Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by the quick devastation of nerve cells in the brain and spinal column. No cause or cure for ALS is currently known, but a subset of familial forms of ALS has been linked to point mutations in the enzyme copper-zinc superoxide dismutase (CuZnSOD). Copper is required for the activity of many enzymes involved in vital cellular processes, one of which is CuZnSOD. Despite its great importance for the process of life, copper is highly toxic if its uptake and subcellular distribution is left uncontrolled. A large body of recent data identifies a novel class of intracellular proteins, known as copper chaperones. These proteins bind, escort, and insert the copper ions into the active site of a target enzyme. The molecular identification of metal ion transporters is of great importance since an increasing number of human diseases are thought to be related to deficiencies in metal ion trafficking pathways, which can result in aberrant, misfolded proteins aggregating into insoluble deposits. The research we have conducted focuses on attempting to isolate and purify tomato chloroplast CuZnSOD and its copper chaperone, in order to more closely study the intracellular trafficking mechanisms by which copper is bound to its protein carriers and subsequently inserted into its target proteins.