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A kinetic study on the copper-albumin catalyzed oxidation of ascorbate

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Abstract

Serum albumin can specifically bind one Cu(II)-ion, and is proposed to function as a copper transport protein in vivo. Cu(II)-albumin is rapidly reduced by ascorbate. A second order rate constant of 0.54 mM−1 min−1 was estimated for the reaction. The oxidation process is catalytic, the Cu(I)-albumin molecule being reoxidized by molecular oxygen. The reaction was found to follow Michaelis-Menten kinetics, characterized by an apparent Km-value of 0.89 mM, and a catalytic constant of 0.066 μM O2/min. An apparent inhibition of oxygen uptake was obtained with catalase (but not with superoxide dismutase), suggesting the formation of H2O2 in the system. Wilson's disease patients usually have increased amounts of non-ceruloplasmin copper in plasma. The low level of plasma ascorbate observed in such patients could possibly be due, at least in part, to an oxidation by Cu(II)-albumin.

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Authors and Affiliations

  1. Department of Medical Biochemistry, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway

    Rolf A. Løvstad

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Løvstad, R.A. A kinetic study on the copper-albumin catalyzed oxidation of ascorbate. Biometals 15, 351–355 (2002). https://doi.org/10.1023/A:1020247323914

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