The binding of vanadium (V) oligoanions to sarcoplasmic reticulum
The binding of monovanadate and decavanadate anions to sarcoplasmic reticulum vesicles was measured by equilibrium sedimentation. The affinity of vanadate binding and the molar amount of vanadium (V) bound at equilibrium is much greater with decavanadate than with monovanadate. The binding data can...
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| Veröffentlicht in: | European journal of biochemistry 1985-04, Vol.148 (1), p.119-126 |
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| container_title | European journal of biochemistry |
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| creator | VARGA, Sandor CSERMELY, Peter MARTONOSI, Anthony |
| description | The binding of monovanadate and decavanadate anions to sarcoplasmic reticulum vesicles was measured by equilibrium sedimentation. The affinity of vanadate binding and the molar amount of vanadium (V) bound at equilibrium is much greater with decavanadate than with monovanadate. The binding data can be rationalized in terms of one binding site per ATPase molecule for monovanadate and two sites per ATPase for decavanadate.
The Ca‐ATPase crystals formed with monovanadate and with decavanadate are similar in appearance, but decavanadate is particularly effective in promoting the crystallization of Ca2+‐ATPase at low V concentration (10–100 μM) in a Ca2+‐free medium. |
| doi_str_mv | 10.1111/j.1432-1033.1985.tb08815.x |
| format | Article |
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The Ca‐ATPase crystals formed with monovanadate and with decavanadate are similar in appearance, but decavanadate is particularly effective in promoting the crystallization of Ca2+‐ATPase at low V concentration (10–100 μM) in a Ca2+‐free medium.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1985.tb08815.x</identifier><identifier>PMID: 3156737</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Biological and medical sciences ; calcium ; Calcium-Transporting ATPases - antagonists & inhibitors ; Calcium-Transporting ATPases - metabolism ; Cell physiology ; Crystallization ; Fundamental and applied biological sciences. Psychology ; In Vitro Techniques ; Microscopy, Electron ; Microsomes - metabolism ; Molecular and cellular biology ; Muscle contraction ; Polymers - metabolism ; Polymers - pharmacology ; Rabbits ; sarcoplasmic reticulum ; Sarcoplasmic Reticulum - enzymology ; Sarcoplasmic Reticulum - metabolism ; Vanadates ; vanadium ; Vanadium - metabolism ; Vanadium - pharmacology</subject><ispartof>European journal of biochemistry, 1985-04, Vol.148 (1), p.119-126</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5489-d8fad3c08c3afe49b6ae8707e4f6e7b8b74e5355a1db7d545fc2f3ae7604b71f3</citedby><cites>FETCH-LOGICAL-c5489-d8fad3c08c3afe49b6ae8707e4f6e7b8b74e5355a1db7d545fc2f3ae7604b71f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8442289$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3156737$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>VARGA, Sandor</creatorcontrib><creatorcontrib>CSERMELY, Peter</creatorcontrib><creatorcontrib>MARTONOSI, Anthony</creatorcontrib><title>The binding of vanadium (V) oligoanions to sarcoplasmic reticulum</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The binding of monovanadate and decavanadate anions to sarcoplasmic reticulum vesicles was measured by equilibrium sedimentation. The affinity of vanadate binding and the molar amount of vanadium (V) bound at equilibrium is much greater with decavanadate than with monovanadate. The binding data can be rationalized in terms of one binding site per ATPase molecule for monovanadate and two sites per ATPase for decavanadate.
