Screening of RNA molecules inhibiting human acetylcholinesterase by virtue of systematic evolution of ligands by exponential enrichment
To acquire the specific RNA aptamers inhibiting human red blood cell (RBC) acetylcholinesterase (AChE). Systematic evolution of ligands by exponential enrichment (SELEX) aptamer against human red blood cell membrane AChE was selected by microtiter plate method in vitro. The specifity binding to AChE...
Gespeichert in:
| Veröffentlicht in: | Acta pharmacologica Sinica 2003-07, Vol.24 (7), p.711-714 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 714 |
|---|---|
| container_issue | 7 |
| container_start_page | 711 |
| container_title | Acta pharmacologica Sinica |
| container_volume | 24 |
| creator | Zhang, Xing-Mei Shao, Ning-Sheng Chi, Mu-Gen Sun, Man-Ji |
| description | To acquire the specific RNA aptamers inhibiting human red blood cell (RBC) acetylcholinesterase (AChE).
Systematic evolution of ligands by exponential enrichment (SELEX) aptamer against human red blood cell membrane AChE was selected by microtiter plate method in vitro. The specifity binding to AChE was determined by gel mobility shift analysis. Microcolorispectrophotometric method was used to measure the activity of AChE.
The aptamers to human RBC AChE were identified by 9 reiterative rounds. At the same concentration (2.25 micromol/L), the aptamers did not bind to the recombinant human butyrylcholinesterase (rhBChE) but specifically bound to human RBC AChE and inhibited the enzyme activity.
It is an effective way to isolate the specific AChE inhibitor from the vast oligonucleotide combinatorial library by virtue of SELEX. |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_73399559</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>73399559</sourcerecordid><originalsourceid>FETCH-LOGICAL-p207t-63d70d91b170f6f8fdd1222d50a765c7e43523f7ee6426dff206c16c2dca63bc3</originalsourceid><addsrcrecordid>eNo1kM1KxDAUhbtQnHH0FSQrd4U0aZN2OQz-waDgz7qkyc00kia1SQf7BL62LY6rwz3n48A9Z8k6YzxLc1zSVXIZwifGlNCsukhWGSkLUuZ4nfy8yQHAGXdAXqPX5y3qvAU5WgjIuNY0Ji5ZO3bCISEhTla23hoHIcIgAqBmQkczxBGWgjDNdieikQiO3o7ReLf41hyEU2GB4bv3Dlw0wiJwg5FtN19XybkWNsD1STfJx_3d--4x3b88PO22-7QnmMeUUcWxqrIm41gzXWqlMkKIKrDgrJAccloQqjkAywlTWhPMZMYkUVIw2ki6SW7_evvBf43zE3VnggRrhQM_hppTWlVFUc3gzQkcmw5U3Q-mE8NU_09HfwFhMm2E</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>73399559</pqid></control><display><type>article</type><title>Screening of RNA molecules inhibiting human acetylcholinesterase by virtue of systematic evolution of ligands by exponential enrichment</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Zhang, Xing-Mei ; Shao, Ning-Sheng ; Chi, Mu-Gen ; Sun, Man-Ji</creator><creatorcontrib>Zhang, Xing-Mei ; Shao, Ning-Sheng ; Chi, Mu-Gen ; Sun, Man-Ji</creatorcontrib><description>To acquire the specific RNA aptamers inhibiting human red blood cell (RBC) acetylcholinesterase (AChE).
Systematic evolution of ligands by exponential enrichment (SELEX) aptamer against human red blood cell membrane AChE was selected by microtiter plate method in vitro. The specifity binding to AChE was determined by gel mobility shift analysis. Microcolorispectrophotometric method was used to measure the activity of AChE.
The aptamers to human RBC AChE were identified by 9 reiterative rounds. At the same concentration (2.25 micromol/L), the aptamers did not bind to the recombinant human butyrylcholinesterase (rhBChE) but specifically bound to human RBC AChE and inhibited the enzyme activity.
