Abstract
Analysis of electron paramagnetic resonance spectra of human and porcine ceruloplasmin indicated the presence of one type 2 and two type 1 paramagnetic copper ions per enzyme molecule. The two type 1 copper ions are spectrometrically distinguishable, exhibiting different hyper‐fine splittings, and in the case of human ceruloplasmin respond differently to variation of pH over the range 4.5–7.0. Comparative experiments carried out with porcine enzyme provided evidence that there is no direct relationship between observed pH‐dependent changes of the type 1 copper signal in spectra of human ceruloplasmin and the variation with pH of the rate of reduction of the enzyme.
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