Immunological and structural characterization of sarafotoxin/endothelin family of peptides
A highly specific and sensitive radioimmunoassay (RIA) was developed for the potent vasoconstrictor peptides, sarafotoxin-b and human endothelin. The antigenic determinants of the antibodies employed in studies with these assays were found to be localized within the amino acid sequence at positions...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 1989-08, Vol.162 (3), p.1317-1323 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1323 |
|---|---|
| container_issue | 3 |
| container_start_page | 1317 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 162 |
| creator | Fleminger, Gideon Bousso-Mittler, Daniele Bdolah, Avner Kloog, Yoel Sokolovsky, Mordechai |
| description | A highly specific and sensitive radioimmunoassay (RIA) was developed for the potent vasoconstrictor peptides, sarafotoxin-b and human endothelin. The antigenic determinants of the antibodies employed in studies with these assays were found to be localized within the amino acid sequence at positions 4–7. This was confirmed by CNBr cleavage of the methionyl residue at position 6 in the sarafotoxin and at position 7 in the endothelin. The chemically characterized modified peptides showed very low cross reactivity in the RIAs. On the other hand, the binding properties as well as the ability to induce phosphoinositide hydrolysis were very similar in the modified and native peptides, indicating that despite cleavage of the peptide bond the biologically active conformation responsible for either binding or phoshoinositide hydrolysis is retained, probably because of the disulfide bonds. Thus, structural alteration might be a valuable means of curtailing some of the various activities induced by the sarafotoxin/endothelin family of peptides. |
| doi_str_mv | 10.1016/0006-291X(89)90817-6 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79165130</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006291X89908176</els_id><sourcerecordid>15316588</sourcerecordid><originalsourceid>FETCH-LOGICAL-c417t-c55b0200ac6c778750cd11c43058a4becba4feaf9d558ef7188030e50c5b6fa63</originalsourceid><addsrcrecordid>eNqFkEtv1DAQgC1EVZbCPwApB4TgkHZmEz9yqYQqHpUqcQEJcbEcZ0yNknixHUT59XXY1R7paTQz3zz0MfYC4RwBxQUAiHrb4bc3qnvbgUJZi0dsg9BBvUVoH7PNEXnCnqb0EwCxFd0pO922kiOoDft-PU3LHMbww1szVmYeqpTjYvMSS2pvTTQ2U_R_TfZhroKrUim5kMMfP1_QPIR8S6OfK2cmP96twI522Q-UnrETZ8ZEzw_xjH398P7L1af65vPH66t3N7VtUebact7DFsBYYaVUkoMdEG3bAFem7cn2pnVkXDdwrshJVAoaoILxXjgjmjP2er93F8OvhVLWk0-WxtHMFJakZYeCYwMPgsibQipVwHYP2hhSiuT0LvrJxDuNoFf3ehWrV7Fadfqfe70-8vKwf-knGo5DB9ml_-rQN6nIdtHM1qcjVk6DErJgl3uMirTfnqJO1tNsafCRbNZD8P__4x46z6Hp</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15316588</pqid></control><display><type>article</type><title>Immunological and structural characterization of sarafotoxin/endothelin family of peptides</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Fleminger, Gideon ; Bousso-Mittler, Daniele ; Bdolah, Avner ; Kloog, Yoel ; Sokolovsky, Mordechai</creator><creatorcontrib>Fleminger, Gideon ; Bousso-Mittler, Daniele ; Bdolah, Avner ; Kloog, Yoel ; Sokolovsky, Mordechai</creatorcontrib><description>A highly specific and sensitive radioimmunoassay (RIA) was developed for the potent vasoconstrictor peptides, sarafotoxin-b and human endothelin. The antigenic determinants of the antibodies employed in studies with these assays were found to be localized within the amino acid sequence at positions 4–7. This was confirmed by CNBr cleavage of the methionyl residue at position 6 in the sarafotoxin and at position 7 in the endothelin. The chemically characterized modified peptides showed very low cross reactivity in the RIAs. On the other hand, the binding properties as well as the ability to induce phosphoinositide hydrolysis were very similar in the modified and native peptides, indicating that despite cleavage of the peptide bond the biologically active conformation responsible for either binding or phoshoinositide hydrolysis is retained, probably because of the disulfide bonds. Thus, structural alteration might be a valuable means of curtailing some of the various activities induced by the sarafotoxin/endothelin family of peptides.