Solubilization and identification of human placental endothelin receptor
Endothelin-1 (ET-1) receptor was identified on the membranes from human placenta and 66% of original binding activity in the membranes was solubilized with 0.75% ( w v ) CHAPS. Binding studies of the solubilized membranes using 125I-ET-1 indicated the presence of a single class of high-affinity bind...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1989-10, Vol.164 (1), p.205-211 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Nakajo, Shigeo Sugiura, Masanori Snajdar, Rudolf M. Boehm, Frank H. Inagami, Tadashi |
| description | Endothelin-1 (ET-1) receptor was identified on the membranes from human placenta and 66% of original binding activity in the membranes was solubilized with 0.75% (
w
v
) CHAPS. Binding studies of the solubilized membranes using
125I-ET-1 indicated the presence of a single class of high-affinity binding sites with an apparent Kd of 760 pM and a Bmax of 1.8 pmol/mg of protein. The binding was inhibited by addition of unlabeled ET-1 and ET-3 in dose dependent manner. The Ki values of solubilized membranes were 84 pM for ET-1 and 250 pM for ET-3, whereas particulate membranes had weaker affinities (Ki=410 pM for ET-1, 2500 pM for ET-3). Calcium channel blockers such as nicardipine, verapamil and diltiazem did not affect the binding of
125I-ET-1. Affinity labeling of the particulate and solubilized membranes with CHAPS revealed a specific binding protein with a Mr of 32,000. |
| doi_str_mv | 10.1016/0006-291X(89)91703-8 |
| format | Article |
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w
v
) CHAPS. Binding studies of the solubilized membranes using
125I-ET-1 indicated the presence of a single class of high-affinity binding sites with an apparent Kd of 760 pM and a Bmax of 1.8 pmol/mg of protein. The binding was inhibited by addition of unlabeled ET-1 and ET-3 in dose dependent manner. The Ki values of solubilized membranes were 84 pM for ET-1 and 250 pM for ET-3, whereas particulate membranes had weaker affinities (Ki=410 pM for ET-1, 2500 pM for ET-3). Calcium channel blockers such as nicardipine, verapamil and diltiazem did not affect the binding of
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w
v
) CHAPS. Binding studies of the solubilized membranes using
125I-ET-1 indicated the presence of a single class of high-affinity binding sites with an apparent Kd of 760 pM and a Bmax of 1.8 pmol/mg of protein. The binding was inhibited by addition of unlabeled ET-1 and ET-3 in dose dependent manner. The Ki values of solubilized membranes were 84 pM for ET-1 and 250 pM for ET-3, whereas particulate membranes had weaker affinities (Ki=410 pM for ET-1, 2500 pM for ET-3). Calcium channel blockers such as nicardipine, verapamil and diltiazem did not affect the binding of
125I-ET-1. Affinity labeling of the particulate and solubilized membranes with CHAPS revealed a specific binding protein with a Mr of 32,000.</description><subject>Autoradiography</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Calcium Channel Blockers - pharmacology</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cross-Linking Reagents</subject><subject>Detergents</subject><subject>Endothelins</subject><subject>Endothelium, Vascular - metabolism</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>man</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>Peptides - metabolism</subject><subject>placenta</subject><subject>Placenta - metabolism</subject><subject>Pregnancy</subject><subject>Receptors, Cell Surface - isolation & purification</subject><subject>Receptors, Endothelin</subject><subject>Solubility</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFqFTEUhoMo9bb6BgqzUXQx9ZxJZpJsBCnWCgUXVXAXMskZGslNrsmMUJ_eud5L3dlVDvm_83P4GHuBcI6AwzsAGNpO4_c3Sr_VKIG36hHbIGhoOwTxmG3ukafstNYfAIhi0CfspOt7Dsg37Oomx2UMMfy2c8ipsck3wVOawxTc4StPze2ytanZRevWxMaGks_zLcWQmkKOdnMuz9iTycZKz4_vGft2-fHrxVV7_eXT54sP160TqOZWCe4kkITRefAT92LUCjgApwnlQHyE9XQFvkewIyi_jlJ2Xndcg7aOn7HXh95dyT8XqrPZhuooRpsoL9VI3UlEiQ-C2AuQQsgVFAfQlVxrocnsStjacmcQzN602Ws0e41GafPXtFHr2stj_zJuyd8vHdWu-atjbquzcSo2uVD_dWvR62HY97w_cLRa-xWomOoCJUc-rG5n43P4_yF_AJcYmcg</recordid><startdate>19891016</startdate><enddate>19891016</enddate><creator>Nakajo, Shigeo</creator><creator>Sugiura, Masanori</creator><creator>Snajdar, Rudolf M.