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    Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10405-9.

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

    Crapo JD, Oury T, Rabouille C, Slot JW, Chang LY.

    Source

    Department of Medicine, Duke University Medical Center, Durham, NC 27710.

    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.

    PMID:
    1332049
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC50347
    Free PMC Article

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