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(89)90817-6</identifier><identifier>PMID: 2475108</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Aminoacids, peptides. Hormones. Neuropeptides ; Analytical, structural and metabolic biochemistry ; Animals ; Binding, Competitive ; Biological and medical sciences ; Chromatography, High Pressure Liquid ; Cyanogen Bromide ; endothelin ; Endothelins ; Epitopes ; Fundamental and applied biological sciences. Psychology ; Peptide Fragments - immunology ; Peptides - immunology ; Protein Conformation ; Proteins ; Rabbits ; Radioimmunoassay ; Viper Venoms - immunology</subject><ispartof>Biochemical and biophysical research communications, 1989-08, Vol.162 (3), p.1317-1323</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-c55b0200ac6c778750cd11c43058a4becba4feaf9d558ef7188030e50c5b6fa63</citedby><cites>FETCH-LOGICAL-c417t-c55b0200ac6c778750cd11c43058a4becba4feaf9d558ef7188030e50c5b6fa63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X89908176$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6580867$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2475108$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fleminger, Gideon</creatorcontrib><creatorcontrib>Bousso-Mittler, Daniele</creatorcontrib><creatorcontrib>Bdolah, Avner</creatorcontrib><creatorcontrib>Kloog, Yoel</creatorcontrib><creatorcontrib>Sokolovsky, Mordechai</creatorcontrib><title>Immunological and structural characterization of sarafotoxin/endothelin family of peptides</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>A highly specific and sensitive radioimmunoassay (RIA) was developed for the potent vasoconstrictor peptides, sarafotoxin-b and human endothelin. The antigenic determinants of the antibodies employed in studies with these assays were found to be localized within the amino acid sequence at positions 4–7. This was confirmed by CNBr cleavage of the methionyl residue at position 6 in the sarafotoxin and at position 7 in the endothelin. The chemically characterized modified peptides showed very low cross reactivity in the RIAs. On the other hand, the binding properties as well as the ability to induce phosphoinositide hydrolysis were very similar in the modified and native peptides, indicating that despite cleavage of the peptide bond the biologically active conformation responsible for either binding or phoshoinositide hydrolysis is retained, probably because of the disulfide bonds. Thus, structural alteration might be a valuable means of curtailing some of the various activities induced by the sarafotoxin/endothelin family of peptides.</description><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cyanogen Bromide</subject><subject>endothelin</subject><subject>Endothelins</subject><subject>Epitopes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Peptide Fragments - immunology</subject><subject>Peptides - immunology</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Radioimmunoassay</subject><subject>Viper Venoms - immunology</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>eNqFkEtv1DAQgC1EVZbCPwApB4TgkHZmEz9yqYQqHpUqcQEJcbEcZ0yNknixHUT59XXY1R7paTQz3zz0MfYC4RwBxQUAiHrb4bc3qnvbgUJZi0dsg9BBvUVoH7PNEXnCnqb0EwCxFd0pO922kiOoDft-PU3LHMbww1szVmYeqpTjYvMSS2pvTTQ2U_R_TfZhroKrUim5kMMfP1_QPIR8S6OfK2cmP96twI522Q-UnrETZ8ZEzw_xjH398P7L1af65vPH66t3N7VtUebact7DFsBYYaVUkoMdEG3bAFem7cn2pnVkXDdwrshJVAoaoILxXjgjmjP2er93F8OvhVLWk0-WxtHMFJakZYeCYwMPgsibQipVwHYP2hhSiuT0LvrJxDuNoFf3ehWrV7Fadfqfe70-8vKwf-knGo5DB9ml_-rQN6nIdtHM1qcjVk6DErJgl3uMirTfnqJO1tNsafCRbNZD8P__4x46z6Hp</recordid><startdate>19890815</startdate><enddate>19890815</enddate><creator>Fleminger, Gideon</creator><creator>Bousso-Mittler, Daniele</creator><creator>Bdolah, Avner</creator><creator>Kloog, Yoel</creator><creator>Sokolovsky, Mordechai</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890815</creationdate><title>Immunological