Proteolytic Activity of the Purified Hormone-Binding Subunit in the Estrogen Receptor
The hormone-binding subunit of the calf uterus estradiol receptor was purified as a hormone-free molecule. Immunoaffinity chromatography with a specific monoclonal antibody was used as the final step. The purified subunit was specifically labeled by radioactive diisopropyl fluorophosphate. The diiso...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1991-05, Vol.88 (10), p.4463-4467 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 4467 |
|---|---|
| container_issue | 10 |
| container_start_page | 4463 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 88 |
| creator | Molinari, A. M. Abbondanza, C. Armetta, I. Medici, N. Minucci, S. |
| description | The hormone-binding subunit of the calf uterus estradiol receptor was purified as a hormone-free molecule. Immunoaffinity chromatography with a specific monoclonal antibody was used as the final step. The purified subunit was specifically labeled by radioactive diisopropyl fluorophosphate. The diisopropyl fluorophosphate-labeled amino acid was serine. The purified receptor was able to release the fluorogenic or chromogenic group from synthetic peptides containing phenylalanine at the carboxyl terminus. This occurred only in the presence of estradiol and was hampered by aprotinin and diisopropyl fluorophosphate. Estradiol-dependent hydrolytic activity was also found in the eluate from gel slices after SDS/PAGE of purified receptor. This activity comigrated with the renaturable estradiol-binding activity. The estradiol antagonists 4-hydroxytamoxifen and ICI 164,384 as well as other steroid hormones were unable to activate this hydrolytic activity. |
| doi_str_mv | 10.1073/pnas.88.10.4463 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pnas_</sourceid><recordid>TN_cdi_pnas_primary_88_10_4463_fulltext</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>2357065</jstor_id><sourcerecordid>2357065</sourcerecordid><originalsourceid>FETCH-LOGICAL-c523t-5c1b895751c9ed7b58925975790bfd00e7ce8198d1c804e1dc878044b5239d483</originalsourceid><addsrcrecordid>eNqFkUFv1DAQhS0EKkvhzAVQLsAp23Fix7bEpVSFIlWiAnq2EmeydZW1F9up2H-Pwy5duMDJHr3veWb8CHlOYUlB1Ccb18allLlYMtbUD8iCgqJlwxQ8JAuASpSSVewxeRLjLQAoLuGIHFEBSrBqQa6vgk_ox22ypjg1yd7ZtC38UKQbLK6mYAeLfXHhw9o7LN9b11u3Kr5O3eRsKqz7xZ3HFPwKXfEFDW6SD0_Jo6EdIz7bn8fk-sP5t7OL8vLzx09np5el4VWdSm5oJxUXnBqFvei4VBVXggsF3dADoDAoqZI9NRIY0t5IkS-sy27VM1kfk3e7dzdTt8beoEuhHfUm2HUbttq3Vv-tOHujV_5Oc9pIyPY3e3vw3yeMSa9tNDiOrUM_RS2BNzJ_039ByvPgkvEMnuxAE3yMAYf7WSjoOTA9B6alnOs5sOx4-ecKB36XUNZf7_U2mnYcQuuMjQcsQ0JUTebe7rm5wW_50EgP0zgm_JEy-eqfZAZe7IDbmLO8J6qaC2h4_RPuJMCx</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15925845</pqid></control><display><type>article</type><title>Proteolytic Activity of the Purified Hormone-Binding Subunit in the Estrogen Receptor</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Molinari, A. M. ; Abbondanza, C. ; Armetta, I. ; Medici, N. ; Minucci, S.</creator><creatorcontrib>Molinari, A. M. ; Abbondanza, C. ; Armetta, I. ; Medici, N. ; Minucci, S.</creatorcontrib><description>The hormone-binding subunit of the calf uterus estradiol receptor was purified as a hormone-free molecule. Immunoaffinity chromatography with a specific monoclonal antibody was used as the final step. The purified subunit was specifically labeled by radioactive diisopropyl fluorophosphate. The diisopropyl fluorophosphate-labeled amino acid was serine. The purified receptor was able to release the fluorogenic or chromogenic group from synthetic peptides containing phenylalanine at the carboxyl terminus. This occurred only in the presence of estradiol and was hampered by aprotinin and diisopropyl fluorophosphate. Estradiol-dependent hydrolytic activity was also found in the eluate from gel slices after SDS/PAGE of purified receptor. This activity comigrated with the renaturable estradiol-binding activity. The estradiol antagonists 4-hydroxytamoxifen and ICI 164,384 as well as other steroid hormones were unable to activate this hydrolytic activity.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.88.10.4463</identifier><identifier>PMID: 1709742</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Active sites ; affinity chromatography ; Amino Acid Sequence ; Amino acids ; Animals ; Antibodies ; Aprotinin - pharmacology ; Biochemistry ; Biological and medical sciences ; Cattle ; Cell receptors ; Cell structures and functions ; Chromatography ; Chromogenic Compounds - metabolism ; Electrophoresis, Polyacrylamide Gel ; Endopeptidases - metabolism ; Estradiol - analogs & derivatives ; Estradiol - metabolism ; Estradiol - pharmacology ; Estrogen Antagonists - pharmacology ; Female ; Fundamental and applied biological sciences. Psychology ; Gels ; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors ; Hormones ; Hydrolysis ; Isoflurophate - metabolism ; Isoflurophate - pharmacology ; Molecular and cellular biology ; Molecular Sequence Data ; Polyunsaturated Alkamides ; Proteins ; Receptors ; Receptors, Estrogen - isolation & purification ; Receptors, Estrogen - metabolism ; Sodium ; Tamoxifen - analogs & derivatives ; Tamoxifen - pharmacology ; uterus ; Uterus - chemistry</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1991-05, Vol.88 (10), p.4463-4467</ispartof><rights>Copyright 1991 The National Academy of Sciences of the United States of America</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-5c1b895751c9ed7b58925975790bfd00e7ce8198d1c804e1dc878044b5239d483</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/88/10.