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Superoxide dismutase/albumin

Two classes of antioxidants are known the low-molecular weight compounds (tocopherols, ascorbate, -carotene, glutathione, uric acid and etc.) and the proteins (albumin, transferrin, caeruloplasmin, ferritin, etc.) including antioxidant enzymes (e.g. superoxide dismutase, catalase, glutathione peroxidase). [Pg.354]

Lovstad, R.A. (1984). Catecholamine stimulation of copper-dependent haemolysis protective action of superoxide dismutase, catalase, hydroxyl radical scavengers and scrum proteins (ceruloplasmin, albumin and apotransferrin). Acta Pharmacol. Toxicol. 54, 340-345. [Pg.81]

Hirota, M., Inoue, M., Ando, Y. and Morino, Y. (1990). Inhibition of stress-induced gastric mucosal injury by a long acting superoxide dismutase that circulates bound to albumin. Arch. Biochem. Biophys. 280, 269-273. [Pg.164]

Bacillus subtilis defense mechanism, 610 bovine semm albumin y-radiation, 614 generation inhibition, 612 hydroperoxide synthesis, 315, 320 ludgenin oxidation, 645, 1250-1 luminol oxidation, 643, 644, 1242-4 organic sulfur compounds, 1032-9 ozone water disinfection, 606 peroxynitrite generation, 10, 611-12 Superoxide dismutase (SOD)... [Pg.1491]

The applicability of CE-ICP-MS for fast screening of weak metal interactions of Cd2+ with several test proteins (such as carbonic anhydrase from bovine erythrocytes, bovine serum albumin, human holotransferrin, ceruloplasmin and superoxide dismutase) has been studied by Cahmoun and Hagege.74 The sensitivity of element species and their detection limits in CE-ICP-MS have been improved by introducing a preconcentration step involving large volume stacking with polarity... [Pg.330]

Copper is an essential trace element absorbed in the gut and transported to the liver bound to albumin. It is found in a variety of enzymes, including superoxide dismutase. In the bloodstream Cu is present mostly in ceruloplasmin. Tissues with a relatively high content of Cu are liver, heart, and brain. The RDA for Cu in normal, healthy adults is 0.9 mg day-1, but newborns usually have liver levels higher than those of adults. The concentration of Cu in mature milk ranges between 0.2 and 0.3 mg l-1 in colostrum it is higher (0.4-0.6 mg l-1), but decreases along the lactation period (see the Chapter 13 by de la Flor St Remy et al.). [Pg.545]

ACS = anunonium (-l-)-DlO-camphorsulfonate BSA = bovine serum albumin CD = circular dichroism CT = charge transfer hCCS = human copper chaperone for superoxide dismutase hSCAN = human soluble calcium-activated nucleotidase-1 LMCT = ligand-to-metal charge transfer METP = miniaturized electron transfer protein MECT = metal-ligand charge transfer ORD = optical rotatory dispersion SODs = superoxide dismutases tCCS = tomato copper chaperone for superoxide dismutase UTP = uracil triphosphate. [Pg.6451]

Much of the copper in the plasma (60-95%) is bound to ceruloplasmin. The complex of copper and cenjloplasmir is assembled and secreted by the liver. A small fraction of plasma copper, under 7%, is weakly bound to albumin and to free amino acids, especially histidine, threonine, and glutamine. The copper bound to serum albumin is associated with a histidine residue near the amino terminus of the protein. The copper in red blood cells is bound to superoxide dismutase. [Pg.810]

A computer study has identified the critical chemical feature required in an AI agent to exploit serum albumin bound copper. Although the mechanism of action of copper complexes is unknown, stimulation of superoxide dismutase has been proposed as a contributing factor. ... [Pg.324]

Table 5 verifies the low permeability of the monolayer to a number of proteins ranging in molecular weight from a 5000 kDa random synthetic peptide with primarily hydrophilic amino acids to a 600,000 kDa conjugate of albumin and superoxide dismutase with an average molar ratio of approximately 10 1. The movement of these molecules across the monolayer over a 4-hour period is extremely slow and only slightly above background. Insulin and LDL cross the monolayer quite effectively and in a concentration-dependent manner. These experiments verify earlier work from King s laboratory [2,8]. Furthermore, when... [Pg.46]

