A kinetic study of the coupled iron-ceruloplasmin catalyzed oxidation of ascorbate in the presence of albumin.
Ascorbate is catalytically oxidized by a couple iron-ceruloplasmin system, the iron ions functioning as a red/ox cycling intermediate between ceruloplasmin and ascorbate. Serum albumin, an iron binding compound, was found to stimulate the ascorbate oxidation rate. It is proposed that ferrous ions react more rapidly with ceruloplasmin when they are bound to albumin. A Km value of 39 microM was estimated for Fe(2+)-albumin. Citrate and urate inhibit the iron-ceruloplasmin-dependent ascorbate oxidation by chelating ferric ions. In the presence of albumin only citrate reduced the oxidation rate, the observation suggesting the following order of iron binding ability: citrate > albumin > urate. Physiological aspects of the results have been discussed.
Løvstad
R A
RA
Department of Medical Biochemistry, University of Oslo, Norway.
D000818:Animals; D001205:Ascorbic Acid / Q000378:metabolism*; D002417:Cattle; D002570:Ceruloplasmin / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D012710:Serum Albumin, Bovine / Q000494:pharmacology*
D012710:Serum Albumin, Bovine; D007501:Iron; D002570:Ceruloplasmin; D001205:Ascorbic Acid