An Improved Measurement of Isotopic Ratios by High Resolution Mass Spectrometry
The study of protein kinetics requires an accurate measurement of isotopic ratios of peptides. Although Fourier transform-ion cyclotron resonance (FT-ICR) mass spectrometers yield accurate mass measurements of analytes, the isotopologue ratios are consistently lower than predicted. Recently, we demo...
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Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2013-02, Vol.24 (2), p.309-312 |
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creator | Ilchenko, Serguei Previs, Stephen F. Rachdaoui, Nadia Willard, Belinda McCullough, Arthur J. Kasumov, Takhar |
description | The study of protein kinetics requires an accurate measurement of isotopic ratios of peptides. Although Fourier transform-ion cyclotron resonance (FT-ICR) mass spectrometers yield accurate mass measurements of analytes, the isotopologue ratios are consistently lower than predicted. Recently, we demonstrated that the magnitude of the spectral error in the FT-ICR mass spectrometer is proportional to the scan duration of ions. Here, we present a novel isotopic ratio extrapolation (IRE) method for obtaining accurate isotopic ratio measurements. Accuracy is achieved by performing scans with different duration and extrapolation of the data to the initial moment of the ion rotation; IRE minimizes the absolute isotopic ratio error to ≤1 %. We demonstrate the application of IRE in protein turnover studies using
2
H
2
O-metabolic labeling. Overall, this technique allows accurate measurements of the isotopic ratios of proteolytic peptides, a critical step for enabling routine studies of proteome dynamics. |
doi_str_mv | 10.1007/s13361-012-0536-2 |
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2
H
2
O-metabolic labeling. Overall, this technique allows accurate measurements of the isotopic ratios of proteolytic peptides, a critical step for enabling routine studies of proteome dynamics.</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1007/s13361-012-0536-2</identifier><identifier>PMID: 23283729</identifier><language>eng</language><publisher>New York: Springer-Verlag</publisher><subject>Albumins - analysis ; Albumins - chemistry ; Albumins - metabolism ; Analytical Chemistry ; Animals ; Application Note ; Bioinformatics ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Cyclotron resonance ; Deuterium - analysis ; Deuterium - metabolism ; Extrapolation ; Fourier transforms ; Ions ; Isotope Labeling - methods ; Isotopes ; Mass spectrometers ; Mass spectrometry ; Mass Spectrometry - methods ; Organic Chemistry ; Peptide Fragments - analysis ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Peptides ; Peptides - analysis ; Peptides - chemistry ; Peptides - metabolism ; Proteome - analysis ; Proteome - chemistry ; Proteome - metabolism ; Proteomics ; Rats ; Reproducibility of Results ; Spectrometers</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2013-02, Vol.24 (2), p.309-312</ispartof><rights>American Society for Mass Spectrometry 2012</rights><rights>Journal of The American Society for Mass Spectrometry is a copyright of Springer, 2013.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-8561bdbc9d612ae12b5bba071d9c2e85bfab2038baf468fc98cfd2ba00a1bb903</citedby><cites>FETCH-LOGICAL-c470t-8561bdbc9d612ae12b5bba071d9c2e85bfab2038baf468fc98cfd2ba00a1bb903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s13361-012-0536-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s13361-012-0536-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23283729$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ilchenko, Serguei</creatorcontrib><creatorcontrib>Previs, Stephen F.</creatorcontrib><creatorcontrib>Rachdaoui, Nadia</creatorcontrib><creatorcontrib>Willard, Belinda</creatorcontrib><creatorcontrib>McCullough, Arthur J.</creatorcontrib><creatorcontrib>Kasumov, Takhar</creatorcontrib><title>An Improved Measurement of Isotopic Ratios by High Resolution Mass Spectrometry</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J. Am. Soc. Mass Spectrom</addtitle><addtitle>J Am Soc Mass Spectrom</addtitle><description>The study of protein kinetics requires an accurate measurement of isotopic ratios of peptides. Although Fourier transform-ion cyclotron resonance (FT-ICR) mass spectrometers yield accurate mass measurements of analytes, the isotopologue ratios are consistently lower than predicted. Recently, we demonstrated that the magnitude of the spectral error in the FT-ICR mass spectrometer is proportional to the scan duration of ions. Here, we present a novel isotopic ratio extrapolation (IRE) method for obtaining accurate isotopic ratio measurements. Accuracy is achieved by performing scans with different duration and extrapolation of the data to the initial moment of the ion rotation; IRE minimizes the absolute isotopic ratio error to ≤1 %. We demonstrate the application of IRE in protein turnover studies using
