Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry
- 21 November 2000
- journal article
- research article
- Published by Wiley in Rapid Communications in Mass Spectrometry
- Vol. 14 (23) , 2147-2153
- https://doi.org/10.1002/1097-0231(20001215)14:23<2147::aid-rcm145>3.0.co;2-m
Abstract
Tryptic digests of three proteins are reacted with O‐methylisourea in order to convert lysine residues to homoarginines. The resulting homoarginine‐terminated peptides exhibit more intense MALDI mass spectral peaks than their lysine‐terminated predecessors. This simple chemical reaction should therefore facilitate protein sequencing and mass mapping. Copyright © 2000 John Wiley & Sons, Ltd.Keywords
This publication has 15 references indexed in Scilit:
- Probability-based protein identification by searching sequence databases using mass spectrometry dataElectrophoresis, 1999
- The Dominance of Arginine-Containing Peptides in MALDI-Derived Tryptic Mass Fingerprints of ProteinsAnalytical Chemistry, 1999
- Proteomics and automationElectrophoresis, 1999
- Protein Identification at the Low Femtomole Level from Silver-Stained Gels Using a New Fritless Electrospray Interface for Liquid Chromatography–Microspray and Nanospray Mass SpectrometryAnalytical Biochemistry, 1998
- Mass SpectrometryAnalytical Chemistry, 1998
- C-Terminal Sequence Analysis of Peptides and Proteins Using Carboxypeptidases and Mass Spectrometry after Derivatization of Lys and Cys ResiduesAnalytical Chemistry, 1997
- Derivatization to enhance sequence-specific fragmentation of peptides and proteinsInternational Journal of Mass Spectrometry and Ion Processes, 1993
- Rapid identification of proteins by peptide-mass fingerprintingCurrent Biology, 1993
- [70] Guanidination of proteinsPublished by Elsevier ,1967
- Preparation and Properties of Serum and Plasma Proteins. XXII. A Crystallizable Guanidinated Derivative of Human Serum AlbuminJournal of the American Chemical Society, 1949