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. Author manuscript; available in PMC: 2009 Oct 5.
Published in final edited form as: J Biol Chem. 2006 Nov 8;282(1):345–352. doi: 10.1074/jbc.M604503200

FIGURE 2. FALS mutations at copper-binding histidine residues of SOD1 dramatically reduce affinity for copper.

FIGURE 2

A, CHO cells were transfected to express human SOD variants before being metabolically labeled with 50 μCi/ml of 64Cu for 3 h. 100 μg of each cell lysate was separated on a non-reducing 10% polyacrylamide gel containing 0.1% SDS. The 64Cu autoradiogram shows Cu-labeled endogenous hamster SOD1 dimer (solid arrow) in all samples, and Cu-labeled human SOD1 dimer (solid arrowhead) only in the WT sample. B, a duplicate of the gel used for 64Cu autoradiogram was analyzed by SOD1 immunoblot, which reveals endogenous hamster SOD1 monomer and human SOD1 monomers that are not labeled by 64Cu. Note: apo refers to the absence or presence of copper.