Carbonyl formation on a copper-bound prion protein fragment, PrP23-98, associated with its dopamine oxidase activity.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Shiraishi N,Nishikimi M

doi

10.1016/s0014-5793(01)03324-5

keywords:

subject

Has Abstract

pub_date

2002-01-30 00:00:00

pages

118-22

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579301033245

journal_volume

511

pub_type

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