Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport
X-ray and neutron diffraction studies of oriented multilayers of a highly purified fraction of isolated sarcoplasmic reticulum (SR) have previously provided the separate profile structures of the lipid bilayer and the Ca2+-ATPase molecule within the membrane profile to approximately 10-A resolution....
Gespeichert in:
| Veröffentlicht in: | Biophysical journal 1985-07, Vol.48 (1), p.9-18 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 18 |
|---|---|
| container_issue | 1 |
| container_start_page | 9 |
| container_title | Biophysical journal |
| container_volume | 48 |
| creator | Blasie, J.K. Herbette, L.G. Pascolini, D. Skita, V. Pierce, D.H. Scarpa, A. |
| description | X-ray and neutron diffraction studies of oriented multilayers of a highly purified fraction of isolated sarcoplasmic reticulum (SR) have previously provided the separate profile structures of the lipid bilayer and the Ca2+-ATPase molecule within the membrane profile to approximately 10-A resolution. These studies used biosynthetically deuterated SR phospholipids incorporated isomorphously into the isolated SR membranes via phospholipid transfer proteins. Time-resolved x-ray diffraction studies of these oriented SR membrane multilayers have detected significant changes in the membrane profile structure associated with phosphorylation of the Ca2+-ATPase within a single turnover of the Ca2+-transport cycle. These studies used the flash photolysis of caged ATP to effectively synchronize the ensemble of Ca2+-ATPase molecules in the multilayer, synchrotron x-radiation to provide 100–500-ms data collection times, and double-beam spectrophotometry to monitor the Ca2+-transport process directly in the oriented SR membrane multilayer. |
| doi_str_mv | 10.1016/S0006-3495(85)83756-5 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1329373</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349585837565</els_id><sourcerecordid>14395906</sourcerecordid><originalsourceid>FETCH-LOGICAL-c522t-a931ff11110a3be3a1cb683519c841d93d23d3c27fcc556b14187a1b7ad7759a3</originalsourceid><addsrcrecordid>eNqFkU9r3DAQxUVpSLdpP0JAh1LagxuNZcnSpaGE_oNADknPQpbGiYptbSV7ab595e6ytKcIgUDzm6c3eoScA_sADOTFLWNMVrzR4p0S7xVvhazEM7IB0dQVY0o-J5sj8oK8zPknY1ALBqfklINkXDcb0t-FEauEOQ479PR3lewj9aHvk3VziBPN8-IDZhp7Oj8gzTa5uB1sHoOjCefglmEZ6Yhjl-yE1C8pTPd0bd4hnctd3sY0vyInvR0yvj6cZ-THl893V9-q65uv368-XVdO1PVcWc2h76EsZnmH3ILrpOICtFMNeM19zT13dds7J4TsoAHVWuha69tWaMvPyMe97nbpRvQOp2JhMNsURpseTbTB_F-ZwoO5jzsDvNa85UXg7UEgxV8L5tmMITschjJcXLJpJWhdM_EkCA3XQjNZQLEHXYo5J-yPboCZNUnzN0mzxmRU2WuSZn3g_N9Rjl2H6Er9zaFus7NDCWxyIR8xJRpVhirY5R7D8u27gMlkF3By6ENCNxsfwxNG_gDB7r0t</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14395906</pqid></control><display><type>article</type><title>Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>Cell Press Free Archives</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Blasie, J.K. ; Herbette, L.G. ; Pascolini, D. ; Skita, V. ; Pierce, D.H. ; Scarpa, A.</creator><creatorcontrib>Blasie, J.K. ; Herbette, L.G. ; Pascolini, D. ; Skita, V. ; Pierce, D.H. ; Scarpa, A.</creatorcontrib><description>X-ray and neutron diffraction studies of oriented multilayers of a highly purified fraction of isolated sarcoplasmic reticulum (SR) have previously provided the separate profile structures of the lipid bilayer and the Ca2+-ATPase molecule within the membrane profile to approximately 10-A resolution. These studies used biosynthetically deuterated SR phospholipids incorporated isomorphously into the isolated SR membranes via phospholipid transfer proteins. Time-resolved x-ray diffraction studies of these oriented SR membrane multilayers have detected significant changes in the membrane profile structure associated with phosphorylation of the Ca2+-ATPase within a single turnover of the Ca2+-transport cycle. These studies used the flash photolysis of caged ATP to effectively synchronize the ensemble of Ca2+-ATPase molecules in the multilayer, synchrotron x-radiation to provide 100–500-ms data collection times, and double-beam spectrophotometry to monitor the Ca2+-transport process directly in the oriented SR membrane multilayer.