Superoxide dismutase , copper

Erythrocuprein, which contains about 60 wt % of the erythrocyte copper, hepatocuprein, and cerebrocuprein act as superoxide dismutases. Each contains two atoms of copper per molecule, having mol wt ca 34,000. The superoxide ion, O", and peroxide, two main toxic by-products of... [Pg.385]

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]

Copper-zinc-superoxide dismutase (from blood cell haemolysis) [9054-89-1J Mr 32,000... [Pg.523]

McLachlan, A.D. Repeated folding pattern in copper-zinc superoxide dismutase. Nature 285 267-268, 1980. [Pg.87]

Richardson, J.S., et al. Similarity of three-dimensional stmcture between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit. [Pg.87]

Tainer, J.A., et al. Determination and analysis of the 2 A structure of copper, zinc superoxide dismutase. [Pg.87]

Water soluble protein with a relative molecular mass of ca. 32600, which particularly contains copper and zinc bound like chelate (ca. 4 gram atoms) and has superoxide-dismutase-activity. It is isolated from bovine liver or from hemolyzed, plasma free erythrocytes obtained from bovine blood. Purification by manyfold fractionated precipitation and solvolyse methods and definitive separation of the residual foreign proteins by denaturizing heating of the orgotein concentrate in buffer solution to ca. 65-70 C and gel filtration and/or dialysis. [Pg.1493]

Structure and Properties of Copper-Zinc Superoxide Dismutases Ivano Bertini, Stefano Mangani, and Maria Silvia Viezzoli... [Pg.514]

C20-0084. In superoxide dismutase it is the Cu center that oxidizes 0. Why is copper more suitable than the center for the role of the oxidizing agent in SOD ... [Pg.1493]

Ceballos-Picot, I., Nicole, A., Briand, P., Grimber, G., Delacourte, A., Defossez, A., Javoy-Agid, F., Lafon, M., Blouin, J.L. and Sinet, P.M. (1991). Neuronal-specific expression of human copper-zinc superoxide dismutase gene in transgenic mice animal model of gene dosage effects in Down s syndrome. Brain Res, 552, 198-214. [Pg.81]

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]

Marklund, S.L., Westman, N.G., Lundgren, E. and Roos, G. (1982). Copper and zincsuperoxide dismutase, manganese-containing superoxide dismutase, catalase, and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues. Cancer Res. 42, 1955-1961. [Pg.82]

Phase II trial of copper zinc superoxide dismutase (CuZnSOD) in treatment of Crohn s disease. Free Rad. Biol. Med. 7, 145-149. [Pg.163]

Oka, S., Ogino, K., Hobara, T., Yoshimura, S., Okazaki, Y., Takemoto, T., Kato, N., lida, Y. and Uda, T. (1990b). An immunohistochemical study of copper, zinc-containing superoxide dismutase detected by a monocloncal antibody in gastric mucosa and gastric cancer. Histopathology 17, 231-236. [Pg.168]

Kensler, T.W. and Trush, M.A, (1983). Inhibition of oxygen radical metabolism in phorbol ester-activated polymorphonuclear leukocytes by an antitumor promoting copper complex with superoxide dismutase-mimetic activity. Biochem. Pharmacol. 32, 3485-3487. [Pg.259]

Kulkami-Narla A., Getchell T.V. and Getchell M.L. (1997). Differential expression of manganese and copper-zinc superoxide dismutases in the olfactory and vomeronasal receptor neurons of rats during ontogeny. J Comp Neurol 381, 31-40. [Pg.222]

Figure 12.2 Copper chaperone function, (a) Copper homeostasis in Enterococcus hirae is affected by the proteins encoded by the cop operon. CopA, Cu1+-import ATPase CopB, Cu1+-export ATPase CopY, Cu1+-responsive repressor copZ, chaperone for Cu1+ delivery to CopY. (b) The CTR family of proteins transports copper into yeast cells. Atxlp delivers copper to the CPx-type ATPases located in the post Golgi apparatus for the maturation of Fet3p. (c) Coxl7p delivers copper to the mitochondrial intermembrane space for incorporation into cytochrome c oxidase (CCO). (d) hCTR, a human homologue of CTR, mediates copper-ion uptake into human cells. CCS delivers copper to cytoplasmic Cu/Zn superoxide dismutase (SOD1). Abbreviations IMM, inner mitochondrial membrane OMM, outer mitochondrial membrane PM, plasma membrane PGV, post Golgi vessel. Reprinted from Harrison et al., 2000. Copyright (2000), with permission from Elsevier Science.

FIGURE 10.6 Comparison of solid-state and liquid-state spectra from a copper protein. The figure illustrates shifts in apparent gz and Az-values of the S = 1/2 and I =3/2 spectrum from Cu11 in bovine superoxide dismutase as a function of the surrounding medium. Top trace frozen aqueous solution at 60 K middle trace frozen water/glycerol (90/10) solution at 60 K bottom trace aqueous solution at room temperature. (Modified from Hagen 1981.)... [Pg.180]

IV. Superoxide dismutase (EC 1.15.1.1) Within a cell the superoxide dismutases (SODs) constitute the first line of defense against ROS. Superoxide radical (02) is produced where an electron transport chain is present, as in mitochondria and chloroplasts, but 02 activation may occur in other subcellular locations such as glyoxysomes, peroxisomes, apoplast and the cytosol. Thus SODs are present in all these cellular locations, converting superoxide into hydrogen peroxide and water (i.e. copper/zinc SODs are typically found in the nuclei and cytosol of eukaryotic cells). [Pg.141]

Y. Tian, M. Shioda, S. Kasahara, T. Okajima, F. Mao, T. Hisabori, and T. Ohsaka, A facilitated electron transfer of copper-zinc superoxide dismutase (SOD) based on a cysteine-bridged SOD electrode. Biochim. Biophys. Acta. 1569, 151-158 (2002). [Pg.205]

J.S. Valentine, M.W. Pantoliano, PJ. Mcdonnell, A.R. Burger, and S.J. Lippard, pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 76, 4245-4249 (1979). [Pg.205]

J.A. Fee and R.G. Briggs, Reconstitution of bovine erythrocyte superoxide dismutase. V. Preparation and properties of derivatives in which both zinc and copper sites contain copper. Biochim. Biophy. Acta. 400, 439 150 (1975). [Pg.205]

W.C. Stallings, T.B. Powers, K.A. Partridge, J.A. Fee, and M.L. Ludwig, Iron superoxide dismutase from Escherichia coli at 3.1. ANG. resolution a structure unlike that of copper/zinc protein at both monomer and dimer levels. Proc. Natl. Acad. Sci. U.SA. 80, 3884—3888 (1983). [Pg.205]

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