Figures on the top left shows the velocity calibration spectra in 298K (Room Temperature) and 78K (usually using a 99.85% in purity α-Fe foil with a thickness of 8 μm at room temperature or a Fe powder). The isomer shift (δ) value of the α-Fe foil relative to the 57Co/Rh source at Room Temperature found to be -0.110 mm/s, consistent with the source manufactured specifications (chemical shift of the source relative to α-Fe is 0.108 mm/s).
Figures on the top right shows measurements on custom-made holders for samples were fabricated though the thermo-forming method using copper molds and polypropylene (PP) sheets of 0.75 mm in thickness. Cylindrical holders of different size in diameter (10 mm and 7 mm) used, to better fit the corresponding sample volume within the holder.
Proofreading: Dr. Petousis
Calibration Measurements in 298K and 78K Testing different materials for sample holders
Figures on the bottom left show the MS spectra at 78K of the blood samples for the normal (a) and the thalassaemic (b) mice, respectively. The spectrum of the normal sample with a signal-to-noise ratio (S/N) of 23 was fitted with two quadrupole doublets, representing the α- and β-chains of oxy-haemoglobin.
Figures on the bottom right shows the MS spectra at 78K of the spleen samples from the normal (a) and thalassaemic (b) mice, respectively. The spectrum of the normal sample (Fig.a, S/N=27) was fitted with a single symmetrical doublet.
Normal (a) and Thalassaemic (b) Normal (a) and Thalassaemic (b)
Lab mice Blood spectra Lab mice spleen spectra