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Protein identification methods in proteomics

2000; Wiley; Volume: 21; Issue: 6 Linguagem: Inglês

10.1002/(sici)1522-2683(20000401)21

1522-2683

Kris Gevaert, Joël Vandekerckhove,

Metabolomics and Mass Spectrometry Studies

ELECTROPHORESISVolume 21, Issue 6 p. 1145-1154 Review Protein identification methods in proteomics Kris Gevaert, Kris Gevaert Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Belgium Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, BelgiumSearch for more papers by this authorJoël Vandekerckhove, Corresponding Author Joël Vandekerckhove joel.vandekerckhove@rug.ac.be Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Belgium Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, BelgiumDepartment of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, K.L. Ledeganckstraat 35, B-9000 Ghent, Belgium, Fax: +32-92645337===Search for more papers by this author Kris Gevaert, Kris Gevaert Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Belgium Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, BelgiumSearch for more papers by this authorJoël Vandekerckhove, Corresponding Author Joël Vandekerckhove joel.vandekerckhove@rug.ac.be Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Belgium Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, BelgiumDepartment of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, K.L. Ledeganckstraat 35, B-9000 Ghent, Belgium, Fax: +32-92645337===Search for more papers by this author First published: 17 April 2000 https://doi.org/10.1002/(SICI)1522-2683(20000401)21:6 3.0.CO;2-ZCitations: 239AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract A combination of high-resolution two-dimensional (2-D) polyacrylamide gel electrophoresis, highly sensitive biological mass spectrometry, and the rapidly growing protein and DNA databases has paved the way for high-throughput proteomics. This review concentrates on protein identification. We first discuss the use of protein electroblotting and Edman sequencing as tools for de novo sequencing and protein identification. In the second part, we highlight matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) as one of the main contemporary analytical methods for linking gel-separated proteins to entries in sequence databases. In this context we describe the two main MALDI-MS-based identification methods: (i) peptide mass fingerprinting, and (ii) post-source decay (PSD) analysis. In the last part, we briefly emphasize the importance of sample preparation for obtaining highly sensitive and high-quality MALDI-MS spectra. Citing Literature Volume21, Issue61 April 2000Pages 1145-1154 RelatedInformation