Development of a novel electron-transfer secondary reaction matrix, characterization of the site–specificity of novel bilin-lyase, and Fundulus grandis protein expression investigation using mass spectrometry
Date of Award
Dr. Richard B. Cole
Dr. Wendy M. Schluchter
Dr. Bernard B. Rees
Dr. Yang Cai
Dr. Matthew A. Tarr
Reported in this dissertation are the results of investigations performed at the New Orleans Center for Mass Spectrometry at the University of New Orleans. The projects that are detailed in the coming pages take on a variety of subjects, but a common thread is that each employs matrix-assisted laser desorption/ionization (MALDI) mass spectrometry to solve a problem. Fundamental aspects of MALDI in-plume ionization are implicated in the introduction of a newly developed electron-transfer secondary ionization matrix. The remaining projects are related to the ever expanding field of proteomics. Mass spectrometry was used to investigate the site specificity of a newly developed bilin-lyase enzyme, a new approach was developed to distinguish between A-ring and D-ring attachment of bilins, and F. grandis protein expression pattern was investigated in several tissues. All obtained results were acquired using a MALDI TOF/TOF mass spectrometer. The sensitivity, mass accuracy, mass resolution and the ability to perform collision induced decomposition (CID) experiments were all valuable features that served to raise the quality of data, and thereby improved the detail of inferences to be drawn for the different projects.
Boutaghou, Mohamed N., "Development of a novel electron-transfer secondary reaction matrix, characterization of the site–specificity of novel bilin-lyase, and Fundulus grandis protein expression investigation using mass spectrometry" (2011). University of New Orleans Theses and Dissertations. 1369.