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(85)83756-5</identifier><identifier>PMID: 3160394</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; ATP ; Biological and medical sciences ; Biological Transport, Active ; calcium ; Calcium-Transporting ATPases - metabolism ; Cell physiology ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Membrane and intracellular transports ; Molecular and cellular biology ; Muscles - metabolism ; Neutrons ; Rabbits ; sarcoplasmic reticulum ; Sarcoplasmic Reticulum - metabolism ; Spectrum Analysis ; Time Factors ; X-ray diffraction ; X-Ray Diffraction - methods</subject><ispartof>Biophysical journal, 1985-07, Vol.48 (1), p.9-18</ispartof><rights>1985 The Biophysical Society</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-a931ff11110a3be3a1cb683519c841d93d23d3c27fcc556b14187a1b7ad7759a3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1329373/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006349585837565$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,3537,27901,27902,53766,53768,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8548132$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3160394$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blasie, J.K.</creatorcontrib><creatorcontrib>Herbette, L.G.</creatorcontrib><creatorcontrib>Pascolini, D.</creatorcontrib><creatorcontrib>Skita, V.</creatorcontrib><creatorcontrib>Pierce, D.H.</creatorcontrib><creatorcontrib>Scarpa, A.</creatorcontrib><title>Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>X-ray and neutron diffraction studies of oriented multilayers of a highly purified fraction of isolated sarcoplasmic reticulum (SR) have previously provided the separate profile structures of the lipid bilayer and the Ca2+-ATPase molecule within the membrane profile to approximately 10-A resolution. These studies used biosynthetically deuterated SR phospholipids incorporated isomorphously into the isolated SR membranes via phospholipid transfer proteins. Time-resolved x-ray diffraction studies of these oriented SR membrane multilayers have detected significant changes in the membrane profile structure associated with phosphorylation of the Ca2+-ATPase within a single turnover of the Ca2+-transport cycle. These studies used the flash photolysis of caged ATP to effectively synchronize the ensemble of Ca2+-ATPase molecules in the multilayer, synchrotron x-radiation to provide 100–500-ms data collection times, and double-beam spectrophotometry to monitor the Ca2+-transport process directly in the oriented SR membrane multilayer.</description><subject>Animals</subject><subject>ATP</subject><subject>Biological and medical sciences</subject><subject>Biological Transport, Active</subject><subject>calcium</subject><subject>Calcium-Transporting ATPases - metabolism</subject><subject>Cell physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Membrane and intracellular transports</subject><subject>Molecular and cellular biology</subject><subject>Muscles - metabolism</subject><subject>Neutrons</subject><subject>Rabbits</subject><subject>sarcoplasmic reticulum</subject><subject>Sarcoplasmic Reticulum - metabolism</subject><subject>Spectrum Analysis</subject><subject>Time Factors</subject><subject>X-ray diffraction</subject><subject>X-Ray Diffraction - methods</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9r3DAQxUVpSLdpP0JAh1LagxuNZcnSpaGE_oNADknPQpbGiYptbSV7ab595e6ytKcIgUDzm6c3eoScA_sADOTFLWNMVrzR4p0S7xVvhazEM7IB0dQVY0o-J5sj8oK8zPknY1ALBqfklINkXDcb0t-FEauEOQ479PR3lewj9aHvk3VziBPN8-IDZhp7Oj8gzTa5uB1sHoOjCefglmEZ6Yhjl-yE1C8pTPd0bd4hnctd3sY0vyInvR0yvj6cZ-THl893V9-q65uv368-XVdO1PVcWc2h76EsZnmH3ILrpOICtFMNeM19zT13dds7J4TsoAHVWuha69tWaMvPyMe97nbpRvQOp2JhMNsURpseTbTB_F-ZwoO5jzsDvNa85UXg7UEgxV8L5tmMITschjJcXLJpJWhdM_EkCA3XQjNZQLEHXYo5J-yPboCZNUnzN0mzxmRU2WuSZn3g_N9Rjl2H6Er9zaFus7NDCWxyIR8xJRpVhirY5R7D8u27gMlkF3By6ENCNxsfwxNG_gDB7r0t</recordid><startdate>19850701</startdate><enddate>19850701</enddate><creator>Blasie, J.K.</creator><creator>Herbette, L.G.</creator><creator>Pascolini, D.</creator><creator>Skita, V.</creator><creator>Pierce, D.H.</creator><creator>Scarpa, A.