Electron paramagnetic resonance study of storage effects on ceruloplasmin in human serum compared with purified ceruloplasmin in aqueous solution.

The EPR signal amplitude of human serum ceruloplasmin shows significant changes as a function of time and temperature during storage. The same behavior occurs with aqueous solutions of purified ceruloplasmin. From the observation that the spectral lines of the EPR signal of ceruloplasmin from unmanipulated serum are identical to those coming from purified ceruloplasmin, we conclude that only type I Cu2+ of ceruloplasmin are involved in the signal changes. A temperature-dependent electron shift toward type I Cu2+ paramagnetic centers, occurring via the type II and type III Cu2+ species of the protein, is believed responsible for the process. The possible origin of the reducing electrons is discussed. A procedure to obtain reproducibility of recording of EPR spectra of ceruloplasmin in physiological fluids is proposed.