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Proteome Profiling—Pitfalls and Progress
In this review we examine the current state of analytical methods in proteomics. The conventional methodology using two-dimensional electrophoresis gels and mass spectrometry is discussed, with particular reference to the advantages and shortcomings thereof. Two recently published methods which offe...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2000
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2448324/ https://www.ncbi.nlm.nih.gov/pubmed/10900454 http://dx.doi.org/10.1002/1097-0061(20000630)17:2<81::AID-YEA22>3.0.CO;2-Z |
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author | Haynes, Paul A. Yates III, John R. |
author_facet | Haynes, Paul A. Yates III, John R. |
author_sort | Haynes, Paul A. |
collection | PubMed |
description | In this review we examine the current state of analytical methods in proteomics. The conventional methodology using two-dimensional electrophoresis gels and mass spectrometry is discussed, with particular reference to the advantages and shortcomings thereof. Two recently published methods which offer an alternative approach are presented and discussed, with emphasis on how they can provide information not available via two-dimensional gel electrophoresis. These two methods are the isotope-coded affinity tags approach of Gygi et al. and the two-dimensional liquid chromatography–tandem mass spectrometry approach as presented by Link et al. We conclude that both of these new techniques represent significant advances in analytical methodology for proteome analysis. Furthermore, we believe that in the future biological research will continue to be enhanced by the continuation of such developments in proteomic analytical technology. |
format | Text |
id | pubmed-2448324 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-24483242008-07-14 Proteome Profiling—Pitfalls and Progress Haynes, Paul A. Yates III, John R. Yeast Research Article In this review we examine the current state of analytical methods in proteomics. The conventional methodology using two-dimensional electrophoresis gels and mass spectrometry is discussed, with particular reference to the advantages and shortcomings thereof. Two recently published methods which offer an alternative approach are presented and discussed, with emphasis on how they can provide information not available via two-dimensional gel electrophoresis. These two methods are the isotope-coded affinity tags approach of Gygi et al. and the two-dimensional liquid chromatography–tandem mass spectrometry approach as presented by Link et al. We conclude that both of these new techniques represent significant advances in analytical methodology for proteome analysis. Furthermore, we believe that in the future biological research will continue to be enhanced by the continuation of such developments in proteomic analytical technology. Hindawi Publishing Corporation 2000 /pmc/articles/PMC2448324/ /pubmed/10900454 http://dx.doi.org/10.1002/1097-0061(20000630)17:2<81::AID-YEA22>3.0.CO;2-Z Text en Copyright © 2000 Hindawi Publishing Corporation. http://creativecommons.org/licenses/by/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Haynes, Paul A. Yates III, John R. Proteome Profiling—Pitfalls and Progress |
title | Proteome Profiling—Pitfalls and Progress |
title_full | Proteome Profiling—Pitfalls and Progress |
title_fullStr | Proteome Profiling—Pitfalls and Progress |
title_full_unstemmed | Proteome Profiling—Pitfalls and Progress |
title_short | Proteome Profiling—Pitfalls and Progress |
title_sort | proteome profiling—pitfalls and progress |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2448324/ https://www.ncbi.nlm.nih.gov/pubmed/10900454 http://dx.doi.org/10.1002/1097-0061(20000630)17:2<81::AID-YEA22>3.0.CO;2-Z |
work_keys_str_mv | AT haynespaula proteomeprofilingpitfallsandprogress AT yatesiiijohnr proteomeprofilingpitfallsandprogress |