Copper-zinc superoxide dismutase-1 (CuZnSOD) is a radical-scavenging enzyme occurring intracellularly in humans. A toxic gain-of-function in this enzyme has been established as a cause of amyotrophic lateral sclerosis (ALS or Lou Gehrig’ s Disease). Approximately 3% of cases of ALS have been linked to various genetic point mutations in the gene encoding CuZnSOD. This study examines the chemistry of CuZnSOD. Our first goal was to develop methods to produce and purify the SOD. We were able to isolate a very pure sample of the wild-type protein and have begun to test its metal binding properties. Our group has also worked with various mutant forms of CuZnSOD responsible for ALS. We will present results on the purification of the A4V mutant and the production of a plasmid sequence encoding the G93A mutant.
Jonathan Bostrom, ’07 Zimmerman, MN
Majors: Music, Biochemistry and Molecular Biology
Sponsor: Cynthia Strong