Carbonyl formation on a copper-bound prion protein fragment, PrP23-98, associated with its dopamine oxidase activity
| Autor: | Noriyuki Shiraishi, Morimitsu Nishikimi |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Arginine
Prions Dopamine Blotting Western Lysine Biophysics L-Ascorbate chemistry.chemical_element Ascorbic Acid Biochemistry law.invention Carbonyl Structural Biology law Escherichia coli Genetics Consensus sequence Humans Proline Amino Acids Molecular Biology Histidine Chelating Agents Oxidase test Cell Biology Copper Peptide Fragments Prion protein chemistry Recombinant DNA Oxidoreductases Oxidation-Reduction |
| Zdroj: | FEBS Letters. 511:118-122 |
| ISSN: | 0014-5793 |
| Popis: | 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, PrP23–98, that was prepared by the recombinant DNA technique. Carbonyl formations on copper-bound PrP23–98 induced by dopamine and L-ascorbate were analyzed kinetically, and it was found that the redox cycling of PrP23–98-bound copper, especially induced by dopamine, was coupled to the formation of carbonyls on the protein. |
| Databáze: | OpenAIRE |
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