Role of Oxidative Modification in the Lability of Ceruloplasmin
Ceruloplasmin (CP) is a blue copper oxidase found in human serum. It has been suggested that CP functions as an antioxidant by virtue of its ability to scavenge the superoxide anion radical1 and/or its ability to catalyse the conversion of Fe(II) to Fe(III), thereby inhibiting the Fenton reaction2. However, the true physiological role of CP is still not clear. In attempting to define such a role it is important to recognise the relative lability of this protein3. Many of the changes in the physicochemical properties of CP3 which occur during isolation and storage can be ascribed to proteolysis3. However, this does not appear to account for all of the modifications which occur during the ageing of CP preparations.
KeywordsCircular Dichroism Beta Sheet Visible Fluorescence Beta Sheet Structure Human Ceruloplasmin
Unable to display preview. Download preview PDF.
- 2.D.J. Al-Timini and T.L. Dormandy, The inhibition of lipid autoxidation by human ceruloplasmin, Biochem. J. 168:283 (1977).Google Scholar
- 3.L. Ryden, Ceruloplasmin, in.: “Copper proteins and copper enzymes Volume III”, R. Lontie, ed., CRC Press, Boca Raton, Florida (1984).Google Scholar