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A blood glycoprotein to which copper is bound during transport and storage.

American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.


a protein responsible for copper detoxification, found in the blood
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References in periodicals archive ?
in this research Cu shows positive correlation with Fe while negative correlation with Pb, more over in another study done by James A Bush in USA, iron deficiency was reported in Childs because of prolong intake of cow's milk, cow's milk has low quantities of Cu to balance the metabolism [28].Cu has a major role in Fe metabolism, oxidation of ferrous to ferric state is carried out by the ferroxidase activity of major plasma Cu protein, ceruloplasmin.
CP exhibits function as antioxidant by taking part in ferroxidase activity, ascorbate oxidase activity, oxygen radical clearance activity and GSH dependent peroxidase activity.23,24
The exported [Fe.sup.2+] is oxidized to [Fe.sup.3+] by the astrocytic ferroxidase, glycosylphosphatidylinositol (GPI)-anchored cerulopasmin.
Ceruloplasmin (ferroxidase) is a glycoprotein enzyme produced in the liver and essential in iron oxidation, permitting it to bind with the iron transport protein transferrin (Jain, 1993).
Ceruloplasmin (ferroxidase) oxidizes hydroxylamine probes: Deceptive implications for free radical detection.
The hephaestin, a transmembrane copper-containing ferroxidase, having 50% homology to ceruloplasmin, works as a facilitator for iron export from enterocytes into blood circulation.
(2003) A Novel Extracellular Multicopper Oxidase from Phanerochaete chrysosporium with Ferroxidase Activity.
Ceruloplasmin(Cp) is a ferroxidase enzyme synthesized in the liver and is involved in carrying copper in the blood and in addition plays a role in iron metabolism [28, 29].
(ix) Total ferroxidase (total FeOx) activity was measured in serum samples according to Erel's method [23] with some minor modifications.
The H chains of ferritin have ferroxidase activity and convert Fe(II) to Fe(III) as the iron is internalized within the ferritin complex [27].
In addition, ceruloplasmin appears to exert protective effects against OxS because of its ability to isolate copper from the plasmatic environment and its well-described ferroxidase activity.
Tyagi, "Ferritin structure from Mycobacterium tuberculosis: comparative study with homologues identifies extended C-terminus involved in ferroxidase activity," PLoS One, vol.