PMID: 9542060May 9, 1998Paper

An electron spin resonance (ESR) study on the mechanism of ascorbyl radical production by metal-binding proteins

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
A Mouithys-MickaladM Lamy

Abstract

The mechanism of ascorbate oxidation by metal-binding proteins (ceruloplasmin, albumin and transferrin) was investigated in vitro and in isolated plasma by the measurement of the ascorbyl free radicals (AFR) by electron spin resonance (ESR). In plasma of 13 healthy volunteers, a spontaneous and variable production of AFR was detected, which was increased by a 10(-4) M ascorbate overloading; however, this increase was not correlated to the intensity of the spontaneous AFR signal. The addition of Cu2+ and ceruloplasmin to plasma increased the ESR signal, while the addition of transferrin decreased the signal intensity in a dose-dependent manner. In vitro, we demonstrated that ascorbate was oxidized by human serum albumin and by ceruloplasmin, and that this oxidase-like activity was lost by trypsin or heat treatment of these proteins. These two proteins positively interacted in the oxidation of ascorbate, since addition of crude albumin to a solution of ascorbate and ceruloplasmin increased the intensity of ESR signal in a dose-dependent manner. The treatment of albumin by a metal chelator (DDTC) abolished these positive interactions. The respective roles of copper and iron in ascorbate oxidation were studied and showed a dose-dep...Continue Reading

Citations

Mar 7, 2008·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Günther WeberHeiko Hayen
Apr 5, 2007·Journal of Neural Transmission·J Healy, K Tipton

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