Conformational transition in biological membrane studyed by the spin label method
Conformational transitions in electron transport particles (ETP) are recorded by variations in the electron spin resonance spectra of the spin label (2,2,6,6-tetramethyl -4-piperidone-1-oxyl-4-caprilic ether) anisotropy. The spin is solubilized in ETP membrane and fixed by hydrophobic interactions....
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Veröffentlicht in: | Biochemical and biophysical research communications 1968-08, Vol.32 (3), p.421-425 |
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creator | Koltover, V.K. Goldfield, M.G. Hendel, L.Ya Rozantzev, E.G. |
description | Conformational transitions in electron transport particles (ETP) are recorded by variations in the electron spin resonance spectra of the spin label (2,2,6,6-tetramethyl -4-piperidone-1-oxyl-4-caprilic ether) anisotropy. The spin is solubilized in ETP membrane and fixed by hydrophobic interactions. Conformational transition takes place after addition of oxidation substrates (succinate, NAD-H
2). Respiratory chain oxidation with ferricyanide restores the correlation time which is the ESR spectrum anisotropy quantitative measure, to its original value. |
doi_str_mv | 10.1016/0006-291X(68)90678-5 |
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2). Respiratory chain oxidation with ferricyanide restores the correlation time which is the ESR spectrum anisotropy quantitative measure, to its original value.</description><subject>Animals</subject><subject>Cattle</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Electron Transport - analysis</subject><subject>Ferricyanides - pharmacology</subject><subject>Membranes - metabolism</subject><subject>Methods</subject><subject>Mitochondria, Muscle - metabolism</subject><subject>NAD - pharmacology</subject><subject>Succinates - pharmacology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1968</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMo67r6DxR6Ej1UkzRNk4sgi1-wIIKCt5AmUzfSNmvSFfbfm7qLR09heJ-ZzDwInRJ8RTDh1xhjnlNJ3i-4uJSYVyIv99CUYIlzSjDbR9M_5BAdxfiJMSGMywmaMColrqopepn7vvGh04PzvW6zIeg-urHIXJ_Vzrf-w5kUdNDVKYMsDmu7AZvVm2xYpnKVuFbXMCLD0ttjdNDoNsLJ7p2ht_u71_ljvnh-eJrfLnLDaDHkkhS4ZrLElSZFVTTUmEIIQRtpLNScpK2ZkQWGdAm1ogRtjTSaS1pyyowtZuh8O3cV_Nca4qA6Fw20bVrSr6MSLDlhhCeQbUETfIwBGrUKrtNhowhWo0k1alKjJsWF-jWpytR2tpu_rjuwf007dSm_2eaQjvx2EFQ0DnoD1gUwg7Le_f_BD2TbgvY</recordid><startdate>19680813</startdate><enddate>19680813</enddate><creator>Koltover, V.K.</creator><creator>Goldfield, M.G.</creator><creator>Hendel, L.Ya</creator><creator>Rozantzev, E.G.</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>19680813</creationdate><title>Conformational transition in biological membrane studyed by the spin label method</title><author>Koltover, V.K. ; Goldfield, M.G. ; Hendel, L.Ya ; Rozantzev, E.G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-9130b49507a1373f2cc38882f9cdeb612914c930e1042d85eadc9ca6925624cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1968</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Electron Transport - analysis</topic><topic>Ferricyanides - pharmacology</topic><topic>Membranes - metabolism</topic><topic>Methods</topic><topic>Mitochondria, Muscle - metabolism</topic><topic>NAD - pharmacology</topic><topic>Succinates - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koltover, V.K.</creatorcontrib><creatorcontrib>Goldfield, M.G.</creatorcontrib><creatorcontrib>Hendel, L.Ya</creatorcontrib><creatorcontrib>Rozantzev, E.G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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>Koltover, V.K.</au><au>Goldfield, M.G.</au><au>Hendel, L.Ya</au><au>Rozantzev, E.G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformational transition in biological membrane studyed by the spin label method</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1968-08-13</date><risdate>1968</risdate><volume>32</volume><issue>3</issue><spage>421</spage><epage>425</epage><pages>421-425</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Conformational transitions in electron transport particles (ETP) are recorded by variations in the electron spin resonance spectra of the spin label (2,2,6,6-tetramethyl -4-piperidone-1-oxyl-4-caprilic ether) anisotropy. The spin is solubilized in ETP membrane and fixed by hydrophobic interactions. Conformational transition takes place after addition of oxidation substrates (succinate, NAD-H
2). Respiratory chain oxidation with ferricyanide restores the correlation time which is the ESR spectrum anisotropy quantitative measure, to its original value.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4299077</pmid><doi>10.1016/0006-291X(68)90678-5</doi><tpages>5</tpages></addata></record> |
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subjects | Animals Cattle Electron Spin Resonance Spectroscopy Electron Transport - analysis Ferricyanides - pharmacology Membranes - metabolism Methods Mitochondria, Muscle - metabolism NAD - pharmacology Succinates - pharmacology |
title | Conformational transition in biological membrane studyed by the spin label method |
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