The Ca‐ATPase crystals formed with monovanadate and with decavanadate are similar in appearance, but decavanadate is particularly effective in promoting the crystallization of Ca2+‐ATPase at low V concentration (10–100 μM) in a Ca2+‐free medium.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>calcium</subject><subject>Calcium-Transporting ATPases - antagonists & inhibitors</subject><subject>Calcium-Transporting ATPases - metabolism</subject><subject>Cell physiology</subject><subject>Crystallization</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>In Vitro Techniques</subject><subject>Microscopy, Electron</subject><subject>Microsomes - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Muscle contraction</subject><subject>Polymers - metabolism</subject><subject>Polymers - pharmacology</subject><subject>Rabbits</subject><subject>sarcoplasmic reticulum</subject><subject>Sarcoplasmic Reticulum - enzymology</subject><subject>Sarcoplasmic Reticulum - metabolism</subject><subject>Vanadates</subject><subject>vanadium</subject><subject>Vanadium - metabolism</subject><subject>Vanadium - pharmacology</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE9LwzAYh4Moc04_glBERA-tSZM0qReZY1Nh4MHpNaRpohltM5tWt29vx8qu4nt5D7_n_cMDwAWCEerqdhkhguMQQYwjlHIaNRnkHNFofQCG--gQDCFEJIxTmhyDE--XEMIkTdgADDCiCcNsCMaLTx1ktspt9RE4E3zLSua2LYPr95vAFfbDycq6ygeNC7yslVsV0pdWBbVurGqLtjwFR0YWXp_1fQTeZtPF5Cmcvzw-T8bzUFHC0zDnRuZYQa6wNJqkWSI1Z5BpYhLNMp4xoimmVKI8Yzkl1KjYYKlZAknGkMEjcLXbu6rdV6t9I0rrlS4KWWnXetGBOCYp-xNEJCaMJqQD73agqp33tTZiVdtS1huBoNiKFkuxtSm2NsVWtOhFi3U3fN5fabNS5_vR3myXX_a59EoWppaVsn6PcULimKcddr_DfmyhN_94QMymD68IpfgX_niadQ</recordid><startdate>198504</startdate><enddate>198504</enddate><creator>VARGA, Sandor</creator><creator>CSERMELY, Peter</creator><creator>MARTONOSI, Anthony</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</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>7QP</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>198504</creationdate><title>The binding of vanadium (V) oligoanions to sarcoplasmic reticulum</title><author>VARGA, Sandor ; CSERMELY, Peter ; MARTONOSI, Anthony</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5489-d8fad3c08c3afe49b6ae8707e4f6e7b8b74e5355a1db7d545fc2f3ae7604b71f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>calcium</topic><topic>Calcium-Transporting ATPases - antagonists & inhibitors</topic><topic>Calcium-Transporting ATPases - metabolism</topic><topic>Cell physiology</topic><topic>Crystallization</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>In Vitro Techniques</topic><topic>Microscopy, Electron</topic><topic>Microsomes - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Muscle contraction</topic><topic>Polymers - metabolism</topic><topic>Polymers - pharmacology</topic><topic>Rabbits</topic><topic>sarcoplasmic reticulum</topic><topic>Sarcoplasmic Reticulum - enzymology</topic><topic>Sarcoplasmic Reticulum - metabolism</topic><topic>Vanadates</topic><topic>vanadium</topic><topic>Vanadium - metabolism</topic><topic>Vanadium - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>VARGA, Sandor</creatorcontrib><creatorcontrib>CSERMELY, Peter</creatorcontrib><creatorcontrib>MARTONOSI, Anthony</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>Calcium & Calcified Tissue Abstracts</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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>VARGA, Sandor</au><au>CSERMELY, Peter</au><au>MARTONOSI, Anthony</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The binding of vanadium (V) oligoanions to sarcoplasmic reticulum</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1985-04</date><risdate>1985</risdate><volume>148</volume><issue>1</issue><spage>119</spage><epage>126</epage><pages>119-126</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The binding of monovanadate and decavanadate anions to sarcoplasmic reticulum vesicles was measured by equilibrium sedimentation. The affinity of vanadate binding and the molar amount of vanadium (V) bound at equilibrium is much greater with decavanadate than with monovanadate. The binding data can be rationalized in terms of one binding site per ATPase molecule for monovanadate and two sites per ATPase for decavanadate.
The Ca‐ATPase crystals formed with monovanadate and with decavanadate are similar in appearance, but decavanadate is particularly effective in promoting the crystallization of Ca2+‐ATPase at low V concentration (10–100 μM) in a Ca2+‐free medium.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>3156737</pmid><doi>10.1111/j.1432-1033.1985.tb08815.x</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1985-04, Vol.148 (1), p.119-126 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76032497 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences calcium Calcium-Transporting ATPases - antagonists & inhibitors Calcium-Transporting ATPases - metabolism Cell physiology Crystallization Fundamental and applied biological sciences. Psychology In Vitro Techniques Microscopy, Electron Microsomes - metabolism Molecular and cellular biology Muscle contraction Polymers - metabolism Polymers - pharmacology Rabbits sarcoplasmic reticulum Sarcoplasmic Reticulum - enzymology Sarcoplasmic Reticulum - metabolism Vanadates vanadium Vanadium - metabolism Vanadium - pharmacology |
| title | The binding of vanadium (V) oligoanions to sarcoplasmic reticulum |
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