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In vitro interaction between ceruloplasmin and human serum transferrin.

Authors
  • Ha-Duong, Nguyêt-Thanh
  • Eid, Chantal
  • Hémadi, Miryana
  • El Hage Chahine, Jean-Michel
Type
Published Article
Journal
Biochemistry
Publisher
American Chemical Society
Publication Date
Dec 07, 2010
Volume
49
Issue
48
Pages
10261–10263
Identifiers
DOI: 10.1021/bi1014503
PMID: 21049900
Source
Medline
License
Unknown

Abstract

The thermodynamics of the interactions of serum apotransferrin (T) and holotransferrin (TFe(2)) with ceruloplasmin (Cp), as well as those of human lactoferrin (Lf), were assessed by fluorescence emission spectroscopy. Cp interacts with two Lf molecules. The first interaction depends on pH and μ, whereas the second does not. Dissociation constants were as follows: K(11Lf) = 1.5 ± 0.2 μM, and K(12Lf) = 11 ± 2 μM. Two slightly different interactions of T or TFe(2) with Cp are detected for the first time. They are both independent of pH and μ and occur with 1:1 stoichiometry: K(1T) = 19 ± 7 μM, and K(1TFe2) = 12 ± 4 μM. These results can improve our understanding of the probable process of the transfer of iron from Cp to T in iron and copper transport and homeostasis.

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