Accurate mass measurements using MALDI-TOF with delayed extraction
Matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry is now an essential tool in biopolymer analysis. Sensitivity and mass range are unsurpassed, but mass measurement accuracy and resolution have been limited. With delayed extraction and a reflecting analyzer, mas...
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| Veröffentlicht in: | Journal of Protein Chemistry 1997-07, Vol.16 (5), p.363-369 |
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| container_title | Journal of Protein Chemistry |
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| creator | Takach, E J Hines, W M Patterson, D H Juhasz, P Falick, A M Vestal, M L Martin, S A |
| description | Matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry is now an essential tool in biopolymer analysis. Sensitivity and mass range are unsurpassed, but mass measurement accuracy and resolution have been limited. With delayed extraction and a reflecting analyzer, mass measurements using MALDI-TOF can be made with an accuracy of a few parts per million (ppm). It is possible to distinguish Lys from Gln in peptides, and to determine the elemental composition of smaller molecules (mass 100-500). In database searching strategies, a smaller mass window, resulting from an increase in mass accuracy, greatly decreases the number of possible candidates. Mass measurement accuracy with errors less than 5 ppm is demonstrated on a mixture of 12 peptides ranging in mass from ca. 900 to 3700 Da. Mass measurements on 13 peaks in an unseparated tryptic digest of myoglobin gave results with an overall average error less than 3.5 ppm, with a maximum error of 7 ppm. |
| doi_str_mv | 10.1023/A:1026376403468 |
| format | Article |
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Sensitivity and mass range are unsurpassed, but mass measurement accuracy and resolution have been limited. With delayed extraction and a reflecting analyzer, mass measurements using MALDI-TOF can be made with an accuracy of a few parts per million (ppm). It is possible to distinguish Lys from Gln in peptides, and to determine the elemental composition of smaller molecules (mass 100-500). In database searching strategies, a smaller mass window, resulting from an increase in mass accuracy, greatly decreases the number of possible candidates. Mass measurement accuracy with errors less than 5 ppm is demonstrated on a mixture of 12 peptides ranging in mass from ca. 900 to 3700 Da. Mass measurements on 13 peaks in an unseparated tryptic digest of myoglobin gave results with an overall average error less than 3.5 ppm, with a maximum error of 7 ppm.</description><identifier>ISSN: 0277-8033</identifier><identifier>ISSN: 1572-3887</identifier><identifier>EISSN: 1573-4943</identifier><identifier>DOI: 10.1023/A:1026376403468</identifier><identifier>PMID: 9246615</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>Accuracy ; Adrenocorticotropic Hormone - analysis ; Amino Acid Sequence ; Animals ; Apoproteins - analysis ; Biopolymers ; Bradykinin - analogs & derivatives ; Bradykinin - analysis ; Chemical composition ; Corticotropin-Like Intermediate Lobe Peptide ; Database searching ; Fibrinopeptide A - analysis ; Horses ; Ionization ; Ions ; Mass spectrometry ; Mass spectroscopy ; Molecular Sequence Data ; Molecular Weight ; Myoglobin - analysis ; Myoglobins ; Oligopeptides - analysis ; Peptide Fragments - analysis ; Peptides ; Polymers ; Proteins ; Proteins - analysis ; Reference Standards ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><ispartof>Journal of Protein Chemistry, 1997-07, Vol.16 (5), p.363-369</ispartof><rights>Plenum Publishing Corporation 1997.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-d675b0810c8205ded2585d9924dc7fd80aa32784cb59a1afa4ddde6912c4daf43</citedby><cites>FETCH-LOGICAL-c389t-d675b0810c8205ded2585d9924dc7fd80aa32784cb59a1afa4ddde6912c4daf43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9246615$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takach, E J</creatorcontrib><creatorcontrib>Hines, W M</creatorcontrib><creatorcontrib>Patterson, D H</creatorcontrib><creatorcontrib>Juhasz, P</creatorcontrib><creatorcontrib>Falick, A M</creatorcontrib><creatorcontrib>Vestal, M L</creatorcontrib><creatorcontrib>Martin, S A</creatorcontrib><title>Accurate mass measurements using MALDI-TOF with delayed extraction</title><title>Journal of Protein Chemistry</title><addtitle>J Protein Chem</addtitle><description>Matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry is now an essential tool in biopolymer analysis. Sensitivity and mass range are unsurpassed, but mass measurement accuracy and resolution have been limited. With delayed extraction and a reflecting analyzer, mass measurements using MALDI-TOF can be made with an accuracy of a few parts per million (ppm). It is possible to distinguish Lys from Gln in peptides, and to determine the elemental composition of smaller molecules (mass 100-500). In database searching strategies, a smaller mass window, resulting from an increase in mass accuracy, greatly decreases the number of possible candidates. Mass measurement accuracy with errors less than 5 ppm is demonstrated on a mixture of 12 peptides ranging in mass from ca. 900 to 3700 Da. Mass measurements on 13 peaks in an unseparated tryptic digest of myoglobin gave results with an overall average error less than 3.5 ppm, with a maximum error of 7 ppm.