The Cu chelates using EDTA or serum albumin display no superoxide dismutase activity. It is very attractive to conclude that — as in the case of the catalatic action of Cu2+ — one or more Cu-coordination sites are fully accessible to water or the substrate. [Pg.51]

PPL Therapeutics Bile human gastric Lipase, Fibrinogen, thrombin, Factor VII, Factor IX, alpha-antitrypsin, calcitonin (salmon), collagen, superoxide dismutase, Glucagon lipopeptide, Human serum albumin, Protein C 59-63... [Pg.837]

More copper is found in the brain and heart than in any other tissue except for liver, where it is stored as copper thionein and released as ceruloplasmin or in the form of a complex with serum albumin. The high metabolic rate of the heart and brain requires relatively large amounts of copper metalloenzymes including tyrosinase, cytochrome c oxidase, dopamine-/3-hydroxylase, pyridoxal-requiring monamine oxidases, and Cu-Zn superoxide dismutase. Copper deficiency, which can occur for reasons analogous to those discussed above for Fe and Zn, leads to brain disease in infants, anemia (since cytochrome oxidase is required for blood formation), and heart disease. Few details are known about the molecular basis for copper uptake from foods. [Pg.508]

Ceruloplasmin Cu-amino acid complexes Cu-albumin complex (and extracellular superoxide dismutases)... [Pg.443]

Figure 7 Correlation of plateau values with protein surface hydrophobicity (from hydrophobic interaction chromatography data) for the adsorption of egg-white lysozyme ( ), bovine pancrease ribonuclease (A), a-lact-albumin (x), sperm whale myoglobin ( ), and superoxide dismutase ( ) on negatively charged polystyrene in 50 mM KCI at 25°C and pH equal to pi of each protein. (From Ref. 17. Reprinted with permission.)... Figure 7 Correlation of plateau values with protein surface hydrophobicity (from hydrophobic interaction chromatography data) for the adsorption of egg-white lysozyme ( ), bovine pancrease ribonuclease (A), a-lact-albumin (x), sperm whale myoglobin ( ), and superoxide dismutase ( ) on negatively charged polystyrene in 50 mM KCI at 25°C and pH equal to pi of each protein. (From Ref. 17. Reprinted with permission.)...
Dameron, C.T. and Harris. E.D. (1987b) Regulation of aortic CuZn-superoxide dismutase with copper. Ceruloplasmin and albumin re-activate and transfer copper to the enzyme in culture. Biochem. J. 248 669-675. [Pg.485]

Wong K, Cleland L G, Poznansky M J (1980). Enhanced anti-inflammatory effect and reduced immunogenicity of bovine liver superoxide dismutase by conjugation with homologous albumin. Agents Actions. 10 231-239. [Pg.457]

Concerning the catalytic superoxide dismutase activity of low molecular mass copper complexes, some general comments are neccessary. Firstly, it should be emphasized, that apart from the inactive Cu-penicillamine, all complexes described above do not survive high concentrations of biological chelators in aqueous solutions. For example, bovine serum albumine is able to remove most of the copper from these complexes (Fig. 14). [Pg.44]


See other pages where Superoxide dismutase/albumin is mentioned: [Pg.312]    [Pg.42]    [Pg.245]    [Pg.185]    [Pg.282]    [Pg.62]    [Pg.312]    [Pg.205]    [Pg.209]    [Pg.355]    [Pg.436]    [Pg.206]    [Pg.116]    [Pg.956]    [Pg.305]    [Pg.195]    [Pg.824]    [Pg.200]    [Pg.204]    [Pg.50]    [Pg.21]    [Pg.824]    [Pg.266]    [Pg.955]    [Pg.711]    [Pg.312]    [Pg.917]   
See also in sourсe #XX -- [ Pg.43 , Pg.44 , Pg.45 , Pg.46 ]




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Dismutase

Superoxide dismutase

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