Superoxide Dismutase Cu,Zn, Bovine (SOD)

Catalog Number

S8060

References

Abernethy, J., Steinman, H., and Hill, R.: Bovine Erythrocyte Superoxide Dismutase. Subunit Structure and Sequence Location of the Intrasubunit Disulfide Bond, J. Biol. Chem., 249, 7339 (1974).\n\nAllen, R., Yevich, S., Orth, R., and Steele, R.: The Superoxide Anion and Singlet Molecular Oxygen: Their Role in the Mitochondrial Activity of the Polymorphonuclear Leukocyte, Biochem. Biophys. Res. Comm., 60, 909 (1974).\n\nArgese, E., Rigo, A., Viglino, P., Orsega, E., Marmocchi, F., Cocco, D., and Rotilo, G.: A Study of the pH Dependence of the Activity of Porcine Cu,Zn Superoxide Dismutase, Biochim. Biophys. Acta, 787, 205 (1984).\n\nArgese, E., Viglino, P., Rotilio, G., Scarpa, M., and Rigo, A.: Electrostatic Control of the Rate-Determining Step of the Copper,Zinc Superoxide Dismutase Catalytic Reaction, Biochem., 26, 3224 (1987).\n\nAustin, L., Arthur, H., de Niese, M., Gurusinghe, A., Baker, M.: Micromethods in Single Muscle Fibers. 1. Determination of Catalase and Superoxide Dismutase, Anal. Biochem., 174, 568 (1988).\n\nBannister, J., Bannister, W., and Wood, E.: Bovine Erythrocyte Cupro-zinc Protein. I. Isolation and General Characterization, Eur. J. Biochem., 18, 178 (1971).\n\nBarra, D., Schinina, M., Simmaco, M., Bannister, J., Bannister, W., Rotilo, G., and Bossa, F.: The Primary Structure of Human Liver Manganese Superoxide Dismutase, J. Biol. Chem., 259, 12595 (1984).\n\nBasin, M., Patterson, L., Ronfard-Haret, J., and Santus, R.: Superoxide Dismutase as an Amplifier of the Chemical Reactivity of Porphyrin Radical Cations, Photochem. Photobiol., 48, 177 (1988).\n\nBeaman, B., Scates, S., Moring, S., Deem, R., and Misra, H.: Purification and Properties of a Unique Superoxide Dismutase from Nocardia asteroides, J. Biol. Chem., 258, 91 (1983).\n\nBeauchamp, C., and Fridovich, I.: Superoxide Dismutase: Improved Assays and an Assay Applicable to Acrylamide Gels, Anal. Biochem., 44, 276 (1971).\n\nBeauchamp, C., and Fridovich, I.: Isozymes of Superoxide Dismutase from Wheat Germ, Biochim. Biophys. Acta, 317, 50 (1973).\n\nBeem, K., Rich, W., and Rajagopalan, K.: Total Reconstitution of Copper-Zinc Superoxide Dismutase, J. Biol. Chem., 249, 7298 (1974).\n\nBenkovic, J., Tillman, T., Cudd, A., and Fridovich, I.: Electrostatic Facilitation of the Reaction Catalyzed by the Manganese-Containing and the Iron-Containing Superoxide Dismutases, Arch. Biochem. Biophys., 221, 329 (1983).\n\nBeyer, W., and Fridovich, I.: Effect of Hydrogen Peroxide on the Iron-Containing Superoxide Dismutase of Escherichia coli, Biochem., 26, 1251 (1987).\n\nBeyer, W., Wang, Y., and Fridovich, I.: Phosphate Inhibition of the Copper-and Zinc-Containing Superoxide Dismutase: A Reaxamination, Biochem., 25, 6084 (1986).\n\nBolann, B., and Ulvik, R.: Improvement of a Direct Spectrophotometric Assay for Routine Determination of Superoxide Dismutase Activity, Clin. Chem., 37, 1992 (1991).\n\nBray, R., Cockel, S., Fielden, E., Roberts, P., Rotilio, G., and Calabrese, L.: Reduction and Inactivation of Superoxide Dismutase by Hydrogen Peroxide, Biochem. J., 139, 43 (1974).\n\nCalabrese, L., Federici, G., Bannister, W., Bannister, J., Rotilio, G., and Finazzi-Agro, A.: Labile Sulfur in Human Superoxide Dismutase, Eur. J. Biochem., 56, 305 (1975).