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2357065$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2357065$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,729,782,786,805,887,27931,27932,53798,53800,58024,58257</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19747726$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1709742$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Molinari, A. M.</creatorcontrib><creatorcontrib>Abbondanza, C.</creatorcontrib><creatorcontrib>Armetta, I.</creatorcontrib><creatorcontrib>Medici, N.</creatorcontrib><creatorcontrib>Minucci, S.</creatorcontrib><title>Proteolytic Activity of the Purified Hormone-Binding Subunit in the Estrogen Receptor</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The hormone-binding subunit of the calf uterus estradiol receptor was purified as a hormone-free molecule. Immunoaffinity chromatography with a specific monoclonal antibody was used as the final step. The purified subunit was specifically labeled by radioactive diisopropyl fluorophosphate. The diisopropyl fluorophosphate-labeled amino acid was serine. The purified receptor was able to release the fluorogenic or chromogenic group from synthetic peptides containing phenylalanine at the carboxyl terminus. This occurred only in the presence of estradiol and was hampered by aprotinin and diisopropyl fluorophosphate. Estradiol-dependent hydrolytic activity was also found in the eluate from gel slices after SDS/PAGE of purified receptor. This activity comigrated with the renaturable estradiol-binding activity. The estradiol antagonists 4-hydroxytamoxifen and ICI 164,384 as well as other steroid hormones were unable to activate this hydrolytic activity.</description><subject>Active sites</subject><subject>affinity chromatography</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Aprotinin - pharmacology</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Chromatography</subject><subject>Chromogenic Compounds - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endopeptidases - metabolism</subject><subject>Estradiol - analogs & derivatives</subject><subject>Estradiol - metabolism</subject><subject>Estradiol - pharmacology</subject><subject>Estrogen Antagonists - pharmacology</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</subject><subject>Hormones</subject><subject>Hydrolysis</subject><subject>Isoflurophate - metabolism</subject><subject>Isoflurophate - pharmacology</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Polyunsaturated Alkamides</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Receptors, Estrogen - isolation & purification</subject><subject>Receptors, Estrogen - metabolism</subject><subject>Sodium</subject><subject>Tamoxifen - analogs & derivatives</subject><subject>Tamoxifen - pharmacology</subject><subject>uterus</subject><subject>Uterus - chemistry</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhS0EKkvhzAVQLsAp23Fix7bEpVSFIlWiAnq2EmeydZW1F9up2H-Pwy5duMDJHr3veWb8CHlOYUlB1Ccb18allLlYMtbUD8iCgqJlwxQ8JAuASpSSVewxeRLjLQAoLuGIHFEBSrBqQa6vgk_ox22ypjg1yd7ZtC38UKQbLK6mYAeLfXHhw9o7LN9b11u3Kr5O3eRsKqz7xZ3HFPwKXfEFDW6SD0_Jo6EdIz7bn8fk-sP5t7OL8vLzx09np5el4VWdSm5oJxUXnBqFvei4VBVXggsF3dADoDAoqZI9NRIY0t5IkS-sy27VM1kfk3e7dzdTt8beoEuhHfUm2HUbttq3Vv-tOHujV_5Oc9pIyPY3e3vw3yeMSa9tNDiOrUM_RS2BNzJ_039ByvPgkvEMnuxAE3yMAYf7WSjoOTA9B6alnOs5sOx4-ecKB36XUNZf7_U2mnYcQuuMjQcsQ0JUTebe7rm5wW_50EgP0zgm_JEy-eqfZAZe7IDbmLO8J6qaC2h4_RPuJMCx</recordid><startdate>19910515</startdate><enddate>19910515</enddate><creator>Molinari, A. M.</creator><creator>Abbondanza, C.</creator><creator>Armetta, I.</creator><creator>Medici, N.</creator><creator>Minucci, S.