Allosteric effects of phenyltrimethylammonium and propidium on acetylcholinesterase active site
Different spin labelled fluorophosphates and fluorophosphonates with different chain length were investigated with respect to their sensitivity to the allosteric changes of acetylcholinesterase active site produced by phenyltrimethylammonium (Pta) or d-tubocurarine (TC); only fluorophosphates were f...
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| Veröffentlicht in: | Pflügers Archiv 1996, Vol.431 (6 Suppl 2), p.R277-R278 |
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| container_end_page | R278 |
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| container_issue | 6 Suppl 2 |
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| container_title | Pflügers Archiv |
| container_volume | 431 |
| creator | Stalc, A Sentjurc, M Pecar, S |
| description | Different spin labelled fluorophosphates and fluorophosphonates with different chain length were investigated with respect to their sensitivity to the allosteric changes of acetylcholinesterase active site produced by phenyltrimethylammonium (Pta) or d-tubocurarine (TC); only fluorophosphates were found to be sensitive to these changes. Therefore fluorophosphates were chosen also for the study of allosteric effects of propidium. The addition of Pta and propidium to spin labelled membrane acetylcholinesterase of the Torpedo marmorata electric organ decreased maximal hyperfine splitting of the EPR spectrum, indicating that the microgeography of the acetylcholinesterase active site is usually changed in a way which increases the freedom of motion of the spin label's piperidine ring. TC alone did not change the EPR spectrum, but it prevented the influence of Pta and not that of propidium. |
| doi_str_mv | 10.1007/bf02346376 |
| format | Article |
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Therefore fluorophosphates were chosen also for the study of allosteric effects of propidium. The addition of Pta and propidium to spin labelled membrane acetylcholinesterase of the Torpedo marmorata electric organ decreased maximal hyperfine splitting of the EPR spectrum, indicating that the microgeography of the acetylcholinesterase active site is usually changed in a way which increases the freedom of motion of the spin label's piperidine ring. TC alone did not change the EPR spectrum, but it prevented the influence of Pta and not that of propidium.</description><identifier>ISSN: 0031-6768</identifier><identifier>EISSN: 1432-2013</identifier><identifier>DOI: 10.1007/bf02346376</identifier><identifier>PMID: 8739372</identifier><language>eng</language><publisher>Germany</publisher><subject>Acetylcholinesterase - chemistry ; Allosteric Site ; Animals ; Electric Organ - enzymology ; Electron Spin Resonance Spectroscopy ; Indicators and Reagents ; Kinetics ; Propidium - chemistry ; Protein Conformation ; Quaternary Ammonium Compounds - chemistry ; Spin Labels ; Torpedo - metabolism</subject><ispartof>Pflügers Archiv, 1996, Vol.431 (6 Suppl 2), p.R277-R278</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c156t-538573bb8a5b4e8c8afe4f6521f9615e651cdc01f3ce73d96fdeb341191b9f7c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8739372$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stalc, A</creatorcontrib><creatorcontrib>Sentjurc, M</creatorcontrib><creatorcontrib>Pecar, S</creatorcontrib><title>Allosteric effects of phenyltrimethylammonium and propidium on acetylcholinesterase active site</title><title>Pflügers Archiv</title><addtitle>Pflugers Arch</addtitle><description>Different spin labelled fluorophosphates and fluorophosphonates with different chain length were investigated with respect to their sensitivity to the allosteric changes of acetylcholinesterase active site produced by phenyltrimethylammonium (Pta) or d-tubocurarine (TC); only fluorophosphates were found to be sensitive to these changes. Therefore fluorophosphates were chosen also for the study of allosteric effects of propidium. The addition of Pta and propidium to spin labelled membrane acetylcholinesterase of the Torpedo marmorata electric organ decreased maximal hyperfine splitting of the EPR spectrum, indicating that the microgeography of the acetylcholinesterase active site is usually changed in a way which increases the freedom of motion of the spin label's piperidine ring. TC alone did not change the EPR spectrum, but it prevented the influence of Pta and not that of propidium.