\n\nCalabrese, L., Polticelli, F., Capo, C., and Musci, G.: Involvement of the Copper in the Inhibition of Cu,Zn Superoxide Dismutase Activity at High pH, Free Rad. Res. Comm., 12, 305 (1991).\n\nCarrico, R., and Deutsch, H.: The Presence of Zinc in Human Cytocuprein and Some Properties of the Apoprotein, J. Biol. Chem., 245, 723 (1970).\n\nChelack, W., and Petkau, A.: Concentration-dependent Inactivation of Superoxide Dismutase, Biochim. Biophys.Acta, 660, 83 (1981).\n\nChuaqui, C., and Petkau, A.: Radiation-induced Inactivation of Superoxide Dismutase in Nitrous Oxide-saturated Solutions. A Kinetic Model, Biochim. Biophys. Acta, 702, 112 (1982).\n\nCiriolo, M., Desideri, A., Paci, M., and Rotilio, G.: Reconstitution of Cu, Zn-Superoxide Dismutase by the Cu(I)-Glutathione Complex, J. Biol. Chem., 265, 11030 (1990).\n\nCivalleri, L., Pino, C., Rigio, A., Federico, R., Calabrese, L., and Rotilio, G.: Isolation and Preliminary Characterization of Electrophoretic Variants of Copper, Zinc Superoxide Dismutase, Mol. Cell. Biochem., 47, 3 (1982).\n\nClare, D., Blum, J., and Fridovich, I.: A Hybrid Superoxide Dismutase Containing both Functional Iron and Manganese, J. Biol. Chem., 259, 5932 (1984).\n\nCocco, D., Calabrese, L., Finazzi-Agro, A., and Rotilio, G.: Electrostatic Interactions in Cu,Zn Superoxide Dismutase. Effects of Ca(II) and of Anions not Binding to the Copper, Biochim. Biophys. Acta, 746, 61 (1983).\n\nCocco, D., Calabrese, L., Rigo, A., Argese, E., and Rotilio, G.: Re-examination of the Reaction of Diethyldithiocarbamate with the Copper of Superoxide Dismutase, J. Biol. Chem., 256, 8983 (1981).\n\nCuperus, R., Muijsers, A., and Wever, R.: The Superoxide Dismutase Activity of Myeloperoxidase: Formation of Compound III, Biochim. Biophys. Acta, 871, 78 (1986).\n\nde Freitas, D., and Valentine, J.: Phosphate Is an Inhibitor of Copper-Zinc Superoxide Dismutase, Biochem., 23, 2079 (1984).\n\nDeChatelet, L., McCall, C., McPhail, L., and Johnston, R.: Superoxide Dismutase Activity in Leukocytes, J. Clin. Invest., 53, 1197 (1974).\n\nDesideri, A., Cocco, D., Calabrese, L., and Rotilio, G.: Co(II) Derivatives of Cu, Zn-Superoxide Dismutase with the Cobalt Bound in the Place of Copper. A New Spectroscopic Tool for the Study of the Active Site, Biochim. Biophys. Acta, 785, 111 (1984).\n\nDionisi, O., Galeotti, T., Terranova, T., and Azzi, A.: Superoxide Radicals and Hydrogen Peroxide Formation in Mitochondria from Normal and Noeplastic Tissues, Biochim. Biophys. Acta, 403, 292 (1975).\n\nDunbar, J., Holmquist, B., and Johansen, J.: Asymmetric Active Site Structures in Yeast Dicopper Dizinc Superoxide Dismutase. I. Reconstitution of Apo-Superoxide Dismutase, Biochem., 23, 4324 (1984).\n\nEvans, H., Steinman, H., and Hill, R.: Bovine Erythrocyte Superoxide Dismutase. Isolation and Characterization of Tryptic, Cyanogen Bromide, and Methylated Tryptic Peptides, J. Biol. Chem., 249, 7315 (1974).\n\nFee, J.: Studies on the Reconstitution of Bovine Erythrocyte Superoxide Dismutase. IV. Preparation and Some Properties of the Enzyme in Which Co(II) is Substituted for Zn(II), J. Biol. Chem., 248, 4229 (1973a).\n\nFee, J.: Studies on the Reconstitution of Bovine Erythrocyte Superoxide Dismutase. I. The Presence of Four Divalent Metal-Binding Sites on the Apo Protein Which are Different from the Native Sites, Biochim. Biophys. Acta, 295, 87 (1973b).