Mass spectrometry: analytical capabilities and potentials.
The mass range of mass spectrometers has been extended by almost an order of magnitude in the past decade, ionization procedures have been introduced which allow ionic, nonvolatile compounds to be examined, and new capabilities have been achieved through the successful integration of separation and analysis techniques. In combination with other techniques, mass spectrometry has been used in biological and environmental research to characterize constituents of mixtures, including those present in trace amounts; in metabolic profiling, where high throughput and large dynamic range are important; and in protein structure determinations. Measurements of stable isotope abundances by mass spectrometry have been used in enzymology, studies of photosynthesis, and carbon dating. Outside the area of chemical analysis, mass spectrometry has been used to study gas-phase acidities and basicities and to study organic reaction mechanisms in the gas phase. Trends in mass spectrometry include multidimensional experiments, use of ionization methods, direct analysis without extensive sample preparation, and the development of advanced instrumentation including an ion trap and an inductively coupled plasma mass spectrometer. It is likely that mass spectrometry will come to be much more widely used and that data will increasingly be other than conventional mass spectra.
D005583:Fourier Analysis; D008401:Gas Chromatography-Mass Spectrometry / Q000379:methods; D006441:Hemoglobin A / Q000032:analysis; D006451:Hemoglobin, Sickle / Q000032:analysis; D013058:Mass Spectrometry / Q000379:methods*; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis*
D006451:Hemoglobin, Sickle; D010455:Peptides; D006441:Hemoglobin A