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Any ambiguities by capillary sequencing were clarified by mass spectroscopic validation [ 6].
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This factor is identified as the lead protein in the SCS of NPCs by tandem mass spectroscopic profiling, and further validated by western blotting and immunocytochemistry [ 131].
Potent fractions were chosen for further identifications using the chromatographic and spectroscopic methods as follows: a- Mass spectroscopic (MS) analyses of potent fractions The biologically potent fractions of E. crassipes were analyzed by Mass spectra (MS).
In other projects computers were used to analyze the massive data sets generated by mass spectroscopic or even tandem (multiple and simultaneous) mass spectroscopic analyses of proteins or small metabolites in biological samples.
Figure 4 shows the result of the mass spectroscopic analysis.
Mass spectroscopic analysis indicated the protein to be 17.5 kDa, which equalled the theoretically expected mass.
Mass spectroscopic analysis of those clusters was carried out to investigate the component of the structures.
The structures of these hybrids have been confirmed by NMR and mass spectroscopic data.
All the sensitizers have been characterized by NMR, mass spectroscopic and IR techniques.
Mass spectroscopic analysis indicated the protein to be of 16.6 kDa which equals the theoretically expected mass.
All the curcucminoids were characterized with the detailed 1H NMR, IR, UV Vis, and mass spectroscopic techniques.
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