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Results: 4

1.
Fig. 2.

Fig. 2. From: Enhanced Sensitivity for Selected Reaction Monitoring Mass Spectrometry-based Targeted Proteomics Using a Dual Stage Electrodynamic Ion Funnel Interface.

Average increase in SRM peak area for dual ion funnel configuration relative to Thermo interface for best transitions from nine peptides in S9 sample (see Table I). Error bars represent standard deviations of the measurements.

Mahmud Hossain, et al. Mol Cell Proteomics. 2011 February;10(2):M000062-MCP201.
2.
Fig. 4.

Fig. 4. From: Enhanced Sensitivity for Selected Reaction Monitoring Mass Spectrometry-based Targeted Proteomics Using a Dual Stage Electrodynamic Ion Funnel Interface.

Comparison of observed extracted ion chromatograms using dual ion funnel and standard Thermo interfaces for two intense transitions (m/z 728.842+ > 1099.51+ of peptide TGQAPGFSYTDANK (A) and m/z 482.772+ > 494.30+ of peptide EDLIAYLK (B)) from protein bovine cytochrome c. AA, peak area; 2F, dual ion funnel; Th, standard Thermo.

Mahmud Hossain, et al. Mol Cell Proteomics. 2011 February;10(2):M000062-MCP201.
3.
Fig. 1.

Fig. 1. From: Enhanced Sensitivity for Selected Reaction Monitoring Mass Spectrometry-based Targeted Proteomics Using a Dual Stage Electrodynamic Ion Funnel Interface.

Schematic of Thermo QqQ Quantum Ultra mass spectrometer equipped with dual ion funnel interface. The main features of this interface are the incorporation of a multicapillary inlet along with two consecutive ion funnels, one high pressure (∼17 torr) funnel and one low pressure (∼1 torr) funnel used in tandem.

Mahmud Hossain, et al. Mol Cell Proteomics. 2011 February;10(2):M000062-MCP201.
4.
Fig. 3.

Fig. 3. From: Enhanced Sensitivity for Selected Reaction Monitoring Mass Spectrometry-based Targeted Proteomics Using a Dual Stage Electrodynamic Ion Funnel Interface.

Plots of peak area versus concentration curves for each of five selected peptides in mouse plasma are constructed (peak area versus ng/ml protein concentration) with dual ion funnel (2F; upper three bold traces) interface and standard Thermo (Th; lower three narrow traces) configurations. Peptide VLDALDSIK is from protein bovine carbonic anhydrase, peptide VDEDQPFPAVPK is from E. coli β-galactosidase, peptide LFTGHPETLEK is from equine skeletal muscle myoglobin, peptide GGLEPINFQTAADQAR is from chicken ovalbumin, and peptide TGQAPGFSYTDANK is from bovine cytochrome c. Three transitions are monitored for each of the peptides. Error bars represent standard deviations of the measurements.

Mahmud Hossain, et al. Mol Cell Proteomics. 2011 February;10(2):M000062-MCP201.

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