Mitchell, John L. A.
B.S. (Bachelor of Science)
Department of Biological Sciences
Polyamines are essential for life and are associated with cell cycle and development. Excess polyamine production occurs during tumor formation and is one possible target for chemopreventative and chemotherapeutic treatment. One enzyme, ornithine decarboxylase (ODC), plays a key role in polyamine biosynthesis. Among other regulators, the protein antizyme (Az) limits polyamine levels in the cell. It binds ODC and renders it unable to produce polyamines. The mechanism by which ODC and Az interact is unknown and is explored in this study. It is known that ODC and Az have high affinity for one another, but the reason for the basal level of ODC activity that remains in excess Az in assays is unclear. Varying the temperature and coenzyme concentrations in an assay revealed that these factors successfully changed the level of ODC activity at which the two proteins ceased to bind. The persistence of ODC activity in excess Az under several assay conditions showed that the remaining activity is not a result of the methods by which the assay is prepared. The mechanism by which some ODC activity is allowed to remain in excess Az remains uncertain.
Cain, Jennifer, "Optimal assay conditions for ODC-antizyme interaction" (2000). Honors Capstones. 855.
Northern Illinois University
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