ac5b01151_si_002.pdf (1.13 MB)
Liquid Extraction Surface Analysis Mass Spectrometry Coupled with Field Asymmetric Waveform Ion Mobility Spectrometry for Analysis of Intact Proteins from Biological Substrates
journal contribution
posted on 2015-12-17, 08:36 authored by Joscelyn Sarsby, Rian L. Griffiths, Alan M. Race, Josephine Bunch, Elizabeth C. Randall, Andrew J. Creese, Helen J. CooperPreviously we have shown that liquid
extraction surface analysis
(LESA) mass spectrometry is suitable for the analysis of intact proteins
from a range of biological substrates. Here we show that LESA mass
spectrometry may be coupled with high field asymmetric waveform ion
mobility spectrometry (FAIMS) for top-down protein analysis directly
from thin tissue sections (mouse liver, mouse brain) and from bacterial
colonies (Escherichia coli) growing
on agar. Incorporation of FAIMS results in significant improvements
in signal-to-noise and reduced analysis time. Abundant protein signals
are observed in single scan mass spectra. In addition, FAIMS enables
gas-phase separation of molecular classes, for example, lipids and
proteins, enabling improved analysis of both sets of species from
a single LESA extraction.
History
Usage metrics
Categories
Keywords
FAIMS resultsanalysis timemouse liverextraction surface analysismass spectrometryField Asymmetric Waveform Ion Mobility Spectrometrywaveform ion mobility spectrometryscan mass spectraIntact ProteinsLESA extractionmouse brainLESA mass spectrometryBiological SubstratesPreviouslytissue sectionsLiquid Extraction Surface Analysis Mass SpectrometryEscherichia coliAbundant protein signals
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC