High-Throughput Proteomics Using High-Efficiency Multiple-Capillary Liquid Chromatography with On-Line High-Performance ESI FTICR Mass Spectrometry
We report on the design and application of a high-efficiency multiple-capillary liquid chromatography (LC) system for high-throughput proteome analysis. The multiple-capillary LC system using commercial LC pumps was operated at a pressure of 10 000 psi to deliver mobile phases through a novel passiv...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2001-07, Vol.73 (13), p.3011-3021 |
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| container_title | Analytical chemistry (Washington) |
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| creator | Shen, Yufeng Tolić, Nikola Zhao, Rui Paša-Tolić, Ljiljana Li, Lingjun Berger, Scott J Harkewicz, Richard Anderson, Gordon A Belov, Mikhail E Smith, Richard D |
| description | We report on the design and application of a high-efficiency multiple-capillary liquid chromatography (LC) system for high-throughput proteome analysis. The multiple-capillary LC system using commercial LC pumps was operated at a pressure of 10 000 psi to deliver mobile phases through a novel passive feedback valve arrangement that permitted mobile-phase flow path switching and efficient sample introduction. The multiple-capillary LC system uses several serially connected dual-capillary column devices. The dual-capillary column approach eliminates the time delays for column regeneration (or equilibration) since one capillary column was used for a separation while the other was being washed. Several serially connected dual-capillary columns and electrospray ionization (ESI) sources were operated independently and can be used either for “backup” operation or for parallel operation with other mass spectrometers. This high-efficiency multiple-capillary LC system utilizes switching valves for all operations, enabling automated operation. The separation efficiency of the dual-capillary column arrangement, optimal capillary dimensions (column length and packed particle size), capillary regeneration conditions, and mobile-phase compositions and their compatibility with electrospray ionization were investigated. A high magnetic field (11.4 T) Fourier transform ion cyclotron resonance (FTICR) mass spectrometer was coupled on-line with this high-efficiency multiple-capillary LC system using an ESI interface. The capillary LC provided a peak capacity of ∼650, and the 2-D capillary LC−FTICR analysis provided a combined resolving power of >6 × 107 components. For yeast cytosolic tryptic digests >100 000 polypeptides were detected, and ∼1000 proteins could be characterized from a single capillary LC-FTICR analysis using the high mass measurement accuracy (∼1 ppm) of FTICR, and likely more if LC retention time information were also exploited for peptide identification. |
| doi_str_mv | 10.1021/ac001393n |
| format | Article |
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The multiple-capillary LC system using commercial LC pumps was operated at a pressure of 10 000 psi to deliver mobile phases through a novel passive feedback valve arrangement that permitted mobile-phase flow path switching and efficient sample introduction. The multiple-capillary LC system uses several serially connected dual-capillary column devices. The dual-capillary column approach eliminates the time delays for column regeneration (or equilibration) since one capillary column was used for a separation while the other was being washed. Several serially connected dual-capillary columns and electrospray ionization (ESI) sources were operated independently and can be used either for “backup” operation or for parallel operation with other mass spectrometers. This high-efficiency multiple-capillary LC system utilizes switching valves for all operations, enabling automated operation. The separation efficiency of the dual-capillary column arrangement, optimal capillary dimensions (column length and packed particle size), capillary regeneration conditions, and mobile-phase compositions and their compatibility with electrospray ionization were investigated. A high magnetic field (11.4 T) Fourier transform ion cyclotron resonance (FTICR) mass spectrometer was coupled on-line with this high-efficiency multiple-capillary LC system using an ESI interface. The capillary LC provided a peak capacity of ∼650, and the 2-D capillary LC−FTICR analysis provided a combined resolving power of >6 × 107 components. For yeast cytosolic tryptic digests >100 000 polypeptides were detected, and ∼1000 proteins could be characterized from a single capillary LC-FTICR analysis using the high mass measurement accuracy (∼1 ppm) of FTICR, and likely more if LC retention time information were also exploited for peptide identification.