</description><subject>Acetylcholinesterase - chemistry</subject><subject>Allosteric Site</subject><subject>Animals</subject><subject>Electric Organ - enzymology</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Indicators and Reagents</subject><subject>Kinetics</subject><subject>Propidium - chemistry</subject><subject>Protein Conformation</subject><subject>Quaternary Ammonium Compounds - chemistry</subject><subject>Spin Labels</subject><subject>Torpedo - metabolism</subject><issn>0031-6768</issn><issn>1432-2013</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kM1LxDAQxYMo67p68S705EGo5qNN0uO6-AULXvRc0nTCRtKmNqnQ_94su8ochhl-PN57CF0TfE8wFg-NwZQVnAl-gpakYDSnmLBTtMSYkZwLLs_RRQhfGGNaSLpACylYxQRdonrtnA8RRqszMAZ0DJk32bCDfnZxtB3E3exU1_neTl2m-jYbRj_Ydn_5PlMa4uz0zjvbw15HBUjPaH8gCzbCJTozygW4Ou4V-nx--ti85tv3l7fNeptrUvKYl0yWgjWNVGVTgNRSGSgMLykxFScl8JLoVmNimAbB2oqbFhpWEFKRpjJCsxW6Pegmd99TclJ3NmhwTvXgp1ALSSVOk8C7A6hHH8IIph5SSjXONcH1vs368fmvzQTfHFWnpoP2Hz3Wx34BXKFx2g</recordid><startdate>1996</startdate><enddate>1996</enddate><creator>Stalc, A</creator><creator>Sentjurc, M</creator><creator>Pecar, S</creator><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>1996</creationdate><title>Allosteric effects of phenyltrimethylammonium and propidium on acetylcholinesterase active site</title><author>Stalc, A ; Sentjurc, M ; Pecar, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c156t-538573bb8a5b4e8c8afe4f6521f9615e651cdc01f3ce73d96fdeb341191b9f7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Acetylcholinesterase - chemistry</topic><topic>Allosteric Site</topic><topic>Animals</topic><topic>Electric Organ - enzymology</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Indicators and Reagents</topic><topic>Kinetics</topic><topic>Propidium - chemistry</topic><topic>Protein Conformation</topic><topic>Quaternary Ammonium Compounds - chemistry</topic><topic>Spin Labels</topic><topic>Torpedo - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stalc, A</creatorcontrib><creatorcontrib>Sentjurc, M</creatorcontrib><creatorcontrib>Pecar, S</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>Pflügers Archiv</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stalc, A</au><au>Sentjurc, M</au><au>Pecar, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Allosteric effects of phenyltrimethylammonium and propidium on acetylcholinesterase active site</atitle><jtitle>Pflügers Archiv</jtitle><addtitle>Pflugers Arch</addtitle><date>1996</date><risdate>1996</risdate><volume>431</volume><issue>6 Suppl 2</issue><spage>R277</spage><epage>R278</epage><pages>R277-R278</pages><issn>0031-6768</issn><eissn>1432-2013</eissn><abstract>Different spin labelled fluorophosphates and fluorophosphonates with different chain length were investigated with respect to their sensitivity to the allosteric changes of acetylcholinesterase active site produced by phenyltrimethylammonium (Pta) or d-tubocurarine (TC); only fluorophosphates were found to be sensitive to these changes. Therefore fluorophosphates were chosen also for the study of allosteric effects of propidium. The addition of Pta and propidium to spin labelled membrane acetylcholinesterase of the Torpedo marmorata electric organ decreased maximal hyperfine splitting of the EPR spectrum, indicating that the microgeography of the acetylcholinesterase active site is usually changed in a way which increases the freedom of motion of the spin label's piperidine ring. TC alone did not change the EPR spectrum, but it prevented the influence of Pta and not that of propidium.</abstract><cop>Germany</cop><pmid>8739372</pmid><doi>10.1007/bf02346376</doi></addata></record> |
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| identifier | ISSN: 0031-6768 |
| ispartof | Pflügers Archiv, 1996, Vol.431 (6 Suppl 2), p.R277-R278 |
| issn | 0031-6768 1432-2013 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78280808 |
| source | MEDLINE; SpringerLink Journals |
| subjects | Acetylcholinesterase - chemistry Allosteric Site Animals Electric Organ - enzymology Electron Spin Resonance Spectroscopy Indicators and Reagents Kinetics Propidium - chemistry Protein Conformation Quaternary Ammonium Compounds - chemistry Spin Labels Torpedo - metabolism |
| title | Allosteric effects of phenyltrimethylammonium and propidium on acetylcholinesterase active site |
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