF receptors. In the second, 125I-ANF was c...
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Veröffentlicht in: | The Journal of biological chemistry 1985-09, Vol.260 (20), p.10889-10892 |
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description | Binding sites in rabbit aorta membranes for atrial natriuretic factor (ANF) have been specifically and covalently labeled by two methods. In the first, the photoreactive analog of ANF, 125I-azidobenzoyl-ANF, was synthesized and used to photoaffinity label ANF receptors. In the second, 125I-ANF was covalently attached to its binding site by treatment of the 125I-ANF-receptor complex with bifunctional cross-linking agents. Analysis of the labeled proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography revealed that by both methods the same three protein bands were labeled. These bands had apparent molecular masses of 60,000, 70,000, and 120,000 daltons. With the photoaffinity label, half-maximal inhibition of labeling of each of these bands was achieved when approximately 200 pM of unlabeled ANF was included in the binding assay. These results suggest that these three different polypeptides are specific components of ANF receptors in rabbit aorta membranes. |
doi_str_mv | 10.1016/S0021-9258(17)39114-7 |
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In the first, the photoreactive analog of ANF, 125I-azidobenzoyl-ANF, was synthesized and used to photoaffinity label ANF receptors. In the second, 125I-ANF was covalently attached to its binding site by treatment of the 125I-ANF-receptor complex with bifunctional cross-linking agents. Analysis of the labeled proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography revealed that by both methods the same three protein bands were labeled. These bands had apparent molecular masses of 60,000, 70,000, and 120,000 daltons. With the photoaffinity label, half-maximal inhibition of labeling of each of these bands was achieved when approximately 200 pM of unlabeled ANF was included in the binding assay. These results suggest that these three different polypeptides are specific components of ANF receptors in rabbit aorta membranes.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)39114-7</identifier><identifier>PMID: 2993293</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Affinity Labels - metabolism ; Animals ; Aorta - metabolism ; Atrial Natriuretic Factor ; Azides - chemical synthesis ; Azides - metabolism ; Binding, Competitive ; Biological and medical sciences ; Cell Membrane - metabolism ; Cell receptors ; Cell structures and functions ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Macromolecular Substances ; Molecular and cellular biology ; Molecular Weight ; Muscle Proteins - chemical synthesis ; Muscle Proteins - metabolism ; Rabbits ; Receptors, Atrial Natriuretic Factor ; Receptors, Cell Surface - isolation & purification ; Receptors, Cell Surface - metabolism</subject><ispartof>The Journal of biological chemistry, 1985-09, Vol.260 (20), p.10889-10892</ispartof><rights>1985 © 1985 ASBMB. 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In the first, the photoreactive analog of ANF, 125I-azidobenzoyl-ANF, was synthesized and used to photoaffinity label ANF receptors. In the second, 125I-ANF was covalently attached to its binding site by treatment of the 125I-ANF-receptor complex with bifunctional cross-linking agents. Analysis of the labeled proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography revealed that by both methods the same three protein bands were labeled. These bands had apparent molecular masses of 60,000, 70,000, and 120,000 daltons. With the photoaffinity label, half-maximal inhibition of labeling of each of these bands was achieved when approximately 200 pM of unlabeled ANF was included in the binding assay. These results suggest that these three different polypeptides are specific components of ANF receptors in rabbit aorta membranes.