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Antioxidant activity related to copper binding of native prion protein
Author(s) -
Brown David R.,
Clive Christine,
Haswell Stephen J.
Publication year - 2001
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2001.00009.x
Subject(s) - copper , superoxide dismutase , antioxidant , peptide , chemistry , prion protein , biochemistry , oxidative stress , microbiology and biotechnology , biology , medicine , disease , organic chemistry
We have developed a method to affinity‐purify mouse prion protein (PrP c ) from mouse brain and cultured cells. PrP c from mouse brain bound three copper atoms; PrP c from cultured cells bound between one and four copper atoms depending on the availability of copper in the culture medium. Purified PrP c exhibited antioxidant activity, as determined by spectrophotometric assay. Incubation of PrP c with the neurotoxic peptide, PrP106‐126, inactivated the superoxide dismutase‐like activity. Culture experiments showed that PrP c protects cells against oxidative stress relative to the amount of copper it binds. These results suggest that PrP c is a copper‐binding protein which can incorporate varying amounts of copper and exhibit protective antioxidant activity.