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B.S. Rutgers University, 1960
M.S. University of Arizona, 1963
PhD. University of Oregon, 1969

The research interests of Dr. Deinzer include the elucidation of large biopolymers by mass spectrometry. For example, the disulfide bonding patterns in the homodimer of human recombinant macrophage colony stimulating factor (rhM-CSF) was determined. More recently, the time course for disulfide bond formation during in vitro folding of rhM-CSF was followed by fast atom bombardment mass spectrometry. In further studies by electrospray mass spectrometry are under way to follow the time course of hydrogen bonding during refolding of the protein. In addition the oligosaccharide structures and sites of attachment are determined for glycoproteins.Another research area of Dr. Deinzer, is the investigation of fundamental processes of ion formation in negative ion electron capture mass spectrometry. A trochoidal electron monochromator/mass spectrometer has been constructed to determine the energies of the electrons that are captured by electrophilic molecules in the process of forming radical anions and fragment ions. This instrument also is used for the analysis of environmental compounds when high detection specificity and sensitivity is required. A new analytical dimension is added by studying the electron energies required to form radical anions in resonance processes.