Chapter title |
Peptide mass fingerprinting: protein identification using MALDI-TOF mass spectrometry.
|
---|---|
Chapter number | 16 |
Book title |
Chemical Genomics
|
Published in |
Methods in molecular biology, December 2005
|
DOI | 10.1007/978-1-59259-948-6_16 |
Pubmed ID | |
Book ISBNs |
978-1-58829-399-2, 978-1-59259-948-6
|
Authors |
Webster J, Oxley D, Judith Webster, David Oxley, Webster, Judith, Oxley, David |
Abstract |
Matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF)-mass spectrometry (MS) is now routinely used in many laboratories for the rapid and sensitive identification of proteins by peptide mass fingerprinting (PMF). We describe a simple protocol that can be performed in a standard biochemistry laboratory, whereby proteins separated by one- or two-dimensional gel electrophoresis can be identified at femtomole levels. The procedure involves excision of the spot or band from the gel, washing and de-staining, reduction and alkylation, in-gel trypsin digestion, MALDI-TOF MS of the tryptic peptides, and database searching of the PMF data. Up to 96 protein samples can easily be manually processed at one time by this method. |
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