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac001393n</identifier><identifier>PMID: 11467548</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Chromatography ; Chromatography, Liquid - methods ; Fundamental and applied biological sciences. 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Chem</addtitle><description>We report on the design and application of a high-efficiency multiple-capillary liquid chromatography (LC) system for high-throughput proteome analysis. The multiple-capillary LC system using commercial LC pumps was operated at a pressure of 10 000 psi to deliver mobile phases through a novel passive feedback valve arrangement that permitted mobile-phase flow path switching and efficient sample introduction. The multiple-capillary LC system uses several serially connected dual-capillary column devices. The dual-capillary column approach eliminates the time delays for column regeneration (or equilibration) since one capillary column was used for a separation while the other was being washed. Several serially connected dual-capillary columns and electrospray ionization (ESI) sources were operated independently and can be used either for “backup” operation or for parallel operation with other mass spectrometers. This high-efficiency multiple-capillary LC system utilizes switching valves for all operations, enabling automated operation. The separation efficiency of the dual-capillary column arrangement, optimal capillary dimensions (column length and packed particle size), capillary regeneration conditions, and mobile-phase compositions and their compatibility with electrospray ionization were investigated. A high magnetic field (11.4 T) Fourier transform ion cyclotron resonance (FTICR) mass spectrometer was coupled on-line with this high-efficiency multiple-capillary LC system using an ESI interface. The capillary LC provided a peak capacity of ∼650, and the 2-D capillary LC−FTICR analysis provided a combined resolving power of >6 × 107 components. For yeast cytosolic tryptic digests >100 000 polypeptides were detected, and ∼1000 proteins could be characterized from a single capillary LC-FTICR analysis using the high mass measurement accuracy (∼1 ppm) of FTICR, and likely more if LC retention time information were also exploited for peptide identification.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chromatography</subject><subject>Chromatography, Liquid - methods</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>General aspects, investigation methods</subject><subject>Peptide Mapping</subject><subject>Proteins</subject><subject>Proteome</subject><subject>Reproducibility of Results</subject><subject>Saccharomyces cerevisiae - chemistry</subject><subject>Spectrometry, Mass, Electrospray Ionization - methods</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Spectrum analysis</subject><subject>Trypsin - chemistry</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpl0ctuEzEUBmALgWhaWPACyEKAxGLgeDy2J0sYpW1QSiOSComN5XHsxO3cas-o5Dl4YQwTtQhWXvg7v84FoRcE3hNIyQelAQid0uYRmhCWQsLzPH2MJgBAk1QAHKHjEK4jIkD4U3RESMYFy_IJ-nnutrtkvfPtsN11Q4-Xvu1NWzsd8FVwzRb_ATNrnXam0Xt8MVS96yqTFKpzVaX8Hi_c7eA2uIgpterbrVfdbo_vXL_Dl02ycI0ZU5bG29bXqtEGz1ZzfLqeF1_xhQoBrzqj-1huer9_hp5YVQXz_PCeoKvT2bo4TxaXZ_Pi4yJRGbA-EcqALQVnKittnpaszDgwQ6ylkCmhVAlMZMQworXelCxjKbeEm5RRmhK-oSfo7Zjb-fZ2MKGXtQvaxJka0w5BCgKU5FMa4at_4HU7-Cb2JlMick6BQ0TvRqR9G4I3Vnbe1XE9koD8fSZ5f6ZoXx4Ch7I2mwd5uEsErw9ABa0q6-POXPgrcUqBsMiSkbnQmx_338rfSC6oYHK9XMlPBf3y7ez7Z5lG_2b0SoeHGf7v7xcEAbWQ</recordid><startdate>20010701</startdate><enddate>20010701</enddate><creator>Shen, Yufeng</creator><creator>Tolić, Nikola</creator><creator>Zhao, Rui</creator><creator>Paša-Tolić, Ljiljana</creator><creator>Li, Lingjun</creator><creator>Berger, Scott J</creator><creator>Harkewicz, Richard</creator><creator>Anderson, Gordon A</creator><creator>Belov, Mikhail E</creator><creator>Smith, Richard D</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>20010701</creationdate><title>High-Throughput Proteomics Using High-Efficiency Multiple-Capillary Liquid Chromatography with On-Line High-Performance ESI FTICR Mass Spectrometry</title><author>Shen, Yufeng ; Tolić, Nikola ; Zhao, Rui ; Paša-Tolić, Ljiljana ; Li, Lingjun ; Berger, Scott J ; Harkewicz, Richard ; Anderson, Gordon A ; Belov, Mikhail E ; Smith, Richard D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a405t-7ae0fb765a4bf82b5b4605e1ff304a7aab05741e51cccdb54526f16e2533216d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chromatography</topic><topic>Chromatography, Liquid - methods</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>General aspects, investigation methods</topic><topic>Peptide Mapping</topic><topic>Proteins</topic><topic>Proteome</topic><topic>Reproducibility of Results</topic><topic>Saccharomyces cerevisiae - chemistry</topic><topic>Spectrometry, Mass, Electrospray Ionization - methods</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Spectrum analysis</topic><topic>Trypsin - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shen, Yufeng</creatorcontrib><creatorcontrib>Tolić, Nikola</creatorcontrib><creatorcontrib>Zhao, Rui</creatorcontrib><creatorcontrib>Paša-Tolić, Ljiljana</creatorcontrib><creatorcontrib>Li, Lingjun</creatorcontrib><creatorcontrib>Berger, Scott J</creatorcontrib><creatorcontrib>Harkewicz, Richard</creatorcontrib><creatorcontrib>Anderson, Gordon A</creatorcontrib><creatorcontrib>Belov, Mikhail E</creatorcontrib><creatorcontrib>Smith, Richard D</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>Shen, Yufeng</au><au>Tolić, Nikola</au><au>Zhao, Rui</au><au>Paša-Tolić, Ljiljana</au><au>Li, Lingjun</au><au>Berger, Scott J</au><au>Harkewicz, Richard</au><au>Anderson, Gordon A</au><au>Belov, Mikhail E</au><au>Smith, Richard D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High-Throughput Proteomics Using High-Efficiency Multiple-Capillary Liquid Chromatography with On-Line High-Performance ESI FTICR Mass Spectrometry</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2001-07-01</date><risdate>2001</risdate><volume>73</volume><issue>13</issue><spage>3011</spage><epage>3021</epage><pages>3011-3021</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>We report on the design and application of a high-efficiency multiple-capillary liquid chromatography (LC) system for high-throughput proteome analysis. The multiple-capillary LC system using commercial LC pumps was operated at a pressure of 10 000 psi to deliver mobile phases through a novel passive feedback valve arrangement that permitted mobile-phase flow path switching and efficient sample introduction. The multiple-capillary LC system uses several serially connected dual-capillary column devices. The dual-capillary column approach eliminates the time delays for column regeneration (or equilibration) since one capillary column was used for a separation while the other was being washed. Several serially connected dual-capillary columns and electrospray ionization (ESI) sources were operated independently and can be used either for “backup” operation or for parallel operation with other mass spectrometers. This high-efficiency multiple-capillary LC system utilizes switching valves for all operations, enabling automated operation. The separation efficiency of the dual-capillary column arrangement, optimal capillary dimensions (column length and packed particle size), capillary regeneration conditions, and mobile-phase compositions and their compatibility with electrospray ionization were investigated. A high magnetic field (11.4 T) Fourier transform ion cyclotron resonance (FTICR) mass spectrometer was coupled on-line with this high-efficiency multiple-capillary LC system using an ESI interface. The capillary LC provided a peak capacity of ∼650, and the 2-D capillary LC−FTICR analysis provided a combined resolving power of >6 × 107 components. For yeast cytosolic tryptic digests >100 000 polypeptides were detected, and ∼1000 proteins could be characterized from a single capillary LC-FTICR analysis using the high mass measurement accuracy (∼1 ppm) of FTICR, and likely more if LC retention time information were also exploited for peptide identification.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>11467548</pmid><doi>10.1021/ac001393n</doi><tpages>11</tpages></addata></record> |
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| source | ACS Publications; MEDLINE |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Chromatography Chromatography, Liquid - methods Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry General aspects, investigation methods Peptide Mapping Proteins Proteome Reproducibility of Results Saccharomyces cerevisiae - chemistry Spectrometry, Mass, Electrospray Ionization - methods Spectrophotometry, Ultraviolet Spectroscopy, Fourier Transform Infrared Spectrum analysis Trypsin - chemistry |
| title | High-Throughput Proteomics Using High-Efficiency Multiple-Capillary Liquid Chromatography with On-Line High-Performance ESI FTICR Mass Spectrometry |
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