| Chapter title |
Peptide Imaging: Maximizing Peptide Yield, Optimization of the “Peptide Mass Fingerprint”
|
|---|---|
| Chapter number | 8 |
| Book title |
Imaging Mass Spectrometry
|
| Published in |
Methods in molecular biology, May 2017
|
| DOI | 10.1007/978-1-4939-7051-3_8 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-7050-6, 978-1-4939-7051-3
|
| Authors |
Ekta Patel, Patel, Ekta |
| Editors |
Laura M. Cole |
| Abstract |
In Matrix Assisted Laser Desorption Ionization Mass Spectrometry Imaging (MALDI-MSI), identification of observed proteins remains a challenge primarily due to the drop in sensitivity of time-of-flight (TOF) mass spectrometers beyond the mass range of 25-35 kDa (Francese et al. High Throughput Screen 12: 156-174, 2009) and inadequate mass resolving power at those molecular weights. To counteract this, a bottom-up proteomic approach is often employed. Proteolysis digests proteins into smaller peptide fragments, typically between 500 and 3000 Da which are easier to detect with a higher mass accuracy. Here, we describe the addition of a MS-compatible detergent to the endopeptidase trypsin, to enhance in situ proteolysis efficiency and peptide intensity. |
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