Remeasurement of electrosprayed proteins in the trapped ion cell of a Fourier transform ion cyclotron resonance mass spectrometer
A single population of multiply charged protein ions formed by electrospray ionization (ESI) is subjected to multiple Fourier transform ion cyclotron resonance (FTICR) excitation and detection events without promoting ion loss from the trapped ion cell. This nondestructive approach to mass spectrome...
Gespeichert in:
| Veröffentlicht in: | Analytical chemistry (Washington) 1993-06, Vol.65 (11), p.1588-1593 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1593 |
|---|---|
| container_issue | 11 |
| container_start_page | 1588 |
| container_title | Analytical chemistry (Washington) |
| container_volume | 65 |
| creator | Guan, Ziqiang Hofstadler, Steven A Laude, David A |
| description | A single population of multiply charged protein ions formed by electrospray ionization (ESI) is subjected to multiple Fourier transform ion cyclotron resonance (FTICR) excitation and detection events without promoting ion loss from the trapped ion cell. This nondestructive approach to mass spectrometric detection will allow detection limits to be significantly reduced by averaging the repetitive time-domain response that follows each excitation event. Under appropriate conditions, unit remeasurement efficiency is observed for large proteins; for example, 250 consecutive remeasurements of a single population of bovine albumin dimer ions (MW 132,532) yield the expected 16-fold improvement in signal-to-noise ratio compared to a single measurement. Examples presented include a 14-fmol sample of horse myoglobin (MW 16,951), which yields a 15:1 S/N for 50 remeasurements compared to a single scan S/N of 2:1 and a 30-fmol sample of bovine albumin dimer which exhibits a S/N of 25:1 for 50 remeasurements compared to a single scan S/N of 3:1. Of both practical and theoretical interest is the observation of a rapid collision-mediated homogeneous relaxation process that can return these large ions to the center of the cell within a few hundred milliseconds after excitation. |
| doi_str_mv | 10.1021/ac00059a018 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_75836939</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>5764193</sourcerecordid><originalsourceid>FETCH-LOGICAL-a410t-bbf8f81440fc1c879a9db7485254f35405031297d6e3c31fbb3368ff474cf8fc3</originalsourceid><addsrcrecordid>eNptkc-L1TAQx4O4rM_Vk2chiOhBqpMmadKjLK4r7KLoqseQ5k2wa5t2kxZ8R_9zU_t4K4ungfl-5sd3hpAnDF4zKNkb6wBA1haYvkc2TJZQVFqX98km53lRKoAH5GFK1wCMAauOybHmpa6U2JDfn7FHm-aYQ5jo4Cl26KY4pDHaHW7pGIcJ25BoG-j0A-kU7TjmfDsE6rDrlhJLz4Y5thgXNSQ_xH7Vd64bcq9AI6Yh2OCQ9jYlmsa_M3qcMD4iR952CR_v4wn5evbu6vS8uPj4_sPp24vCCgZT0TRee82EAO-Y06q29bZRQstSCs-lAAmclbXaVsgdZ75pOK-090IJlysdPyEv1r7Z0c2MaTJ9mxYHNuAwJ6Ok5lXN6ww-uwNeZ3ch72ZKprSEqmYZerVCLp8qRfRmjG1v484wMMtXzD9fyfTTfcu56XF7YPdvyPrzvW6Ts53PV3RtOmBCSVBs2axYsTZN-Osg2_jTVIoraa4-fTHnoPR3xb6Zy8y_XHnr0q2J_y34B73ZsUg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217850691</pqid></control><display><type>article</type><title>Remeasurement of electrosprayed proteins in the trapped ion cell of a Fourier transform ion cyclotron resonance mass spectrometer</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Guan, Ziqiang ; Hofstadler, Steven A ; Laude, David A</creator><creatorcontrib>Guan, Ziqiang ; Hofstadler, Steven A ; Laude, David A</creatorcontrib><description>A single population of multiply charged protein ions formed by electrospray ionization (ESI) is subjected to multiple Fourier transform ion cyclotron resonance (FTICR) excitation and detection events without promoting ion loss from the trapped ion cell. This nondestructive approach to mass spectrometric detection will allow detection limits to be significantly reduced by averaging the repetitive time-domain response that follows each excitation event. Under appropriate conditions, unit remeasurement efficiency is observed for large proteins; for example, 250 consecutive remeasurements of a single population of bovine albumin dimer ions (MW 132,532) yield the expected 16-fold improvement in signal-to-noise ratio compared to a single measurement. Examples presented include a 14-fmol sample of horse myoglobin (MW 16,951), which yields a 15:1 S/N for 50 remeasurements compared to a single scan S/N of 2:1 and a 30-fmol sample of bovine albumin dimer which exhibits a S/N of 25:1 for 50 remeasurements compared to a single scan S/N of 3:1. Of both practical and theoretical interest is the observation of a rapid collision-mediated homogeneous relaxation process that can return these large ions to the center of the cell within a few hundred milliseconds after excitation.