</creator><creator>Boehm, Frank H.</creator><creator>Inagami, Tadashi</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19891016</creationdate><title>Solubilization and identification of human placental endothelin receptor</title><author>Nakajo, Shigeo ; Sugiura, Masanori ; Snajdar, Rudolf M. ; Boehm, Frank H. ; Inagami, Tadashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-843c70e70bcd0df3d4b9803003ef176e3b010480d510ab08d80d772d923909ac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Autoradiography</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Calcium Channel Blockers - pharmacology</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cross-Linking Reagents</topic><topic>Detergents</topic><topic>Endothelins</topic><topic>Endothelium, Vascular - metabolism</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>man</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>Peptides - metabolism</topic><topic>placenta</topic><topic>Placenta - metabolism</topic><topic>Pregnancy</topic><topic>Receptors, Cell Surface - isolation & purification</topic><topic>Receptors, Endothelin</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakajo, Shigeo</creatorcontrib><creatorcontrib>Sugiura, Masanori</creatorcontrib><creatorcontrib>Snajdar, Rudolf M.</creatorcontrib><creatorcontrib>Boehm, Frank H.</creatorcontrib><creatorcontrib>Inagami, Tadashi</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</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>Nakajo, Shigeo</au><au>Sugiura, Masanori</au><au>Snajdar, Rudolf M.</au><au>Boehm, Frank H.</au><au>Inagami, Tadashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solubilization and identification of human placental endothelin receptor</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1989-10-16</date><risdate>1989</risdate><volume>164</volume><issue>1</issue><spage>205</spage><epage>211</epage><pages>205-211</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Endothelin-1 (ET-1) receptor was identified on the membranes from human placenta and 66% of original binding activity in the membranes was solubilized with 0.75% (
w
v
) CHAPS. Binding studies of the solubilized membranes using
125I-ET-1 indicated the presence of a single class of high-affinity binding sites with an apparent Kd of 760 pM and a Bmax of 1.8 pmol/mg of protein. The binding was inhibited by addition of unlabeled ET-1 and ET-3 in dose dependent manner. The Ki values of solubilized membranes were 84 pM for ET-1 and 250 pM for ET-3, whereas particulate membranes had weaker affinities (Ki=410 pM for ET-1, 2500 pM for ET-3). Calcium channel blockers such as nicardipine, verapamil and diltiazem did not affect the binding of
125I-ET-1. Affinity labeling of the particulate and solubilized membranes with CHAPS revealed a specific binding protein with a Mr of 32,000.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2553013</pmid><doi>10.1016/0006-291X(89)91703-8</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1989-10, Vol.164 (1), p.205-211 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Autoradiography Binding, Competitive Biological and medical sciences Calcium Channel Blockers - pharmacology Cell receptors Cell structures and functions Cross-Linking Reagents Detergents Endothelins Endothelium, Vascular - metabolism Female Fundamental and applied biological sciences. Psychology Humans man Miscellaneous Molecular and cellular biology Peptides - metabolism placenta Placenta - metabolism Pregnancy Receptors, Cell Surface - isolation & purification Receptors, Endothelin Solubility |
| title | Solubilization and identification of human placental endothelin receptor |
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