Abstract
The effects of various forms of lactoferrin (Lf) interacting with ceruloplasmin (Cp, ferro-O2-oxidoreductase, EC 1.16.3.1) on oxidase activity of the latter were studied. Comparing the incorporation of Fe3+ oxidized by Cp into Lf and serum transferrin (Tf) showed that at pH 5.5 apo-Lf binds the oxidized iron seven times and at pH 7.4 four times faster than apo-Tf under the same conditions. Apo-Lf increased the oxidation rate of Fe2+ by Cp 1.25 times when Cp/Lf ratio was 1 : 1. Lf saturated with Fe3+ or Cu2+ increased the oxidation rate of iron 1.6 and 2 times when Cp to holo Lf ratios were 1 : 1 and 1 : 2, respectively. Upon adding to Cp the excess amounts of apo-Lf (Cp/apo-Lf < 1 : 1) or of holo Lf (Cp/holo-Lf < 1 : 2) the oxidation rate of iron no longer changed. Complex Cp-Lf demonstrating ferroxidase activity was discovered in breast milk.
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Abbreviations
- Cp:
-
ceruloplasmin
- Lf:
-
lactoferrin
- Tf:
-
transferrin
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Translated from Biokhimiya, Vol. 70, No. 9, 2005, pp. 1231–1236.
Original Russian Text Copyright © 2005 by Sokolov, Pulina, Zakharova, Shavlovski, Vasilyev.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-271, February 13, 2005.
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Sokolov, A.V., Pulina, M.O., Zakharova, E.T. et al. Effect of Lactoferrin on the Ferroxidase Activity of Ceruloplasmin. Biochemistry (Moscow) 70, 1015–1019 (2005). https://doi.org/10.1007/s10541-005-0218-9
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DOI: https://doi.org/10.1007/s10541-005-0218-9