</description><subject>Affinity Labels - metabolism</subject><subject>Animals</subject><subject>Aorta - metabolism</subject><subject>Atrial Natriuretic Factor</subject><subject>Azides - chemical synthesis</subject><subject>Azides - metabolism</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - metabolism</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Muscle Proteins - chemical synthesis</subject><subject>Muscle Proteins - metabolism</subject><subject>Rabbits</subject><subject>Receptors, Atrial Natriuretic Factor</subject><subject>Receptors, Cell Surface - isolation & purification</subject><subject>Receptors, Cell Surface - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2LFDEQhoMo67r6ExZyENFDaz76KyeRxY-FBQ_uwVuopCs7pd3pMcko8-_tnhnGo4FQh3oq9eZh7FqKt1LI9t03IZSsjGr617J7o42UddU9YpdS9LrSjfz-mF2ekafsWc4_xHJqIy_YhTJGK6MvWbwdMBYK5KHQHPkcOPCEHrdlTjwsF0oiGHlc6y5hIc8D-LVLkSdwjgqHORXgE04uQcTM3Z5DCBSp7LlPc87VSPEnxYfn7EmAMeOLU71i958-3t98qe6-fr69-XBX-bptSlWD88phrZ0aHPimbo3sm155g8a0oI0OZjBDC3UbhNPYmWH5qmqcUdD7Tl-xV8dnt2n-tcNc7ETZ4zgu6eZdtl2rukZ0ZgGbI3hImTDYbaIJ0t5KYVfN9qDZrg6t7OxBs10XXJ8W7NyEw3nq5HXpvzz1IXsYw6LFUz5jfW06oc0_bEMPmz-U0Dqa_QYnq1ph1Rqh71fs_RHDRdlvwmSzJ4weh2XEFzvM9J-8fwGFDabg</recordid><startdate>19850915</startdate><enddate>19850915</enddate><creator>Vandlen, R L</creator><creator>Arcuri, K E</creator><creator>Napier, M A</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>19850915</creationdate><title>Identification of a receptor for atrial natriuretic factor in rabbit aorta membranes by affinity cross-linking</title><author>Vandlen, R L ; Arcuri, K E ; Napier, M A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c465t-4abc2be43b2dbac546918582c9e996a393f9d9d6a46f0b3e79d00225b92a8c73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Affinity Labels - metabolism</topic><topic>Animals</topic><topic>Aorta - metabolism</topic><topic>Atrial Natriuretic Factor</topic><topic>Azides - chemical synthesis</topic><topic>Azides - metabolism</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - metabolism</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Muscle Proteins - chemical synthesis</topic><topic>Muscle Proteins - metabolism</topic><topic>Rabbits</topic><topic>Receptors, Atrial Natriuretic Factor</topic><topic>Receptors, Cell Surface - isolation & purification</topic><topic>Receptors, Cell Surface - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vandlen, R L</creatorcontrib><creatorcontrib>Arcuri, K E</creatorcontrib><creatorcontrib>Napier, M A</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vandlen, R L</au><au>Arcuri, K E</au><au>Napier, M A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a receptor for atrial natriuretic factor in rabbit aorta membranes by affinity cross-linking</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1985-09-15</date><risdate>1985</risdate><volume>260</volume><issue>20</issue><spage>10889</spage><epage>10892</epage><pages>10889-10892</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Binding sites in rabbit aorta membranes for atrial natriuretic factor (ANF) have been specifically and covalently labeled by two methods. In the first, the photoreactive analog of ANF, 125I-azidobenzoyl-ANF, was synthesized and used to photoaffinity label ANF receptors. In the second, 125I-ANF was covalently attached to its binding site by treatment of the 125I-ANF-receptor complex with bifunctional cross-linking agents. Analysis of the labeled proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography revealed that by both methods the same three protein bands were labeled. These bands had apparent molecular masses of 60,000, 70,000, and 120,000 daltons. With the photoaffinity label, half-maximal inhibition of labeling of each of these bands was achieved when approximately 200 pM of unlabeled ANF was included in the binding assay. These results suggest that these three different polypeptides are specific components of ANF receptors in rabbit aorta membranes.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2993293</pmid><doi>10.1016/S0021-9258(17)39114-7</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Affinity Labels - metabolism Animals Aorta - metabolism Atrial Natriuretic Factor Azides - chemical synthesis Azides - metabolism Binding, Competitive Biological and medical sciences Cell Membrane - metabolism Cell receptors Cell structures and functions Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Kinetics Macromolecular Substances Molecular and cellular biology Molecular Weight Muscle Proteins - chemical synthesis Muscle Proteins - metabolism Rabbits Receptors, Atrial Natriuretic Factor Receptors, Cell Surface - isolation & purification Receptors, Cell Surface - metabolism |
title | Identification of a receptor for atrial natriuretic factor in rabbit aorta membranes by affinity cross-linking |
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