Open AccessLabile conformation of type 2 Cu 2+ centres in human ceruloplasmin
Author(s) -
RYLKOV Vladimir V.,
TARASIEV Michael Yu.,
MOSHKOV Kirill A.
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb15897.x
Subject(s) - ceruloplasmin , chemistry , electron paramagnetic resonance , hemoglobin , absorption (acoustics) , spectrophotometry , oxidase test , biochemistry , enzyme , nuclear magnetic resonance , chromatography , materials science , physics , composite material
1 The investigation of human ceruloplasmin by spectral methods (EPR and spectrophotometry) demonstrated that type 2 Cu 2+ ‐containing centres occur not in one, but in two stable forms, differing in EPR and optical spectra. The differential optical spectra of these forms were recorded and the differences in molar absorption coefficients determined. 2 By the EPR method, it was shown that both forms of these centres exist in the blood serum of control donors, as well as in the serum of patients. The relative content of these forms depends on the organism physiological state or on the presence of some pathological condition. 3 The ferroxidase activity of ceruloplasmin against hemoglobin was proved spectrophotometrically. The involvement of other serum proteins in this process cannot be ruled out. The conformational state of ceruloplasmin molecules plays an essential role in its oxidase activity.