Nine peptides, some of which were overlapped, were identified through mass spectrometry shotgun analysis.
Aliquots were subjected to mass spectrometry shotgun analysis after pooling of several consecutive fractions (protein concentration estimated by UV trace).
The approximate 20 kDa to 30 kDa band was incised, digested by trypsin, and identified by mass spectrometry shotgun analysis as described previously [46].
Aliquots of 200 μl of each fraction, corresponding to approximately 20 μg of protein, were separated for mass-spectrometry shotgun analysis.
Using a mass-spectrometry, shotgun-proteomics approach combined with a novel "sandwich-dissociation" method, more than 600 proteins from isolated stria vascularis capillaries were identified from adult CBA/CaJ mouse cochlea.
Since mass spectrometry-based shotgun proteomics approaches provide large-scale peptide sequencing data with high throughput, a data repository for shotgun proteogenomics would represent a valuable source of gene expression evidence at the translational level for genome re-annotation.
Shotgun mass spectra were used to identify proteins in salivary exosomes from patients with IBD (UC and CD groups).
Exosomal proteins were extracted from the saliva of patients and healthy controls for shotgun mass spectroscopy analyses.
2-Dimensional Electrophoresis (2-DE) separation combined with Mass Spectrometry and Shotgun Proteomics experiments have been employed to design a thorough picture of protein profile.
A shotgun mass spectroscopy approach enables thousands of proteins to be identified at once; its efficiency and sensitivity render it a powerful technique in protein research (Dowell et al., 2008).
