Identification of proteins separated by one-dimensional sodium dodecyl sulfate/polyacrylamide gel electrophoresis with matrix-assisted laser desorption/ionization ion trap mass spectrometry; comparison with matrix-assisted laser desorption/ionization time-of-flight mass fingerprinting
Digests from ten gel bands containing low abundance proteins were analyzed by both matrix‐assisted laser desorption/ionization ion trap (MALDI‐IT) and matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOF) mass spectrometry (MS) methods. MALDI‐TOF techniques were able to identify onl...
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| Veröffentlicht in: | Rapid communications in mass spectrometry 2003-01, Vol.17 (17), p.1995-2004 |
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| container_end_page | 2004 |
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| container_issue | 17 |
| container_start_page | 1995 |
| container_title | Rapid communications in mass spectrometry |
| container_volume | 17 |
| creator | Zeng, Rong Chen, Yong-Bing Shao, Xiao-Xia Shieh, Chia-Hui Paul Miller, Ken Tran, Helen Xia, Qi-Chang |
| description | Digests from ten gel bands containing low abundance proteins were analyzed by both matrix‐assisted laser desorption/ionization ion trap (MALDI‐IT) and matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOF) mass spectrometry (MS) methods. MALDI‐TOF techniques were able to identify only one protein from all 10 gel bands, while MALDI‐IT identified eight proteins from the same 10 bands. The ability to perform MS/MS experiments with a MALDI‐IT instrument leads to protein identifications based on both peptide molecular mass and sequence information, and is much less prone to errors and uncertainties introduced by peptide fingerprinting methodologies in which protein identification is based on peptide molecular masses alone. Copyright © 2003 John Wiley & Sons, Ltd. |
| doi_str_mv | 10.1002/rcm.1143 |
| format | Article |
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Mass Spectrom</addtitle><date>2003-01-01</date><risdate>2003</risdate><volume>17</volume><issue>17</issue><spage>1995</spage><epage>2004</epage><pages>1995-2004</pages><issn>0951-4198</issn><eissn>1097-0231</eissn><abstract>Digests from ten gel bands containing low abundance proteins were analyzed by both matrix‐assisted laser desorption/ionization ion trap (MALDI‐IT) and matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOF) mass spectrometry (MS) methods. MALDI‐TOF techniques were able to identify only one protein from all 10 gel bands, while MALDI‐IT identified eight proteins from the same 10 bands. The ability to perform MS/MS experiments with a MALDI‐IT instrument leads to protein identifications based on both peptide molecular mass and sequence information, and is much less prone to errors and uncertainties introduced by peptide fingerprinting methodologies in which protein identification is based on peptide molecular masses alone. Copyright © 2003 John Wiley & Sons, Ltd.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12913863</pmid><doi>10.1002/rcm.1143</doi><tpages>10</tpages></addata></record> |
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| ispartof | Rapid communications in mass spectrometry, 2003-01, Vol.17 (17), p.1995-2004 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Amino Acid Sequence Electrophoresis, Polyacrylamide Gel Hydrolysis Molecular Sequence Data Peptide Mapping Precipitin Tests Proteins - chemistry Proteins - isolation & purification Software Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Yeasts - chemistry |
| title | Identification of proteins separated by one-dimensional sodium dodecyl sulfate/polyacrylamide gel electrophoresis with matrix-assisted laser desorption/ionization ion trap mass spectrometry; comparison with matrix-assisted laser desorption/ionization time-of-flight mass fingerprinting |
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