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac00059a018</identifier><identifier>PMID: 8328674</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; Biological and medical sciences ; Cattle ; Chemistry ; Electrochemistry ; Fourier Analysis ; Fundamental and applied biological sciences. Psychology ; Ions ; Mass Spectrometry ; Molecular biophysics ; Myoglobin - analysis ; Proteins ; Scientific imaging ; Serum Albumin, Bovine - analysis ; Spectroscopy : techniques and spectras</subject><ispartof>Analytical chemistry (Washington), 1993-06, Vol.65 (11), p.1588-1593</ispartof><rights>1993 INIST-CNRS</rights><rights>Copyright American Chemical Society Jun 1, 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a410t-bbf8f81440fc1c879a9db7485254f35405031297d6e3c31fbb3368ff474cf8fc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ac00059a018$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ac00059a018$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4750719$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8328674$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Guan, Ziqiang</creatorcontrib><creatorcontrib>Hofstadler, Steven A</creatorcontrib><creatorcontrib>Laude, David A</creatorcontrib><title>Remeasurement of electrosprayed proteins in the trapped ion cell of a Fourier transform ion cyclotron resonance mass spectrometer</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>A single population of multiply charged protein ions formed by electrospray ionization (ESI) is subjected to multiple Fourier transform ion cyclotron resonance (FTICR) excitation and detection events without promoting ion loss from the trapped ion cell. This nondestructive approach to mass spectrometric detection will allow detection limits to be significantly reduced by averaging the repetitive time-domain response that follows each excitation event. Under appropriate conditions, unit remeasurement efficiency is observed for large proteins; for example, 250 consecutive remeasurements of a single population of bovine albumin dimer ions (MW 132,532) yield the expected 16-fold improvement in signal-to-noise ratio compared to a single measurement. Examples presented include a 14-fmol sample of horse myoglobin (MW 16,951), which yields a 15:1 S/N for 50 remeasurements compared to a single scan S/N of 2:1 and a 30-fmol sample of bovine albumin dimer which exhibits a S/N of 25:1 for 50 remeasurements compared to a single scan S/N of 3:1. Of both practical and theoretical interest is the observation of a rapid collision-mediated homogeneous relaxation process that can return these large ions to the center of the cell within a few hundred milliseconds after excitation.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Electrochemistry</subject><subject>Fourier Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Ions</subject><subject>Mass Spectrometry</subject><subject>Molecular biophysics</subject><subject>Myoglobin - analysis</subject><subject>Proteins</subject><subject>Scientific imaging</subject><subject>Serum Albumin, Bovine - analysis</subject><subject>Spectroscopy : techniques and spectras</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc-L1TAQx4O4rM_Vk2chiOhBqpMmadKjLK4r7KLoqseQ5k2wa5t2kxZ8R_9zU_t4K4ungfl-5sd3hpAnDF4zKNkb6wBA1haYvkc2TJZQVFqX98km53lRKoAH5GFK1wCMAauOybHmpa6U2JDfn7FHm-aYQ5jo4Cl26KY4pDHaHW7pGIcJ25BoG-j0A-kU7TjmfDsE6rDrlhJLz4Y5thgXNSQ_xH7Vd64bcq9AI6Yh2OCQ9jYlmsa_M3qcMD4iR952CR_v4wn5evbu6vS8uPj4_sPp24vCCgZT0TRee82EAO-Y06q29bZRQstSCs-lAAmclbXaVsgdZ75pOK-090IJlysdPyEv1r7Z0c2MaTJ9mxYHNuAwJ6Ok5lXN6ww-uwNeZ3ch72ZKprSEqmYZerVCLp8qRfRmjG1v484wMMtXzD9fyfTTfcu56XF7YPdvyPrzvW6Ts53PV3RtOmBCSVBs2axYsTZN-Osg2_jTVIoraa4-fTHnoPR3xb6Zy8y_XHnr0q2J_y34B73ZsUg</recordid><startdate>19930601</startdate><enddate>19930601</enddate><creator>Guan, Ziqiang</creator><creator>Hofstadler, Steven A</creator><creator>Laude, David A</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19930601</creationdate><title>Remeasurement of