</creator><general>Elsevier Inc</general><general>Biophysical Society</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19850701</creationdate><title>Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport</title><author>Blasie, J.K. ; Herbette, L.G. ; Pascolini, D. ; Skita, V. ; Pierce, D.H. ; Scarpa, A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-a931ff11110a3be3a1cb683519c841d93d23d3c27fcc556b14187a1b7ad7759a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Animals</topic><topic>ATP</topic><topic>Biological and medical sciences</topic><topic>Biological Transport, Active</topic><topic>calcium</topic><topic>Calcium-Transporting ATPases - metabolism</topic><topic>Cell physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Membrane and intracellular transports</topic><topic>Molecular and cellular biology</topic><topic>Muscles - metabolism</topic><topic>Neutrons</topic><topic>Rabbits</topic><topic>sarcoplasmic reticulum</topic><topic>Sarcoplasmic Reticulum - metabolism</topic><topic>Spectrum Analysis</topic><topic>Time Factors</topic><topic>X-ray diffraction</topic><topic>X-Ray Diffraction - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blasie, J.K.</creatorcontrib><creatorcontrib>Herbette, L.G.</creatorcontrib><creatorcontrib>Pascolini, D.</creatorcontrib><creatorcontrib>Skita, V.</creatorcontrib><creatorcontrib>Pierce, D.H.</creatorcontrib><creatorcontrib>Scarpa, 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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blasie, J.K.</au><au>Herbette, L.G.</au><au>Pascolini, D.</au><au>Skita, V.</au><au>Pierce, D.H.</au><au>Scarpa, A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1985-07-01</date><risdate>1985</risdate><volume>48</volume><issue>1</issue><spage>9</spage><epage>18</epage><pages>9-18</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>X-ray and neutron diffraction studies of oriented multilayers of a highly purified fraction of isolated sarcoplasmic reticulum (SR) have previously provided the separate profile structures of the lipid bilayer and the Ca2+-ATPase molecule within the membrane profile to approximately 10-A resolution. These studies used biosynthetically deuterated SR phospholipids incorporated isomorphously into the isolated SR membranes via phospholipid transfer proteins. Time-resolved x-ray diffraction studies of these oriented SR membrane multilayers have detected significant changes in the membrane profile structure associated with phosphorylation of the Ca2+-ATPase within a single turnover of the Ca2+-transport cycle. These studies used the flash photolysis of caged ATP to effectively synchronize the ensemble of Ca2+-ATPase molecules in the multilayer, synchrotron x-radiation to provide 100–500-ms data collection times, and double-beam spectrophotometry to monitor the Ca2+-transport process directly in the oriented SR membrane multilayer.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3160394</pmid><doi>10.1016/S0006-3495(85)83756-5</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3495 |
| ispartof | Biophysical journal, 1985-07, Vol.48 (1), p.9-18 |
| issn | 0006-3495 1542-0086 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1329373 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Animals ATP Biological and medical sciences Biological Transport, Active calcium Calcium-Transporting ATPases - metabolism Cell physiology Fundamental and applied biological sciences. Psychology Kinetics Membrane and intracellular transports Molecular and cellular biology Muscles - metabolism Neutrons Rabbits sarcoplasmic reticulum Sarcoplasmic Reticulum - metabolism Spectrum Analysis Time Factors X-ray diffraction X-Ray Diffraction - methods |
| title | Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-15T18%3A26%3A16IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Time-resolved%20x-ray%20diffraction%20studies%20of%20the%20sarcoplasmic%20reticulum%20membrane%20during%20active%20transport&rft.jtitle=Biophysical%20journal&rft.au=Blasie,%20J.K.&rft.date=1985-07-01&rft.volume=48&rft.issue=1&rft.spage=9&rft.epage=18&rft.pages=9-18&rft.issn=0006-3495&rft.eissn=1542-0086&rft.coden=BIOJAU&rft_id=info:doi/10.1016/S0006-3495(85)83756-5&rft_dat=%3Cproquest_pubme%3E14395906%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14395906&rft_id=info:pmid/3160394&rft_els_id=S0006349585837565&rfr_iscdi=true |