Premium
Carbonyl formation on a copper‐bound prion protein fragment, PrP 23–98 , associated with its dopamine oxidase activity
Author(s) -
Shiraishi Noriyuki,
Nishikimi Morimitsu
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03324-5
Subject(s) - copper , chemistry , histidine , recombinant dna , amino acid , arginine , prion protein , lysine , biochemistry , oxidase test , redox , dopamine , dna , enzyme , stereochemistry , organic chemistry , biology , gene , neuroscience , medicine , disease , pathology
The amino‐terminal part of prion protein (PrP), containing a series of octapeptide repeats with the consensus sequence PHGGGWGQ, has been implicated in the binding of copper ion. This region possesses amino acid residues susceptible to oxidation, such as histidine, lysine, arginine and proline. In this study, we have investigated copper‐catalyzed oxidation of an N‐terminal part of human PrP, PrP 23–98 , that was prepared by the recombinant DNA technique. Carbonyl formations on copper‐bound PrP 23–98 induced by dopamine and L ‐ascorbate were analyzed kinetically, and it was found that the redox cycling of PrP 23–98 ‐bound copper, especially induced by dopamine, was coupled to the formation of carbonyls on the protein.