## Matrix -assisted laser desorption/ionization time-of-flight mass spectrometry was used to rapidly detect and profile large proteins from Escherichia coli whole cell lysates in the mass range 25-500 kDa. The bacterial samples were treated with guanidine hydrochloride and Triton X-100 to disrupt a
Nonacid cleavable detergents applied to MALDI mass spectrometry profiling of whole cells
✍ Scribed by Jeremy L. Norris; Matthew J. Hangauer; Ned A. Porter; Richard M. Caprioli
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 328 KB
- Volume
- 40
- Category
- Article
- ISSN
- 1076-5174
- DOI
- 10.1002/jms.914
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✦ Synopsis
Abstract
Although cleavable detergents were first synthesized a number of years ago, they have only recently been successfully applied to problems involving biological molecules. Recent reports have demonstrated that these compounds are useful for applications involving both 2D PAGE and mass spectrometry. However, most cleavable surfactants have utilized acid‐labile functional groups to affect cleavage. In applications where extreme pH is required, acid cleavable detergents have limited usefulness. We report the synthesis of fluoride cleavable silane compounds and photolabile cinnamate esters as cleavable detergents having alternative cleavage chemistries than previously reported cleavable detergents. These compounds were applied to whole cell analysis using MALDI mass spectrometry, and it was demonstrated that their use results in an increase in the number of proteins analyzed by increasing protein solubility. Copyright © 2005 John Wiley & Sons, Ltd.
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