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Ceruloplasmin blood

In sheep fed diets containing 330, 670, or 1000 g/ kg velvet bean (24 g/kg L-dopa) for 42 days, no changes in concentrations of blood ceruloplasmin or L-dopa, or concentrations of L-dopa metabolites, were observed (Chikagwa-Malunga et al. 2009). [Pg.585]

Copper Albumin (portal blood) Ceruloplasmin (nonportal blood) IgGi myeloma protein Diglycyl-histi-dine (synthetic peptide) Evans (1973) Dixon and Sarkar(1974) Evans (1973) Baker and Hultquist (1978) Lau et al. (1974) Metallothionein Evans (1973)... [Pg.9]

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]

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]

It has also been proposed that because of sequence and possible structural homology with the blood clotting factors V and VIII [6] that ceruloplasmin may also participate in blood clotting and its regulation [5]. [Pg.53]

Figure 6. Structural relationships between ascorbate oxidase, ceruloplasmin, nitrite reductase, and blood clotting factor VIII. Figure 6. Structural relationships between ascorbate oxidase, ceruloplasmin, nitrite reductase, and blood clotting factor VIII.
Treated rats had 1000 mg/kg FW liver (vs. 4.7 in controls) lowered hemoglobin, hematocrit, and red cell counts mean survival time of 67 days hepatic and renal histopathology Dose-time-dependent increase in copper concentrations in liver, spleen, and lung little accumulation in muscle and skin. Reduced growth at 2.5 and 3.75 mg/kg BW daily reduced survival at 3.75 mg/kg BW. Maximum copper concentrations recorded, in mg/kg FW (vs. saline controls,) were 710 in liver (<5), 212 in kidney (<10), 7 in lung (<1.5), 27 in spleen (<2.0) 6 in bone (<2.0) and 2.2 in testes (<1.6) Increased serum ceruloplasmin and white blood cell number... [Pg.206]

Increase in blood and urine Mo levels, increases in serum ceruloplasmin, increased xanthine oxidase activity (11) Increased uric acid, decreased copper excretion, high incidence of gout-like disease (11)... [Pg.1566]

Contrary to popular belief, ceruloplasmin5, the principal copper-containing protein in plasma, ceruloplasmin, is not involved in copper transport. This is clearly underlined by the clinical observation that patients with aceruloplasminaemia (i.e. lacking ceruloplasmin in their blood) have perfectly normal copper metabolism and homeostasis. Copper is transported in plasma mostly by serum albumin with smaller amounts bound to low-molecular weight ligands like histidine. Likewise zinc is mostly transported in plasma bound to proteins (albumin and ot2-macroglobulin). [Pg.148]

A blue, copper-containing glycoprotein present in mammalian blood plasma and containing type 1, type 2, and type 3 copper centers. The type 2 and type 3 copper centers are close together, forming a trinuclear copper cluster. Ceruloplasmin has an important role in the transport and storage of copper ions. Thus, it participates in the metabolism of copper-containing enzymes. [Pg.124]

The multi-copper oxidases include laccase, ceruloplasmin, and ascorbate oxidase. Laccase can be found in tree sap and in fungi ascorbate oxidase, in cucumber and related plants and ceruloplasmin, in vertebrate blood serum. Laccases catalyze oxidation of phenolic compounds to radicals with a concomitant 4e reduction of O2 to water, and it is thought that this process may be important in the breakdown of lignin. Ceruloplasmin, whose real biological function is either quite varied or unknown, also catalyzes oxidation of a variety of substrates, again via a 4e reduction of O2 to water. Ferroxidase activity has been demonstrated for it, as has SOD activity. Ascorbate oxidase catalyzes the oxidation of ascorbate, again via a 4e reduction of O2 to water. Excellent reviews of these three systems can be found in Volume 111 of Copper Proteins and Copper Enzymes (Lontie, 1984). [Pg.178]

A number of other proteins are now known to exhibit heterogeneity with respect to their carbohydrate content these include pig pancreatic ribonuclease,9 rabbit19 and human109-238 -yG immunoglobulin, ceruloplasmin,239 2-acetamido-2-deoxy-/3-D-glucosidase,240 and the blood-group substances from ovarian cysts.145,241... [Pg.446]

As demonstrated with "Cu in rats, (Cu,Zn)-SOD receives its copper from ceruloplasmin after 2-3 days The (Cu,Zn)-SOD activity in erythrocytes is reduced in Cu deficiency, as shown with several species With rats e.g. during Cu depletion, plasma Cu and ceruloplasmin were decreased by 78 and 75% respectively against 72 % and only 56 % for the blood cell Cu and (Cu,Zn)-SOD respectively In three patients with Wilson s disease the SOD level of erythrocytes was normal, although the disease is characterized by an accumulation of Cu in the liver e.g. and usually by low concentrations and sometimes the absence of ceruloplasmin... [Pg.14]

A copper-binding protein, ceruloplasmin, which is a blood serum protein, has been demonstrated in milk by immunodiffusion techniques (Hanson et al. 1967 Poulik and Weiss 1975). It may be the enzyme ferroxidase (EC 1.16.3.1). [Pg.105]

Because Cu2+ is the most tightly bound metal ion in most chelating centers (Table 6-9), almost all of the copper present in living cells is complexed with proteins. Copper is transported in the blood by a 132-kDa, 1046-residue sky-blue glycoprotein called ceruloplasmin.471475-477 This one protein contains 3% of the total body copper. [Pg.883]

In addition to its previously mentioned role in copper transport, ceruloplasmin is an amine oxidase, a superoxide dismutase, and a ferrooxidase able to catalyze the oxidation of Fe2+ to Fe3+. Ceruloplasmin contains three consecutive homologous 350-residue sequences which may have originated from an ancestral copper oxidase gene. Like ascorbate oxidase, this blue protein contains copper of the three different types. Blood clotting factors V and VIII (Fig. 12-17), and the iron uptake protein Fet3 (Section A,l) are also closely related. [Pg.887]

Ceruloplasmin is the major copper-containing protein in mammalian blood plasma (see Section 62.1.8.5), and appears to consist of a single polypeptide chain of molecular weight 130 000.1341 The nine-line superhyperfine splitting in the ESR spectrum of the type 2 copper has been interpreted in terms of four equivalent nitrogen ligands.978... [Pg.700]

Wilson s disease is a pathological accumulation of copper in tissue which is later released into the bloodstream, leading to anaemia, and final accumulation of copper in liver and brain. It is the result of a mutation in the Wilson s disease gene in chromosome 13 which ordinarily codes for a cation transporting ATPase so that copper can be incorporated into ceruloplasmin prior to excretion. Also known as ferroxi-dase, in acknowledgement of its primary function as an oxidoreductase responsible for electron transfer, this enzyme contains iron and, more importantly, six copper atoms. It accounts for the transport of 90% of copper in the plasma so any impairment in its production or efficacy has a major impact on copper homeostasis. The greatly reduced concentration of ceruloplasmin in the blood of Wilson s disease sufferers correlates with their inability to metabolize copper effectively. It leads to chronic liver disease, for which the only real cure is a liver transplant,... [Pg.210]

Evidence for Ceruloplasmin Synthesis from Cu64 by Isolated Liver. Figure 8 shows the linear disappearance of Cu64 activity from the perfusion blood during the first 4 hours of a 5-hour perfusion. Analyses of small lobes of the liver removed at 5 minutes, 3 hours, and 5 hours revealed that at least 53% of the initial Cu64 activity was retained by the liver and more than 10% was in the bile collected during the perfusion. Preferential concentration of parenterally administered Cu64 in the liver of intact animals has been described (16). [Pg.51]


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