</description><subject>Accuracy</subject><subject>Adrenocorticotropic Hormone - analysis</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoproteins - analysis</subject><subject>Biopolymers</subject><subject>Bradykinin - analogs & derivatives</subject><subject>Bradykinin - analysis</subject><subject>Chemical composition</subject><subject>Corticotropin-Like Intermediate Lobe Peptide</subject><subject>Database searching</subject><subject>Fibrinopeptide A - analysis</subject><subject>Horses</subject><subject>Ionization</subject><subject>Ions</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Myoglobin - analysis</subject><subject>Myoglobins</subject><subject>Oligopeptides - analysis</subject><subject>Peptide Fragments - analysis</subject><subject>Peptides</subject><subject>Polymers</subject><subject>Proteins</subject><subject>Proteins - analysis</subject><subject>Reference Standards</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><issn>0277-8033</issn><issn>1572-3887</issn><issn>1573-4943</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkD1PwzAYhC0EKqUwMyFFDGyB11-xzRYKhUpFXcpsubYDqZqk2Img_55UrZBguuW5R6dD6BLDLQZC7_L7PjIqMgaUZfIIDTEXNGWK0WM0BCJEKoHSU3QW4woAlJQwQANFWJZhPkQPubVdMK1PKhNjUnkTu-ArX7cx6WJZvyev-exxmi7mk-SrbD8S59dm613iv9tgbFs29Tk6Kcw6-otDjtDb5Gkxfkln8-fpOJ-llkrVpi4TfAkSg5UEuPOOcMmd6pc4KwonwRhKhGR2yZXBpjDMOeczhYllzhSMjtDN3rsJzWfnY6urMlq_XpvaN13UQmHBCKY9eP0PXDVdqPttWmWUMwCys93tIRuaGIMv9CaUlQlbjUHvrtW5_nNt37g6aLtl5d0vf_iS_gDrqHJV</recordid><startdate>19970701</startdate><enddate>19970701</enddate><creator>Takach, E J</creator><creator>Hines, W M</creator><creator>Patterson, D H</creator><creator>Juhasz, P</creator><creator>Falick, A M</creator><creator>Vestal, M L</creator><creator>Martin, S A</creator><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>7QL</scope><scope>7TK</scope><scope>7TM</scope><scope>7U7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19970701</creationdate><title>Accurate mass measurements using MALDI-TOF with delayed extraction</title><author>Takach, E J ; Hines, W M ; Patterson, D H ; Juhasz, P ; Falick, A M ; Vestal, M L ; Martin, S A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-d675b0810c8205ded2585d9924dc7fd80aa32784cb59a1afa4ddde6912c4daf43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Accuracy</topic><topic>Adrenocorticotropic Hormone - analysis</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoproteins - analysis</topic><topic>Biopolymers</topic><topic>Bradykinin - analogs & derivatives</topic><topic>Bradykinin - analysis</topic><topic>Chemical composition</topic><topic>Corticotropin-Like Intermediate Lobe Peptide</topic><topic>Database searching</topic><topic>Fibrinopeptide A - analysis</topic><topic>Horses</topic><topic>Ionization</topic><topic>Ions</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Myoglobin - analysis</topic><topic>Myoglobins</topic><topic>Oligopeptides - analysis</topic><topic>Peptide Fragments - analysis</topic><topic>Peptides</topic><topic>Polymers</topic><topic>Proteins</topic><topic>Proteins - analysis</topic><topic>Reference Standards</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takach, E J</creatorcontrib><creatorcontrib>Hines, W M</creatorcontrib><creatorcontrib>Patterson, D H</creatorcontrib><creatorcontrib>Juhasz, P</creatorcontrib><creatorcontrib>Falick, A M</creatorcontrib><creatorcontrib>Vestal, M L</creatorcontrib><creatorcontrib>Martin, S A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of Protein Chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takach, E J</au><au>Hines, W M</au><au>Patterson, D H</au><au>Juhasz, P</au><au>Falick, A M</au><au>Vestal, M L</au><au>Martin, S A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Accurate mass measurements using MALDI-TOF with delayed extraction</atitle><jtitle>Journal of Protein Chemistry</jtitle><addtitle>J Protein Chem</addtitle><date>1997-07-01</date><risdate>1997</risdate><volume>16</volume><issue>5</issue><spage>363</spage><epage>369</epage><pages>363-369</pages><issn>0277-8033</issn><issn>1572-3887</issn><eissn>1573-4943</eissn><abstract>Matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry is now an essential tool in biopolymer analysis. Sensitivity and mass range are unsurpassed, but mass measurement accuracy and resolution have been limited. With delayed extraction and a reflecting analyzer, mass measurements using MALDI-TOF can be made with an accuracy of a few parts per million (ppm). It is possible to distinguish Lys from Gln in peptides, and to determine the elemental composition of smaller molecules (mass 100-500). In database searching strategies, a smaller mass window, resulting from an increase in mass accuracy, greatly decreases the number of possible candidates. Mass measurement accuracy with errors less than 5 ppm is demonstrated on a mixture of 12 peptides ranging in mass from ca. 900 to 3700 Da. Mass measurements on 13 peaks in an unseparated tryptic digest of myoglobin gave results with an overall average error less than 3.5 ppm, with a maximum error of 7 ppm.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>9246615</pmid><doi>10.1023/A:1026376403468</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0277-8033 |
| ispartof | Journal of Protein Chemistry, 1997-07, Vol.16 (5), p.363-369 |
| issn | 0277-8033 1572-3887 1573-4943 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals - AutoHoldings |
| subjects | Accuracy Adrenocorticotropic Hormone - analysis Amino Acid Sequence Animals Apoproteins - analysis Biopolymers Bradykinin - analogs & derivatives Bradykinin - analysis Chemical composition Corticotropin-Like Intermediate Lobe Peptide Database searching Fibrinopeptide A - analysis Horses Ionization Ions Mass spectrometry Mass spectroscopy Molecular Sequence Data Molecular Weight Myoglobin - analysis Myoglobins Oligopeptides - analysis Peptide Fragments - analysis Peptides Polymers Proteins Proteins - analysis Reference Standards Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods |
| title | Accurate mass measurements using MALDI-TOF with delayed extraction |
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