Journal
RAPID COMMUNICATIONS IN MASS SPECTROMETRY
Volume 24, Issue 1, Pages 11-14Publisher
WILEY
DOI: 10.1002/rcm.4349
Keywords
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Funding
- Defense Threat Reduction Agency [W81XWH-07-C-0061]
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Bacteriophage (phage) proteins have been analyzed previously with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). However, analysis of phage major capsid proteins (MCPs) has been limited by the ability to reproducibly generate ions from MCP monomers. While the acidic conditions of MALDI-TOF MS sample preparation have been shown to aid in disassembly of some phage capsids, many require further treatment to successfully liberate MCP monomers. The findings presented here suggest that beta-mercaptoethanol reduction of the disulfide bonds linking phage MCPs prior to mass spectrometric analysis results in significantly increased MALDI-TOF MS sensitivity and reproducibility of Yersinia pestis-specific phage protein profiles. Copyright (C) 2009 John Wiley & Sons, Ltd.
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