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Figure 1 | BMC Biochemistry

Figure 1

From: The subunit composition of human extracellular superoxide dismutase (EC-SOD) regulate enzymatic activity

Figure 1

The EC-SOD dimers separate into three forms. Human EC-SOD was subjected to non-reduced SDS-PAGE using a 9% acrylamide gel. Glycosylated EC-SOD (-PNGase F) separates into the disulfide-linked dimer and monomers. The monomers are resolved into aEC-SOD and iEC-SOD as previously shown [23]. The dimer migrates as a fuzzy band of ~52 kDa. When EC-SOD is deglycosylated (+PNGase F) the size of the monomers and dimer is reduced consistent with the removal of a single glycan in each subunit. The deglycosylated dimer resolved into three closely migrating bands of 45 – 49 kDa denoted α, β, and γ as indicated. The position of the deglycosylated monomers is indicated. The gel was stained by Coomassie brilliant blue. A molecular weight marker is indicated on the left. Deglycosylation of EC-SOD improved the separation in non-reduced SDS-PAGE and revealed that the disulfide-bonded dimer migrates as 3 bands most likely caused by differences in folding.

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