Amyotrophic lateral sclerosis (ALS), more commonly known as Lou Gehrig’s disease, is a neurodegenerative disease with no known cure. Presently, a portion of familial ALS cases can be linked to a mutation in the sod1 gene, which encodes the protein copper-zinc superoxide dismutase. In many ALS patients, aggregated proteins (amyloid) have been found in their cells. In order to conduct the aggregation experiments, protein was harvested from glycerol stocks of E. coli. During this process, a method was discovered for maximizing yield and purity of the protein. Multiple aggregation experiments were conducted with the superoxide dismutase protein under varying aggregation conditions. These conditions included the superoxide dismutase protein alone, as well as in the presence of actin or bovine serum albumin for various agitation times. Aggregation was detected by adding Congo Red to all solutions and running the solutions on a spectrophotometer to observe the shift in the absorbance peak.
Amanda Johnson, ’12
North Branch, MN
Majors: Biochemistry and Molecular Biology, Mathematics
Kirtley Hitt, ’12
Majors: Biochemistry and Molecular Biology, Kinesiology
Sponsors: Jeffrey Cardon and Cynthia Strong