Ceruloplasmin

Title: Ceruloplasmin
CAS Registry Number: 9031-37-2
Additional Names: Caeruloplasmin; ferroxidase
Literature References: Intensely blue colored copper-containing glycoprotein of the a2-globulin fraction of mammalian blood; it is the principal copper transport protein and is believed to play an important role in iron mobilization via its ferroxidase activity. First reported by C. G. Holmberg, Acta Physiol. Scand. 8, 227 (1944). Isoln, purification and description of properties of porcine and human ceruloplasmin: C. G. Holmberg, C. B. Laurell, Acta Chem. Scand. 2, 550 (1948). Ceruloplasmin accounts for 90-95% of the circulating copper in normal mammals. Its concentration increases by a factor of 2 to 3 during pregnancy and varies significantly in several diseases and hormonal conditions. Prepd by Cohn cold ethanol fractionation: Cohn et al., J. Am. Chem. Soc. 68, 459 (1946); Steinbuch, Quentin, Nature 183, 323 (1959); and further purified from fraction IV: Sanders et al., Arch. Biochem. Biophys. 84, 60 (1959); US 3003918 (1961 to Merck & Co.). Different mol wts have been reported for human ceruloplasmin, ranging from 126,000 to 160,000; the most generally accepted is 134,000 ±3000, cf. L. Ryder, I. Björk, Biochemistry 15, 3411 (1976). Chemical and structural studies of porcine ceruloplasmin: Osaki et al., J. Biochem. (Tokyo) 48, 190 (1960); 50, 24, 29 (1961); Mukasa et al., Biochim. Biophys. Acta 168, 132 (1968); Matsunaga, Nosoh, ibid. 215, 280 (1970); of human: Kasper, Deutsch, J. Biol. Chem. 238, 2325 (1963); Jamieson, ibid. 240, 2019 (1965); Poillon, Bearn, Biochim. Biophys. Acta 127, 407 (1966); Simons, Bearn, ibid. 175, 260 (1969); Ryden, Eur. J. Biochem. 26, 380 (1972); T. G. Samsonidze et al., Int. J. Pept. Protein Res. 14, 161 (1979); V. N. Zaitsev et al., Kristallografiya 25, 174 (1980), C.A. 92, 210415q (1980). Human metabolism: Kekki et al., Nature 209, 1252 (1966). Reviews of biological role: E. Frieden, H. S. Hsieh, Adv. Exp. Med. Biol. 74, 505-529 (1976); J. M. C. Gutteridge, Ann. Clin. Biochem. 15, 293-296 (1978). Comprehensive review: S. H. Laurie, E. S. Mohammed, Coord. Chem. Rev. 33, 279-312 (1980).
Properties: Absorption max: 280, 610 nm (E1%1cm 14.9, 0.68). Electrophoretic mobility (cm/volt/sec): -5.05 ´ 10-5 at pH 7.0 (0.1M phosphate buffer); -5.32 ´ 10-5 at pH 8.6 (0.1M barbital sodium buffer).
Absorption maximum: Absorption max: 280, 610 nm (E1%1cm 14.9, 0.68)
Cervicarcin Cesium Bromide Cesium Carbonate Cesium Chloride Cesium Fluoride

Ceruloplasmin (ferroxidase)

PDB rendering based on 1kcw.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CP (; CP-2)
External IDs OMIM: 117700 MGI: 88476 HomoloGene: 75 GeneCards: CP Gene
EC number 1.16.3.1
RNA expression pattern
PBB GE CP 204846 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1356 12870
Ensembl ENSG00000047457 ENSMUSG00000003617
UniProt P00450 Q61147
RefSeq (mRNA) NM_000096 NM_001042611
RefSeq (protein) NP_000087 NP_001036076
Location (UCSC) Chr 3:
148.88 – 148.94 Mb
Chr 3:
19.96 – 20.01 Mb
PubMed search [1] [2]

Ceruloplasmin (or caeruloplasmin) is a ferroxidase enzyme that in humans is encoded by the CP gene.[1][2][3]

Ceruloplasmin is the major copper-carrying protein in the blood, and in addition plays a role in iron metabolism. It was first described in 1948.[4] Another protein, hephaestin, is noted for its homology to ceruloplasmin, and also participates in iron and probably copper metabolism.