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.

Keywords

CytosolPolyclonal antibodiesSuperoxide dismutaseBiochemistryMolecular biologyCytoplasmDismutaseBiologyMonoclonal antibodyParaformaldehydeChemistryAntibodyEnzymeImmunology

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Year
1992
Type
article
Volume
89
Issue
21
Pages
10405-10409
Citations
489
Access
Closed

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James D. Crapo, Tim D. Oury, Cathérine Rabouille et al. (1992). Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells.. Proceedings of the National Academy of Sciences , 89 (21) , 10405-10409. https://doi.org/10.1073/pnas.89.21.10405

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DOI
10.1073/pnas.89.21.10405