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A kinetic study of the coupled iron-ceruloplasmin catalyzed oxidation of ascorbate in the presence of albumin

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Abstract

Ascorbate is catalytically oxidized by a coupled 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 K m value of 39 μ m was estimated for Fe2+-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.

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References

  • Anghileri LJ. 1967 Fate of intravenously injected iron compounds: ferric-fructose complex, iron-EDTA, ferric hydroxide and iron-albumin labeled with 59Fe. Biochem Pharmacol 16, 2033–2036.

    Google Scholar 

  • Carver FJ, Farb DL, Frieden E. 1982 The effect of albumin, ceruloplasmin and other serum constituents on Fe(II) oxidation. Biol Trace Element Res 4, 1–19.

    Google Scholar 

  • Cleland WW. 1967 The statistical analysis of enzyme kinetic data. Adv Enzymol 29, 1–32.

    Google Scholar 

  • Curzon G. 1961 Some properties of coupled iron-caeruloplasmin oxidation systems. Biochem J 79, 656–663.

    Google Scholar 

  • Davies KJA, Sevanian A, Muakkassah-Kelly SF, Hochstein P. 1986 Uric acid iron complexes. Biochem J 235, 747–754.

    Google Scholar 

  • Frieden E, Hsieh HS. 1974 Ceruloplasmin: the copper transport protein with essential oxidase activity. Adv Enzymol 44, 187–236.

    Google Scholar 

  • Grootveld M, Bell JD, Halliwell B, Arouma OI, Bomford A, Sadler PJ. 1989 Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis. J Biol Chem 264, 4417–4422.

    Google Scholar 

  • Gutteridge JMC, Rowley DA, Griffiths E, Halliwell B. 1985 Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic haemochromatosis. Clin Sci 68, 463–467.

    Google Scholar 

  • Jacobs A, Greenman D, Owen E, Cavill I. 1971 Ascorbic acid status in iron-deficiency anaemia. J Clin Pathol 24, 694–697.

    Google Scholar 

  • Johnson DA, Osaki S, Frieden E. 1967 A micromethod for the determination of ferroxidase (ceruloplasmin) in human serums. Clin Chem 13, 142–150.

    Google Scholar 

  • Lynch M, Seftel HC, Torrance JD, Charlton RW, Botherwell TH. 1967 Accelerated oxidative catabolism of ascorbate in siderotic Bantu. Am J Clin Nutr 20, 641–647.

    Google Scholar 

  • Lovstad RA. 1993 Interaction of serum albumin with the Fe(III)-citrate complex. Int J Biochem 25, 1015–1017.

    Google Scholar 

  • Martin RB, Savory J, Brown S, Bertholf RL, Wills MR. 1987 Transferrin binding of A13+ and Fe3+. Clin Chim 33, 405–407.

    Google Scholar 

  • McDermott JA, Huber CT, Osaki S, Frieden E. 1968 The role or iron in the oxidase activity of ceruloplasmin. Biochim Biophys Acta 151, 541–557.

    Google Scholar 

  • Minetti M, Forte T, Soriani M, Quaresima V, Menditto A, Ferrari M. 1992 Iron-induced ascorbate oxidation in plasma as monitored by ascorbate free radical formation. Biochem J 282, 459–465.

    Google Scholar 

  • Osaki S. 1966 Kinetic studies on the ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin). J Biol Chem 241, 5053–5059.

    Google Scholar 

  • Osaki S, Johnson DA, Frieden E. 1966 The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J Biol Chem 241, 2746–2751.

    Google Scholar 

  • Osaki S, McDermott JA, Frieden E. 1964 Citric acid as the principal serum inhibitor of ceruloplasmin. J Biol Chem 239, PC364-PC366.

    Google Scholar 

  • Rydén L, Björk I. 1976 Reinvestigation of some physicochemical and chemical properties of human ceruloplasmin (ferroxidase). Biochemistry 15, 3411–3417.

    Google Scholar 

  • Smit S, Leijnse B, van der Kroon AM. 1981 Polynuclear ion compounds in human transferrin preparations. J Inorg Chem 15, 329–338.

    Google Scholar 

  • Sober HA. 1970 In: CRC Handhook of Biochemistry. 2nd edn. Cleveland, OH: Chemical Rubber Co.

    Google Scholar 

  • Van der Heul C, van Eijk HG, Wiltink WF, Leijnse B. 1972 The binding of iron to transferrin and other serum components at different degrees of saturation with iron. Clin Chim Acta 38, 347–353.

    Google Scholar 

  • Witwicki J, Chidambaran MV, Frieden E. 1983 Identification of citrate as the albumin-bound inhibitor of the ferroxidase activity of ceruloplasmin. Biol Trace Element Res 5, 81–90.

    Google Scholar 

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

    Rolf Arthur Løvstad

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  1. Rolf Arthur Løvstad
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Løvstad, R.A. A kinetic study of the coupled iron-ceruloplasmin catalyzed oxidation of ascorbate in the presence of albumin. Biometals 8, 328–331 (1995). https://doi.org/10.1007/BF00141606

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  • DOI: https://doi.org/10.1007/BF00141606

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