It is an effective way to isolate the specific AChE inhibitor from the vast oligonucleotide combinatorial library by virtue of SELEX.</description><identifier>ISSN: 1671-4083</identifier><identifier>PMID: 12852840</identifier><language>eng</language><publisher>United States</publisher><subject>Acetylcholinesterase - metabolism ; Binding Sites ; Cholinesterase Inhibitors - isolation & purification ; Cholinesterase Inhibitors - pharmacology ; Combinatorial Chemistry Techniques ; Erythrocyte Membrane - chemistry ; Humans ; Ligands ; RNA - isolation & purification ; RNA - pharmacology ; RNA-Binding Proteins - metabolism</subject><ispartof>Acta pharmacologica Sinica, 2003-07, Vol.24 (7), p.711-714</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12852840$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Xing-Mei</creatorcontrib><creatorcontrib>Shao, Ning-Sheng</creatorcontrib><creatorcontrib>Chi, Mu-Gen</creatorcontrib><creatorcontrib>Sun, Man-Ji</creatorcontrib><title>Screening of RNA molecules inhibiting human acetylcholinesterase by virtue of systematic evolution of ligands by exponential enrichment</title><title>Acta pharmacologica Sinica</title><addtitle>Acta Pharmacol Sin</addtitle><description>To acquire the specific RNA aptamers inhibiting human red blood cell (RBC) acetylcholinesterase (AChE).
Systematic evolution of ligands by exponential enrichment (SELEX) aptamer against human red blood cell membrane AChE was selected by microtiter plate method in vitro. The specifity binding to AChE was determined by gel mobility shift analysis. Microcolorispectrophotometric method was used to measure the activity of AChE.
The aptamers to human RBC AChE were identified by 9 reiterative rounds. At the same concentration (2.25 micromol/L), the aptamers did not bind to the recombinant human butyrylcholinesterase (rhBChE) but specifically bound to human RBC AChE and inhibited the enzyme activity.
It is an effective way to isolate the specific AChE inhibitor from the vast oligonucleotide combinatorial library by virtue of SELEX.</description><subject>Acetylcholinesterase - metabolism</subject><subject>Binding Sites</subject><subject>Cholinesterase Inhibitors - isolation & purification</subject><subject>Cholinesterase Inhibitors - pharmacology</subject><subject>Combinatorial Chemistry Techniques</subject><subject>Erythrocyte Membrane - chemistry</subject><subject>Humans</subject><subject>Ligands</subject><subject>RNA - isolation & purification</subject><subject>RNA - pharmacology</subject><subject>RNA-Binding Proteins - metabolism</subject><issn>1671-4083</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kM1KxDAUhbtQnHH0FSQrd4U0aZN2OQz-waDgz7qkyc00kia1SQf7BL62LY6rwz3n48A9Z8k6YzxLc1zSVXIZwifGlNCsukhWGSkLUuZ4nfy8yQHAGXdAXqPX5y3qvAU5WgjIuNY0Ji5ZO3bCISEhTla23hoHIcIgAqBmQkczxBGWgjDNdieikQiO3o7ReLf41hyEU2GB4bv3Dlw0wiJwg5FtN19XybkWNsD1STfJx_3d--4x3b88PO22-7QnmMeUUcWxqrIm41gzXWqlMkKIKrDgrJAccloQqjkAywlTWhPMZMYkUVIw2ki6SW7_evvBf43zE3VnggRrhQM_hppTWlVFUc3gzQkcmw5U3Q-mE8NU_09HfwFhMm2E</recordid><startdate>200307</startdate><enddate>200307</enddate><creator>Zhang, Xing-Mei</creator><creator>Shao, Ning-Sheng</creator><creator>Chi, Mu-Gen</creator><creator>Sun, Man-Ji</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200307</creationdate><title>Screening of RNA molecules inhibiting human acetylcholinesterase by virtue of systematic evolution of ligands by exponential enrichment</title><author>Zhang, Xing-Mei ; Shao, Ning-Sheng ; Chi, Mu-Gen ; Sun, Man-Ji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p207t-63d70d91b170f6f8fdd1222d50a765c7e43523f7ee6426dff206c16c2dca63bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetylcholinesterase - metabolism</topic><topic>Binding Sites</topic><topic>Cholinesterase Inhibitors - isolation & purification</topic><topic>Cholinesterase Inhibitors - pharmacology</topic><topic>Combinatorial Chemistry Techniques</topic><topic>Erythrocyte Membrane - chemistry</topic><topic>Humans</topic><topic>Ligands</topic><topic>RNA - isolation & purification</topic><topic>RNA - pharmacology</topic><topic>RNA-Binding Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Xing-Mei</creatorcontrib><creatorcontrib>Shao, Ning-Sheng</creatorcontrib><creatorcontrib>Chi, Mu-Gen</creatorcontrib><creatorcontrib>Sun, Man-Ji</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Acta pharmacologica Sinica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Xing-Mei</au><au>Shao, Ning-Sheng</au><au>Chi, Mu-Gen</au><au>Sun, Man-Ji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Screening of RNA molecules inhibiting human acetylcholinesterase by virtue of systematic evolution of ligands by exponential enrichment</atitle><jtitle>Acta pharmacologica Sinica</jtitle><addtitle>Acta Pharmacol Sin</addtitle><date>2003-07</date><risdate>2003</risdate><volume>24</volume><issue>7</issue><spage>711</spage><epage>714</epage><pages>711-714</pages><issn>1671-4083</issn><abstract>To acquire the specific RNA aptamers inhibiting human red blood cell (RBC) acetylcholinesterase (AChE).
Systematic evolution of ligands by exponential enrichment (SELEX) aptamer against human red blood cell membrane AChE was selected by microtiter plate method in vitro. The specifity binding to AChE was determined by gel mobility shift analysis. Microcolorispectrophotometric method was used to measure the activity of AChE.
The aptamers to human RBC AChE were identified by 9 reiterative rounds. At the same concentration (2.25 micromol/L), the aptamers did not bind to the recombinant human butyrylcholinesterase (rhBChE) but specifically bound to human RBC AChE and inhibited the enzyme activity.
It is an effective way to isolate the specific AChE inhibitor from the vast oligonucleotide combinatorial library by virtue of SELEX.</abstract><cop>United States</cop><pmid>12852840</pmid><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1671-4083 |
| ispartof | Acta pharmacologica Sinica, 2003-07, Vol.24 (7), p.711-714 |
| issn | 1671-4083 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73399559 |
| source | MEDLINE; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Acetylcholinesterase - metabolism Binding Sites Cholinesterase Inhibitors - isolation & purification Cholinesterase Inhibitors - pharmacology Combinatorial Chemistry Techniques Erythrocyte Membrane - chemistry Humans Ligands RNA - isolation & purification RNA - pharmacology RNA-Binding Proteins - metabolism |
| title | Screening of RNA molecules inhibiting human acetylcholinesterase by virtue of systematic evolution of ligands by exponential enrichment |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T09%3A08%3A46IST&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=Screening%20of%20RNA%20molecules%20inhibiting%20human%20acetylcholinesterase%20by%20virtue%20of%20systematic%20evolution%20of%20ligands%20by%20exponential%20enrichment&rft.jtitle=Acta%20pharmacologica%20Sinica&rft.au=Zhang,%20Xing-Mei&rft.date=2003-07&rft.volume=24&rft.issue=7&rft.spage=711&rft.epage=714&rft.pages=711-714&rft.issn=1671-4083&rft_id=info:doi/&rft_dat=%3Cproquest_pubme%3E73399559%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=73399559&rft_id=info:pmid/12852840&rfr_iscdi=true |