\n\nFee, J., and Bull, C.: Steady-state Kinetic Studies of Superoxide Dismutases, J. Biol. Chem., 261, 13000 (1986).\n\nFee, J., and DiCorleto, P.: Observations on the Oxidation-Reduction Properties of Bovine Erythrocyte Superoxide Dismutase, Biochem., 12, 4893 (1973).\n\nFee, J., and Gaber, B.: Anion Binding to Bovine Erythrocyte Superoxide Dismutase. Evidence for Multiple Binding Sites with Qualitatively Different Properties, J. Biol. Chem., 247, 60 (1972).\n\nFee, J., and Teitelbaum, H.: Evidence that Superoxide Dismutase Plays a Role in Protecting Red Blood Cells Against Peroxidative Hemolysis, Biochem. Biophys. Res. Comm., 49, 150 (1972).\n\nFee, J., Bergamini, R., and Briggs, R.: Observations on the Mechanism of the Oxygen Dialuric Acid Induced Hemolysis of Vitamin E-Deficient Rat Blood Cells and the Protective Roles of Catalase and Superoxide Dismutase, Arch. Biochem. Biophys., 169, 160 (1975).\n\nFee, J., Natter, R., and Baker, G.: Studies on the Reconstitution of Bovine Erythrocyte Superoxide Dismutase. II. Some Observations on the Nature of Catalyzed Superoxide Anion Dismutation as an Enzymatic Activity, Biochim. Biophys. Acta, 295, 96 (1973).\n\nFee, J., Peisach, J., and Mims, W.: Superoxide Dismutase. Examination of the Metal Binding Sites by Electron Spin Echo Spectroscopy, J. Biol. Chem., 256, 1910 (1981).\n\nFielden, E., Roberts, P., Bray, R., and Rotilio, G.: Mechanism and Inactivation of Superoxide Dismutase Activty, Biochem. Soc. Trans., 1, 52 (1973).\n\nFielden, E., Roberts, P., Bray, R., Lowe, D., Mautner, G., Rotilio, G., and Calabrese, L.: The Mechanism of Action of Superoxide Dismutase from Pulse Radiolysis and Electron Paramagnetic Resonance. Evidence that Only Half the Active Sites Function in Catalysis, Biochem. J., 139, 49 (1974).\n\nForman, H., and Fridovich, I.: Superoxide Dismutase: A Comparison of Rate Constants, Arch. Biochem. Biophys., 158, 396 (1973).\n\nForman, H., and Fridovich, I.: On the Stability of Bovine Superoxide Dismutase. The Effects of Metals, J. Biol. Chem., 248, 2645 (1973).\n\nForman, H., Evans, H., Hill, R., and Fridovich, I.: Histidine at the Active Site of Superoxide Dismutase, Biochem., 12, 823 (1973).\n\nFridovich, I.: Superoxide Radical and Superoxide Dismutase, Accounts Chem. Res., 5, 321 (1972).\n\nFridovich, I.: Superoxide Radical and Superoxide Dismutase, Biochem. Soc. Trans., 1, 48 (1973).\n\nFridovich, I.: Biological Effects of the Superoxide Radical, Arch. Biochem. Biophys., 247, 1 (1986).\n\nGoda, K., Kimura, T., Thayer, A., Kees, K., and Schaap, A.: Singlet Molecular Oxygen in Biological Systems: Non-Quenching of Singlet Oxygen-Mediated Chemiluminescence by Superoxide Dismutase, Biochem. Biophys. Res. Comm., 58, 660 (1974).\n\nGoscin, S., and Fridovich, I.: The Purification and Properties of Superoxide Dismutase from Saccharomyces cerevisiae, Biochim. Biophys. Acta, 289, 276 (1972).\n\nGregory, E., Goscin, S., and Fridovich, I.: Superoxide Dismutase and Oxygen Toxicity in a Eukaryote, J. Bacteriol., 117, 456 (1974).\n\nGregory, E., Yost, F., and Fridovich, I.: Superoxide Dismutases of Escherichia coli: Intracellular Localization and Functions, J. Bacteriol., 115, 987 (1973).\n\nGrunow, M., and Sch