Point mutations of the enzyme copper-zinc superoxide dismutase (CuZnSOD) have been linked to the neurodegenerative disease familial amyotrophic lateral sclerosis (FALS), or Lou Gehrig’ s disease. Although the mechanism of the disease has not been determined, abnormal protein folding and protein aggregation seem to play a role. Shifts in the visible absorption spectra of remetallated mutant apoproteins suggest improper metal binding and protein folding in some of the mutant forms of CuZnSOD, thus leading researchers to suppose that the toxicity of the mutant protein is connected to its metal-binding properties. In this project, human wild-type and mutant (A4V) CuZnSOD were produced in E. coli. In addition, experiments were performed with the bovine form of CuZnSOD in order to lay a foundation for future research into the metal-binding properties of the A4V mutant human protein. These experiments included measurement of enzymatic activity, replacement of metal ions, and quantitation of metals in the protein.
Kathryn Brown, ’06 Wayzata, MN
Major: Chemistry – ACS Certified
Christina Klug, ‘07 Cedar Rapids, IA
Majors: Chemistry – ACS Certified, Biochemistry and Molecular Biology
Sponsor: Cynthia Strong