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. 1992 Nov 1;89(21):10405–10409. doi: 10.1073/pnas.89.21.10405

Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells.

J D Crapo 1, T Oury 1, C Rabouille 1, J W Slot 1, L Y Chang 1
PMCID: PMC50347  PMID: 1332049

Abstract

The intracellular localization of human copper,zinc superoxide dismutase (Cu,Zn-SOD; superoxide:superoxide oxidoreductase, EC 1.15.1.1) was evaluated by using EM immunocytochemistry and both isolated human cell lines and human tissues. Eight monoclonal antibodies raised against either native or recombinant human Cu,Zn-SOD and two polyclonal antibodies raised against either native or recombinant human Cu,Zn-SOD were used. Fixation with 2% paraformaldehyde/0.2% glutaraldehyde was found necessary to preserve normal distribution of the protein. Monoclonal antibodies were less effective than polyclonal antibodies in recognizing the antigen after adequate fixation of tissue. Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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