METHODS OF IONIZATION IN MASS SPECTROSCOPY

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Methods for the analysis of protein structures are being improved, applied and tested in both independent and collaborative research projects. Chromatographic systems, both on-line and gel-based are being tested with for the primary structure determination of indoleamine-2,3- dioxygenase as a model glycoprotein. Collaborative studies on the identification of post-translational modifications or unique gene products are in progress. Methods are also being devised and tested to improve the detectability of trace organic compounds using mass spectrometry. The development of new derivatization reagents and methods to impart improved electron capture properties for negative ionization mass spectrometric detection has been continued and applied to the analysis of glutamate in cell cultures. Liquid-chromatography - electrospray mass spectrometry methods continue to be developed for the quantitative analyses of 13C-labeled NAD and NADP as products of 13C- tryptophan metabolism. Fully 13C and 15N labeled NAD has been isolated from yeast for use as an analytical standard. Hydrophilic interaction chromatography has been successfully used for improved separations of nucleosides and NAD. An interface for coupling capillary zone electrophoresis and electrospray mass spectrometry has been designed to enable enhanced detection of peptides and mixtures isolated from cell extracts and tissues. - liquid chromatography, mass spectrometry, electrospray, capillary electrophoresis, derivatization, MALDI/TOF, protein structure