2
H
2
O-metabolic labeling. Overall, this technique allows accurate measurements of the isotopic ratios of proteolytic peptides, a critical step for enabling routine studies of proteome dynamics.</description><subject>Albumins - analysis</subject><subject>Albumins - chemistry</subject><subject>Albumins - metabolism</subject><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Application Note</subject><subject>Bioinformatics</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Cyclotron resonance</subject><subject>Deuterium - analysis</subject><subject>Deuterium - metabolism</subject><subject>Extrapolation</subject><subject>Fourier transforms</subject><subject>Ions</subject><subject>Isotope Labeling - methods</subject><subject>Isotopes</subject><subject>Mass spectrometers</subject><subject>Mass spectrometry</subject><subject>Mass Spectrometry - methods</subject><subject>Organic Chemistry</subject><subject>Peptide Fragments - analysis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptides</subject><subject>Peptides - analysis</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Proteome - analysis</subject><subject>Proteome - chemistry</subject><subject>Proteome - metabolism</subject><subject>Proteomics</subject><subject>Rats</subject><subject>Reproducibility of Results</subject><subject>Spectrometers</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kU1r3DAQhkVpyG7S_IBeiqCXXtzMSP6QLoUlNMlClkCSnoUkyxsH23IlO7D_Plo2DWmhJw2aZ975eAn5jPAdAarziJyXmAGyDApeZuwDWaKoZIbI-McUQ55nwKFYkJMYnwCwAlkdkwXjTPCKySW5XQ103Y_BP7uabpyOc3C9GybqG7qOfvJja-mdnlofqdnR63b7SO9c9N2cvga60THS-9HZKfjeTWH3iRw1uovu7PU9Jb8ufz5cXGc3t1fri9VNZvMKpkwUJZraWFmXyLRDZgpjNFRYS8ucKEyjDQMujG7yUjRWCtvULBGg0RgJ_JT8OOiOs-ldbdPIQXdqDG2vw0553aq_M0P7qLb-WXEh00FEEvj2KhD879nFSfVttK7r9OD8HBUyUcq84gwT-vUf9MnPYUjrKZQFSMkw31N4oGzwMQbXvA2DoPZ2qYNdKtml9nYplmq-vN_ireKPPwlgByCm1LB14V3r_6q-APZfoXU</recordid><startdate>20130201</startdate><enddate>20130201</enddate><creator>Ilchenko, Serguei</creator><creator>Previs, Stephen F.</creator><creator>Rachdaoui, Nadia</creator><creator>Willard, Belinda</creator><creator>McCullough, Arthur J.</creator><creator>Kasumov, Takhar</creator><general>Springer-Verlag</general><general>Springer Nature B.V</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20130201</creationdate><title>An Improved Measurement of Isotopic Ratios by High Resolution Mass Spectrometry</title><author>Ilchenko, Serguei ; 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Am. Soc. Mass Spectrom</stitle><addtitle>J Am Soc Mass Spectrom</addtitle><date>2013-02-01</date><risdate>2013</risdate><volume>24</volume><issue>2</issue><spage>309</spage><epage>312</epage><pages>309-312</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>The study of protein kinetics requires an accurate measurement of isotopic ratios of peptides. Although Fourier transform-ion cyclotron resonance (FT-ICR) mass spectrometers yield accurate mass measurements of analytes, the isotopologue ratios are consistently lower than predicted. Recently, we demonstrated that the magnitude of the spectral error in the FT-ICR mass spectrometer is proportional to the scan duration of ions. Here, we present a novel isotopic ratio extrapolation (IRE) method for obtaining accurate isotopic ratio measurements. Accuracy is achieved by performing scans with different duration and extrapolation of the data to the initial moment of the ion rotation; IRE minimizes the absolute isotopic ratio error to ≤1 %. We demonstrate the application of IRE in protein turnover studies using
2
H
2
O-metabolic labeling. Overall, this technique allows accurate measurements of the isotopic ratios of proteolytic peptides, a critical step for enabling routine studies of proteome dynamics.</abstract><cop>New York</cop><pub>Springer-Verlag</pub><pmid>23283729</pmid><doi>10.1007/s13361-012-0536-2</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Albumins - analysis Albumins - chemistry Albumins - metabolism Analytical Chemistry Animals Application Note Bioinformatics Biotechnology Chemistry Chemistry and Materials Science Cyclotron resonance Deuterium - analysis Deuterium - metabolism Extrapolation Fourier transforms Ions Isotope Labeling - methods Isotopes Mass spectrometers Mass spectrometry Mass Spectrometry - methods Organic Chemistry Peptide Fragments - analysis Peptide Fragments - chemistry Peptide Fragments - metabolism Peptides Peptides - analysis Peptides - chemistry Peptides - metabolism Proteome - analysis Proteome - chemistry Proteome - metabolism Proteomics Rats Reproducibility of Results Spectrometers |
title | An Improved Measurement of Isotopic Ratios by High Resolution Mass Spectrometry |
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