The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion
Inhibition by calcium of the steady‐state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 ± 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 μM A23187 ionophore). It is concluded that dissociation of the two Ca2+ ions from E‐P·Ca2 is sequential and...
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| Veröffentlicht in: | FEBS letters 1990-01, Vol.260 (1), p.83-84 |
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| container_title | FEBS letters |
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| creator | Khananshvili, D. Myung, J. Kolouch, R. Jencks, W.P. |
| description | Inhibition by calcium of the steady‐state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 ± 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 μM A23187 ionophore). It is concluded that dissociation of the two Ca2+ ions from E‐P·Ca2 is sequential and that the inhibition arises from the binding of one Ca2+ to A‐P·Ca1. |
| doi_str_mv | 10.1016/0014-5793(90)80071-P |
| format | Article |
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It is concluded that dissociation of the two Ca2+ ions from E‐P·Ca2 is sequential and that the inhibition arises from the binding of one Ca2+ to A‐P·Ca1.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(90)80071-P</identifier><identifier>PMID: 2137096</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier</publisher><subject>Animals ; ATPase, calcium ; Binding Sites - drug effects ; Binding, Competitive ; Calcimycin - pharmacology ; Calcium ; Calcium - pharmacology ; Calcium-Transporting ATPases - antagonists & inhibitors ; Exact sciences and technology ; Inhibition ; Magnesium - pharmacology ; Mathematical analysis ; Mathematics ; Potential theory ; Rabbits ; Sarcoplasmic Reticulum - enzymology ; Sciences and techniques of general use</subject><ispartof>FEBS letters, 1990-01, Vol.260 (1), p.83-84</ispartof><rights>FEBS Letters 260 (1990) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19737171$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2137096$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Khananshvili, D.</creatorcontrib><creatorcontrib>Myung, J.</creatorcontrib><creatorcontrib>Kolouch, R.</creatorcontrib><creatorcontrib>Jencks, W.P.</creatorcontrib><title>The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Inhibition by calcium of the steady‐state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 ± 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 μM A23187 ionophore). It is concluded that dissociation of the two Ca2+ ions from E‐P·Ca2 is sequential and that the inhibition arises from the binding of one Ca2+ to A‐P·Ca1.</description><subject>Animals</subject><subject>ATPase, calcium</subject><subject>Binding Sites - drug effects</subject><subject>Binding, Competitive</subject><subject>Calcimycin - pharmacology</subject><subject>Calcium</subject><subject>Calcium - pharmacology</subject><subject>Calcium-Transporting ATPases - antagonists & inhibitors</subject><subject>Exact sciences and technology</subject><subject>Inhibition</subject><subject>Magnesium - pharmacology</subject><subject>Mathematical analysis</subject><subject>Mathematics</subject><subject>Potential theory</subject><subject>Rabbits</subject><subject>Sarcoplasmic Reticulum - enzymology</subject><subject>Sciences and techniques of general use</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkd1LwzAUxYMoc07_A4W8KIpUbz7aNI9zbDoY2If5HNI0ZZF-zGZF9t_bbmU-Xe45Py7ccxC6JfBCgESvAIQHoZDsUcJTDCBIkJyhMYkFCxiP4nM0PiGX6Mr7b-j2mMgRGlHCBMhojJbrjcVGF8a1JZ6uE-0trnPsdWPqbaF96Qxu7M6ZtugA57GrNi51O5vhdI_ryuKZps_Y1dU1ush14e3NMCfoazFfzz6C1ef7cjZdBVvCoyQIWSYiLUXMgdoskwR0CpHUNEsNz-OUGpHnmqZRajlnEoBSypnJtRAW4jxkE_RwvLtt6p_W-p0qnTe2KHRl69YrIUNJYk478G4A27S0mdo2rtTNXg2_d_794GvfJZA3ujLOnzAiBRNEkI5bHLlfV9j9vw-qr0H1Gas-YyVBHWpQiVrM32hv9LqEg5qwP0X6evA</recordid><startdate>19900115</startdate><enddate>19900115</enddate><creator>Khananshvili, D.</creator><creator>Myung, J.</creator><creator>Kolouch, R.</creator><creator>Jencks, W.P.</creator><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>7X8</scope></search><sort><creationdate>19900115</creationdate><title>The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion</title><author>Khananshvili, D. ; Myung, J. ; Kolouch, R. ; Jencks, W.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p146P-53d76a978402edd910ab069a2dbc4f8b2c7ffa2b6be44390022243cfa77e08f53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Animals</topic><topic>ATPase, calcium</topic><topic>Binding Sites - drug effects</topic><topic>Binding, Competitive</topic><topic>Calcimycin - pharmacology</topic><topic>Calcium</topic><topic>Calcium - pharmacology</topic><topic>Calcium-Transporting ATPases - antagonists & inhibitors</topic><topic>Exact sciences and technology</topic><topic>Inhibition</topic><topic>Magnesium - pharmacology</topic><topic>Mathematical analysis</topic><topic>Mathematics</topic><topic>Potential theory</topic><topic>Rabbits</topic><topic>Sarcoplasmic Reticulum - enzymology</topic><topic>Sciences and techniques of general use</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Khananshvili, D.</creatorcontrib><creatorcontrib>Myung, J.</creatorcontrib><creatorcontrib>Kolouch, R.</creatorcontrib><creatorcontrib>Jencks, W.P.</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Khananshvili, D.</au><au>Myung, J.</au><au>Kolouch, R.</au><au>Jencks, W.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1990-01-15</date><risdate>1990</risdate><volume>260</volume><issue>1</issue><spage>83</spage><epage>84</epage><pages>83-84</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Inhibition by calcium of the steady‐state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 ± 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 μM A23187 ionophore). 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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals ATPase, calcium Binding Sites - drug effects Binding, Competitive Calcimycin - pharmacology Calcium Calcium - pharmacology Calcium-Transporting ATPases - antagonists & inhibitors Exact sciences and technology Inhibition Magnesium - pharmacology Mathematical analysis Mathematics Potential theory Rabbits Sarcoplasmic Reticulum - enzymology Sciences and techniques of general use |
| title | The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion |
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