Abstract
The intracellular localization of Cu,Zn superoxide dismutase (superoxide:superoxide oxidoreductase, EC 1.15.1.1) has been examined by immunofluorescence using four monoclonal anti-Cu,Zn superoxide dismutase antibodies raised against a recombinant human Cu,Zn superoxide dismutase derivative produced and purified from Escherichia coli. Colocalization with catalase, a peroxisomal matrix enzyme, was used to demonstrate the peroxisomal localization of Cu,Zn superoxide dismutase in human fibroblasts and hepatoma cells. In the fibroblasts of Zellweger syndrome patients, the enzyme is not transported to the peroxisomal ghosts but, like catalase, remains in the cytoplasm. In addition, immunocryoelectron microscopy of yeast cells expressing human Cu,Zn superoxide dismutase showed that the enzyme is translocated to the peroxisomes.
MeSH Terms
Amino Acid Sequence
Animals
Antibodies, Monoclonal
Carcinoma, Hepatocellular/enzymology
Fibroblasts/enzymology,ultrastructure
Fluorescent Antibody Technique
Humans
Liver Neoplasms/enzymology
Mice
Mice, Inbred BALB C/immunology
Microbodies/enzymology,ultrastructure
Microscopy, Immunoelectron
Molecular Sequence Data
Recombinant Proteins/analysis,immunology
Saccharomyces cerevisiae/genetics
Superoxide Dismutase/analysis,immunology
Zellweger Syndrome/enzymology,pathology
Chemicals
Antibodies, Monoclonal
Recombinant Proteins
Superoxide Dismutase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Keller G A
Genentech Inc., South San Francisco, CA 94080.
Warner T G
Steimer K S
Hallewell R A
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