Superoxide Dismutase (SOD) is an antioxidant enzyme important for maintaining safe levels of reactive oxygen species (ROS). Harnessing the natural antioxidant power of SOD is desirable for the prevention and treatment of diseases that cause, or are caused by, oxidative stress. The Cu/Zn human Superoxide Dismutase 1 (SOD1) produced in this work is also important for research into treatments of amyotrophic lateral sclerosis (ALS), which is a disease characterized by degeneration of motor neurons and subsequent death. 10% of ALS cases are familial and result from deposits of mutated aggregation prone SOD1. The production of SOD1 mutants (particularly ALS mutants) is difficult due to the increased aggregation propensity. A protocol was developed for the expression and purification of soluble SOD1 to minimize the number of steps and cost, making it accessible for both research and teaching laboratories. The systematic approach taken to create the procedure can be followed to tailor production of other proteins and mutants with the same or higher propensity for aggregation. The simplified procedure and reduced cost can be adapted in general biochemistry or molecular biology undergraduate lab courses.

Systematic approach to a simplified SOD1 production suitable for research as well as teaching

ACS Spring 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.