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One µl (1 µl) aliquots of the supernatant were used for mass analysis using the dried droplet technique and α-cyano-4-hydroxycinnamic acid as matrix.
Mass analysis using electrospray ionization mass spectrometry (QTOF-II Hybrid-mass spectrometer; Micromass) yielded a mass of 14,546 Da, which exactly corresponds to the mass of natural RNase 7 [25].
An accurate mass can be detected by intact mass analysis using LC-MS.
An accurate mass can be detected by intact mass analysis using liquid chromatography-mass spectrometry (LC-MS).
This conjecture was confirmed when equine haemoglobin was modified with the pyrrole under reducing and denaturing conditions and a small amount of β-chain adduction was detected by intact mass analysis using ESI-MS.
Both the N- and the C-terminal regions of BCNT were routinely confirmed by mass analysis using Asp-N (endoproteinase which selectively cleaves peptide bonds N-terminal to aspartic acid and glutamic acid residues) digests to identify m/z=MHHHHHHAIAMEEF (m/z=1763.6) or MHHHHHHAIAM (m/z=1358.5) and DLRLSKMKP (m/z=1087.6).
Similar(53)
Two bands migrating at the same positions as on the Western blot analysis were taken for the mass spectrometry analysis using LTQ Velos Orbitrap mass spectrometer (Thermo Fisher Scientific).
All compounds were confirmed by mass spectrometry analysis using a VG Autospec mass spectrometer with electron spray ionisation (ES) at 70 eV.
An overnight digestion with trypsin (Promega, Madison, Wisconsin, USA) was performed and resulting peptides were extracted and prepared for mass spectrometry analysis using an Orbitrap Velos mass spectrometer as described elsewhere [ 48].
10 Protein extracts were analysed by acid urea-polyacrylamide gel electrophoresis (AU-PAGE) followed by mass spectrometric analysis using matrix assisted laser desorption ionisation-time of flight tandem mass spectrometry (MALDI-TOF/TOF MS).
Digested and dried samples were subjected to peptide mass fingerprinting analysis using the Georgia Institute of Technology Bioanalytical Mass Spectrometry Facility.
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