Copper-Induced Oligomerization of Ceruloplasmin
Tóm tắt
Oligomerization of copper-containing ferroxidase of ceruloplasmin in the presence of protein-unbound copper in a solution has been investigated by small-angle X-ray scattering (SAXS). Ceruloplasmin is a monomer with a molecular weight of ~132 kDa. Copper chloride added in a concentration of 10 μM leads to dimerization of 60% of protein. According to the analysis of intersubunit contacts, dimerization can prevent the formation of protein‒protein complexes of ceruloplasmin with leukocyte proteins like myeloperoxidase and eosinophil peroxidase. The formation of these complexes is a part of organism’s protective response to inflammatory processes. In addition, dimeric ceruloplasmin probably loses its ability to bind and oxidize one of substrates p-phenylenediamine.
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