Ceruloplasmin in human plasma and its relationships with the copper-albumin complex.
The electron paramagnetic spectrum of human plasma is dominated, in the g = 2 region, by resonances from copper atoms bound to ceruloplasmin, and does not reveal the fraction of copper normally associated with albumin, except in a few cases, where a copper-albumin signal increases with time after blood withdrawal. This copper-albumin complex is responsible for a resonance at a g value below g = 2 in the spectrum of human serum, which has been recently attributed to a modified form of type 2 copper bound to ceruloplasmin [Rylkov, V.V., Tarasiev, M.Y. & Moshkov, K.A. (1991) Eur. J. Biochem. 197, 185-189]. In the plasma, copper associated to albumin comes from ceruloplasmin. Purified ceruloplasmin is unable to exchange copper with albumin, either purified or in plasma. It can not be ruled out that some serum components trigger the metal exchange, in a defence mechanism operating when ceruloplasmin leaks, by unknown processes, its copper content before discharging the metal into the various organs.
Musci
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G
CNR Center of Molecular Biology, University of Rome La Sapienza, Italy.
Bonaccorsi di Patti
M C
MC
Carlini
P
P
Calabrese
L
L
D000595:Amino Acid Sequence; D002570:Ceruloplasmin / Q000378:metabolism*; D003300:Copper / Q000097:blood*; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*
D012709:Serum Albumin; D003300:Copper; D002570:Ceruloplasmin