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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><scope>5PM</scope></search><sort><creationdate>19910515</creationdate><title>Proteolytic Activity of the Purified Hormone-Binding Subunit in the Estrogen Receptor</title><author>Molinari, A. M. ; Abbondanza, C. ; Armetta, I. ; Medici, N. ; Minucci, S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-5c1b895751c9ed7b58925975790bfd00e7ce8198d1c804e1dc878044b5239d483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Active sites</topic><topic>affinity chromatography</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Aprotinin - pharmacology</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Chromatography</topic><topic>Chromogenic Compounds - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endopeptidases - metabolism</topic><topic>Estradiol - analogs & derivatives</topic><topic>Estradiol - metabolism</topic><topic>Estradiol - pharmacology</topic><topic>Estrogen Antagonists - pharmacology</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</topic><topic>Hormones</topic><topic>Hydrolysis</topic><topic>Isoflurophate - metabolism</topic><topic>Isoflurophate - pharmacology</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Polyunsaturated Alkamides</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Receptors, Estrogen - isolation & purification</topic><topic>Receptors, Estrogen - metabolism</topic><topic>Sodium</topic><topic>Tamoxifen - analogs & derivatives</topic><topic>Tamoxifen - pharmacology</topic><topic>uterus</topic><topic>Uterus - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Molinari, A. M.</creatorcontrib><creatorcontrib>Abbondanza, C.</creatorcontrib><creatorcontrib>Armetta, I.</creatorcontrib><creatorcontrib>Medici, N.</creatorcontrib><creatorcontrib>Minucci, S.</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Molinari, A. M.</au><au>Abbondanza, C.</au><au>Armetta, I.</au><au>Medici, N.</au><au>Minucci, S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteolytic Activity of the Purified Hormone-Binding Subunit in the Estrogen Receptor</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1991-05-15</date><risdate>1991</risdate><volume>88</volume><issue>10</issue><spage>4463</spage><epage>4467</epage><pages>4463-4467</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>The hormone-binding subunit of the calf uterus estradiol receptor was purified as a hormone-free molecule. Immunoaffinity chromatography with a specific monoclonal antibody was used as the final step. The purified subunit was specifically labeled by radioactive diisopropyl fluorophosphate. The diisopropyl fluorophosphate-labeled amino acid was serine. The purified receptor was able to release the fluorogenic or chromogenic group from synthetic peptides containing phenylalanine at the carboxyl terminus. This occurred only in the presence of estradiol and was hampered by aprotinin and diisopropyl fluorophosphate. Estradiol-dependent hydrolytic activity was also found in the eluate from gel slices after SDS/PAGE of purified receptor. This activity comigrated with the renaturable estradiol-binding activity. The estradiol antagonists 4-hydroxytamoxifen and ICI 164,384 as well as other steroid hormones were unable to activate this hydrolytic activity.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1709742</pmid><doi>10.1073/pnas.88.10.4463</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1991-05, Vol.88 (10), p.4463-4467 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_88_10_4463_fulltext |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Active sites affinity chromatography Amino Acid Sequence Amino acids Animals Antibodies Aprotinin - pharmacology Biochemistry Biological and medical sciences Cattle Cell receptors Cell structures and functions Chromatography Chromogenic Compounds - metabolism Electrophoresis, Polyacrylamide Gel Endopeptidases - metabolism Estradiol - analogs & derivatives Estradiol - metabolism Estradiol - pharmacology Estrogen Antagonists - pharmacology Female Fundamental and applied biological sciences. Psychology Gels Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors Hormones Hydrolysis Isoflurophate - metabolism Isoflurophate - pharmacology Molecular and cellular biology Molecular Sequence Data Polyunsaturated Alkamides Proteins Receptors Receptors, Estrogen - isolation & purification Receptors, Estrogen - metabolism Sodium Tamoxifen - analogs & derivatives Tamoxifen - pharmacology uterus Uterus - chemistry |
| title | Proteolytic Activity of the Purified Hormone-Binding Subunit in the Estrogen Receptor |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-04T03%3A55%3A42IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pnas_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Proteolytic%20Activity%20of%20the%20Purified%20Hormone-Binding%20Subunit%20in%20the%20Estrogen%20Receptor&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Molinari,%20A.%20M.&rft.date=1991-05-15&rft.volume=88&rft.issue=10&rft.spage=4463&rft.epage=4467&rft.pages=4463-4467&rft.issn=0027-8424&rft.eissn=1091-6490&rft.coden=PNASA6&rft_id=info:doi/10.1073/pnas.88.10.4463&rft_dat=%3Cjstor_pnas_%3E2357065%3C/jstor_pnas_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15925845&rft_id=info:pmid/1709742&rft_jstor_id=2357065&rfr_iscdi=true |