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Ceruloplasmin human

The Known or Predicted Copper Ligands in All Currently Available Sequences of Hephaestin (Human, hHP Mice, mHP), Ceruloplasmin (Human, hCP Mice, mCP rat, rCP Sheep, sCP), Factor V (Human, hFV Mice, mFV Pig, pFV, Bovine, bFV), and Factor VIII (Human, hFVHI Mice, mFVHI Pig, pFVIII, Dog, dFVHIf... [Pg.326]

Copper is one of the twenty-seven elements known to be essential to humans (69—72) (see Mineral nutrients). The daily recommended requirement for humans is 2.5—5.0 mg (73). Copper is probably second only to iron as an oxidation catalyst and oxygen carrier in humans (74). It is present in many proteins, such as hemocyanin [9013-32-3] galactose oxidase [9028-79-9] ceruloplasmin [9031 -37-2] dopamine -hydroxylase, monoamine oxidase [9001-66-5] superoxide dismutase [9054-89-17, and phenolase (75,76). Copper aids in photosynthesis and other oxidative processes in plants. [Pg.256]

Ceruloplasmin (from human blood plasma) [9031-37-2] Mr 134,000. This principle Cu transporter (90-90% of circulating Cu) is purified by precipitation with polyethylene glycol 4000, balchwise adsorption and elution from QAE-Sephadex, and gradient elution from DEAE-Sepharose CL-6B. Ceruloplasmin... [Pg.519]

Copper appears as the a2-globulin ceruloplasmin in the human body (Sarkar 1994). Deficiency of this protein in serum is characteristic of both Menkes and Wilson s diseases. Wilson s disease is an abnormal storage of Cu(II) in body tissues. Cu(II) in biological material can be determined by spectrophotometry or by FAAS, ceruloplasmin in serum by a spectrophotometric method. [Pg.203]

Figure 12.4 Proposed path for the intracellular transfer of Cu(I) by Atxl. Copper destined for incorporation into the vascular multicopper oxidase Fet3 requires both Ctrl and Ccc2. Cytoplasmic Cu(I)-Atxl, but not apo-Atxl, associates with the amino-terminal domain of Ccc2 and Cu(I) is transferred to the latter. (Inset) A proposed mechanism for the exchange of Cu(I) involving two- and three-coordinate Cu-bridged intermediates. The human homologues of Atxl (Hahl), Ccc2 (Menkes and Wilson s proteins) and Fet3 (ceruloplasmin) are likely to employ similar mechanisms. Reprinted with permission from Pufahl et al., 1997. Copyright (1997) American Association for the Advancement of Science. Figure 12.4 Proposed path for the intracellular transfer of Cu(I) by Atxl. Copper destined for incorporation into the vascular multicopper oxidase Fet3 requires both Ctrl and Ccc2. Cytoplasmic Cu(I)-Atxl, but not apo-Atxl, associates with the amino-terminal domain of Ccc2 and Cu(I) is transferred to the latter. (Inset) A proposed mechanism for the exchange of Cu(I) involving two- and three-coordinate Cu-bridged intermediates. The human homologues of Atxl (Hahl), Ccc2 (Menkes and Wilson s proteins) and Fet3 (ceruloplasmin) are likely to employ similar mechanisms. Reprinted with permission from Pufahl et al., 1997. Copyright (1997) American Association for the Advancement of Science.
It has been reported that ceruloplasmin increases iron uptake into cultured human cells (Mukhopadhyay et al, 1998), although this apparently contradictory in vitro observation must be set against the in vivo evidence presented above from both animal and human studies. Plasma ceruloplasmin levels increase markedly in anaemia, consistent with a physiological role in tissue iron mobilization, and this effect is due to transcriptional activation of ceruloplasmin mRNA synthesis (Mukhopadhyay et al, 2000). [Pg.330]

A typical time course of PCL with luminol as the photosensitizer is shown in Figure 5, as blank. The presence of a water-soluble antioxidant leads to dose-dependent temporary inhibition of PCL. ACW (antioxidant capacity of water-soluble compounds) represents the effect of human blood plasma (2 p.L) on PCL all tested antioxidants, such as ascorbic acid, uric acid, Trolox, taurine, bilirubin, ceruloplasmin, etc., produced the same effects. [Pg.506]

Figure 1. (a) A schematic representation of the overall organization of the molecule of human ceruloplasmin. Domains 2,4, and 6 contain mononuclear copper centers, while the trinuclear copper cluster is located at the interface of domains 1 and 6. (b) An a-carbon ribbon diagram of the human ceruloplasmin molecule viewed along the pseudo threefold axis highlighting the triplication of the structure. Domains 1, 3, and 5 are depicted by striped motifs, whereas domains 2, 4, and 6 are dark shaded. The copper... [Pg.62]

In mammals, phenobarbital and phenytoin increase serum ceruloplasmin concentrations (Aaseth and Norseth 1986). Chronic copper poisoning in sheep is exacerbated when diets contain heliotrope plants (Heliotropium sp., Echium spp., Senecio sp.). Aggravated effects of the heliotrope plants include reduced survival and a twofold to threefold increase in liver and kidney copper concentrations when compared to control animals fed copper without heliotropes (Howell et al. 1991). Rats given acutely toxic doses of 2,3,7,8-tetrachlorodibenzo-para-dioxin had elevated concentrations of copper in liver and kidney because of impaired biliary excretion of copper (Elsenhans et al. 1991). Morphine increases copper concentrations in the central nervous system of rats, and dithiocarbam-ates inhibit biliary excretion (Aaseth and Norseth 1986). In human patients, urinary excretion of copper is increased after treatment with D-penicillamine, calcium disodium EDTA, or calcium trisodium diethylenetriamine penta acetic acid (Flora 1991). [Pg.139]

Bacterial hosts are inappropriate choices for expression of proteins such as the blue copper proteins stellacyanin, laccase, and ceruloplasmin which are extensively glycosylated. In these cases, it may be necessary to employ tissue cultures of appropriate origin to obtain the native protein. In this regard, the amino-terminal half of human serum transferrin, which lacks carbohydrate, has been expressed in high yield in baby hamster kidney cells by Funk et al. [13], while the glycosylated carboxyl-terminus has proved to be more problematic [103]. [Pg.138]


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