and structural characterization of sarafotoxin/endothelin family of peptides</title><author>Fleminger, Gideon ; Bousso-Mittler, Daniele ; Bdolah, Avner ; Kloog, Yoel ; Sokolovsky, Mordechai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-c55b0200ac6c778750cd11c43058a4becba4feaf9d558ef7188030e50c5b6fa63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cyanogen Bromide</topic><topic>endothelin</topic><topic>Endothelins</topic><topic>Epitopes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Peptide Fragments - immunology</topic><topic>Peptides - immunology</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Radioimmunoassay</topic><topic>Viper Venoms - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fleminger, Gideon</creatorcontrib><creatorcontrib>Bousso-Mittler, Daniele</creatorcontrib><creatorcontrib>Bdolah, Avner</creatorcontrib><creatorcontrib>Kloog, Yoel</creatorcontrib><creatorcontrib>Sokolovsky, Mordechai</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</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>Fleminger, Gideon</au><au>Bousso-Mittler, Daniele</au><au>Bdolah, Avner</au><au>Kloog, Yoel</au><au>Sokolovsky, Mordechai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Immunological and structural characterization of sarafotoxin/endothelin family of peptides</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1989-08-15</date><risdate>1989</risdate><volume>162</volume><issue>3</issue><spage>1317</spage><epage>1323</epage><pages>1317-1323</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>A highly specific and sensitive radioimmunoassay (RIA) was developed for the potent vasoconstrictor peptides, sarafotoxin-b and human endothelin. The antigenic determinants of the antibodies employed in studies with these assays were found to be localized within the amino acid sequence at positions 4–7. This was confirmed by CNBr cleavage of the methionyl residue at position 6 in the sarafotoxin and at position 7 in the endothelin. The chemically characterized modified peptides showed very low cross reactivity in the RIAs. On the other hand, the binding properties as well as the ability to induce phosphoinositide hydrolysis were very similar in the modified and native peptides, indicating that despite cleavage of the peptide bond the biologically active conformation responsible for either binding or phoshoinositide hydrolysis is retained, probably because of the disulfide bonds. Thus, structural alteration might be a valuable means of curtailing some of the various activities induced by the sarafotoxin/endothelin family of peptides.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2475108</pmid><doi>10.1016/0006-291X(89)90817-6</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1989-08, Vol.162 (3), p.1317-1323 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79165130 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals Binding, Competitive Biological and medical sciences Chromatography, High Pressure Liquid Cyanogen Bromide endothelin Endothelins Epitopes Fundamental and applied biological sciences. Psychology Peptide Fragments - immunology Peptides - immunology Protein Conformation Proteins Rabbits Radioimmunoassay Viper Venoms - immunology |
| title | Immunological and structural characterization of sarafotoxin/endothelin family of peptides |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-14T06%3A44%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Immunological%20and%20structural%20characterization%20of%20sarafotoxin/endothelin%20family%20of%20peptides&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Fleminger,%20Gideon&rft.date=1989-08-15&rft.volume=162&rft.issue=3&rft.spage=1317&rft.epage=1323&rft.pages=1317-1323&rft.issn=0006-291X&rft.eissn=1090-2104&rft.coden=BBRCA9&rft_id=info:doi/10.1016/0006-291X(89)90817-6&rft_dat=%3Cproquest_cross%3E15316588%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15316588&rft_id=info:pmid/2475108&rft_els_id=0006291X89908176&rfr_iscdi=true |