electrosprayed proteins in the trapped ion cell of a Fourier transform ion cyclotron resonance mass spectrometer</title><author>Guan, Ziqiang ; Hofstadler, Steven A ; Laude, David A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a410t-bbf8f81440fc1c879a9db7485254f35405031297d6e3c31fbb3368ff474cf8fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Electrochemistry</topic><topic>Fourier Analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Ions</topic><topic>Mass Spectrometry</topic><topic>Molecular biophysics</topic><topic>Myoglobin - analysis</topic><topic>Proteins</topic><topic>Scientific imaging</topic><topic>Serum Albumin, Bovine - analysis</topic><topic>Spectroscopy : techniques and spectras</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guan, Ziqiang</creatorcontrib><creatorcontrib>Hofstadler, Steven A</creatorcontrib><creatorcontrib>Laude, David A</creatorcontrib><collection>Istex</collection><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>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guan, Ziqiang</au><au>Hofstadler, Steven A</au><au>Laude, David A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Remeasurement of electrosprayed proteins in the trapped ion cell of a Fourier transform ion cyclotron resonance mass spectrometer</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>1993-06-01</date><risdate>1993</risdate><volume>65</volume><issue>11</issue><spage>1588</spage><epage>1593</epage><pages>1588-1593</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>A single population of multiply charged protein ions formed by electrospray ionization (ESI) is subjected to multiple Fourier transform ion cyclotron resonance (FTICR) excitation and detection events without promoting ion loss from the trapped ion cell. This nondestructive approach to mass spectrometric detection will allow detection limits to be significantly reduced by averaging the repetitive time-domain response that follows each excitation event. Under appropriate conditions, unit remeasurement efficiency is observed for large proteins; for example, 250 consecutive remeasurements of a single population of bovine albumin dimer ions (MW 132,532) yield the expected 16-fold improvement in signal-to-noise ratio compared to a single measurement. Examples presented include a 14-fmol sample of horse myoglobin (MW 16,951), which yields a 15:1 S/N for 50 remeasurements compared to a single scan S/N of 2:1 and a 30-fmol sample of bovine albumin dimer which exhibits a S/N of 25:1 for 50 remeasurements compared to a single scan S/N of 3:1. Of both practical and theoretical interest is the observation of a rapid collision-mediated homogeneous relaxation process that can return these large ions to the center of the cell within a few hundred milliseconds after excitation.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>8328674</pmid><doi>10.1021/ac00059a018</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-2700 |
| ispartof | Analytical chemistry (Washington), 1993-06, Vol.65 (11), p.1588-1593 |
| issn | 0003-2700 1520-6882 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75836939 |
| source | MEDLINE; American Chemical Society Journals |
| subjects | Animals Biological and medical sciences Cattle Chemistry Electrochemistry Fourier Analysis Fundamental and applied biological sciences. Psychology Ions Mass Spectrometry Molecular biophysics Myoglobin - analysis Proteins Scientific imaging Serum Albumin, Bovine - analysis Spectroscopy : techniques and spectras |
| title | Remeasurement of electrosprayed proteins in the trapped ion cell of a Fourier transform ion cyclotron resonance mass spectrometer |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T22%3A43%3A03IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Remeasurement%20of%20electrosprayed%20proteins%20in%20the%20trapped%20ion%20cell%20of%20a%20Fourier%20transform%20ion%20cyclotron%20resonance%20mass%20spectrometer&rft.jtitle=Analytical%20chemistry%20(Washington)&rft.au=Guan,%20Ziqiang&rft.date=1993-06-01&rft.volume=65&rft.issue=11&rft.spage=1588&rft.epage=1593&rft.pages=1588-1593&rft.issn=0003-2700&rft.eissn=1520-6882&rft.coden=ANCHAM&rft_id=info:doi/10.1021/ac00059a018&rft_dat=%3Cproquest_cross%3E5764193%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217850691&rft_id=info:pmid/8328674&rfr_iscdi=true |