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Journal articles on the topic 'Superoxide dismutase'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 July 2024

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1

Öhman, Michael, and Stefan L. Marklund. "Plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-containing superoxide dismutase in alcoholics treated with disulfiram." Clinical Science 70, no. 4 (April 1, 1986): 365–69. http://dx.doi.org/10.1042/cs0700365.

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1. Disulfiram has long been used in the treatment of chronic alcoholism. It is in vivo partially reduced to diethyldithiocarbamate, which is an efficient inhibitor of Cu, Zn-containing superoxide dismutase both in vitro and in vivo. The recently described extracellular superoxide dismutase is even more sensitive to diethyldithiocarbamate than Cu, Zn-superoxide dismutase. 2. To test for the possibility that long term treatment with disulfiram leads to inhibition of the superoxide dismutases, plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-superoxide dismutase were determined in 12 disulfiram-treated alcoholics, and compared with 11 non-treated alcoholics and 19 healthy controls. 3. Plasma extracellular superoxide dismutase was moderately reduced (about 20%) in the disulfiram-treated alcoholics as compared with the non-treated alcoholics and the healthy controls. No effect of disulfiram treatment on erythrocyte Cu, Zn-superoxide dismutase activity was demonstrated.

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2

James, E. R. "Superoxide dismutase." Parasitology Today 10, no. 12 (January 1994): 481–84. http://dx.doi.org/10.1016/0169-4758(94)90161-9.

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3

YUASA, Makoto, Kenichi OYAIZU, and Hidenori MURATA. "Superoxide Dismutase Mimics." Oleoscience 6, no. 6 (2006): 307–17. http://dx.doi.org/10.5650/oleoscience.6.307.

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4

Simovic, Misho O., Martin J. D. Bonham, Fikri M. Abu-Zidan, and John A. Windsor. "Manganese Superoxide Dismutase." Pancreas 15, no. 1 (July 1997): 78–82. http://dx.doi.org/10.1097/00006676-199707000-00011.

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5

&NA;. "Superoxide dismutase cream." Inpharma Weekly &NA;, no. 796 (July 1991): 6. http://dx.doi.org/10.2165/00128413-199107960-00014.

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6

Rosenthal, Rosalind A., Susan R. Doctrow, and Wyeth B. Callaway. "Superoxide Dismutase Mimics." Antioxidants & Redox Signaling 14, no. 6 (March 15, 2011): 1173. http://dx.doi.org/10.1089/ars.2010.3758.

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7

Salvemini, Daniela, Carolina Muscoli, Dennis P. Riley, and Salvatore Cuzzocrea. "Superoxide Dismutase Mimetics." Pulmonary Pharmacology & Therapeutics 15, no. 5 (October 2002): 439–47. http://dx.doi.org/10.1006/pupt.2002.0374.

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8

Nozik-Grayck, Eva, Hagir B. Suliman, and Claude A. Piantadosi. "Extracellular superoxide dismutase." International Journal of Biochemistry & Cell Biology 37, no. 12 (December 2005): 2466–71. http://dx.doi.org/10.1016/j.biocel.2005.06.012.

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9

Hunaiti, A. "Radial Diffusion as a Simple and Rapid Method for Screening Superoxide Dismutase Activity." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 24, no. 5 (September 1987): 511–12. http://dx.doi.org/10.1177/000456328702400515.

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Superoxide dismutases are of great interest due to their increasing medical applications in therapy and diagnosis of some diseases. The radial diffusion assay was evaluated for its usefulness as a simple, cheap and accurate assay for screening superoxide dismutase activity. In this assay O2− radicals were generated from the interaction of reduced riboflavin with molecular oxygen upon exposure of agar gel containing riboflavin and N,N,N̄,N̄-tetramethylethylene diamine (TEMED) to light. If nitrotctrazolium dye is also present, it will be reduced to the blue insoluble formazan, whilst if superoxide dismutase is present it will prevent this blueing.1 The developed assay was found to give reproducible estimates of pure samples of superoxide dismutase with a lower limit of measurements of about 10 mg. It can be adapted to measure the levels of superoxide dismutase in various crude biological samples.

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10

Chary, P., D. Dillon, A. L. Schroeder, and D. O. Natvig. "Superoxide dismutase (sod-1) null mutants of Neurospora crassa: oxidative stress sensitivity, spontaneous mutation rate and response to mutagens." Genetics 137, no. 3 (July 1, 1994): 723–30. http://dx.doi.org/10.1093/genetics/137.3.723.

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Abstract Enzymatic superoxide-dismutase activity is believed to be important in defense against the toxic effects of superoxide. Although superoxide dismutases are among the best studied proteins, numerous questions remain concerning the specific biological roles of the various superoxide-dismutase types. In part, this is because the proposed damaging effects of superoxide are manifold, ranging from inactivation of certain metabolic enzymes to DNA damage. Studies with superoxide-deficient mutants have proven valuable, but surprisingly few such studies have been reported. We have constructed and characterized Neurospora crassa mutants that are null for sod-1, the gene that encodes copper-zinc superoxide dismutase. Mutant strains are sensitive to paraquat and elevated oxygen concentrations, and they exhibit an increased spontaneous mutation rate. They appear to have near wild-type sensitive to near- and far-UV, heat shock and gamma-irradiation. Unlike the equivalent Saccharomyces cerevisiae mutant and the sodA sodB double mutant of Escherichia coli, they do not exhibit aerobic auxotrophy. These results are discussed in the context of an attempt to identify consensus phenotypes among superoxide dismutase-deficient mutants. N. crassa sod-1 null mutant strains were also employed in genetic and subcellular fractionation studies. Results support the hypothesis that a single gene (sod-1), located between Fsr-12 and leu-3 on linkage group I, is responsible for most or all CuZn superoxide dismutase activity in this organism.

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11

Sanchez-Moreno, M., M. Monteoliva, A. Fatou, and M. A. García-Ruiz. "Superoxide dismutase fromAscaris suum." Parasitology 97, no. 2 (October 1988): 345–53. http://dx.doi.org/10.1017/s0031182000058546.

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SummaryThree superoxide dismutases (SOD) (EC 1.15.1.1) were detected in homogenates ofAscaris suum. Each of the three forms of SOD was purified by a sequence of multiple differential centrifugations, ammonium sulphate precipitation, ion-exchange chromatography and G-75 Sephadex column chromatography. The three forms of SOD were present in different cellular locations; one in the cytoplasmic fraction, sensitive to cyanide and hydrogen peroxide, and two in the mitochondrial fraction, one of which was cyanide sensitive. The SOD forms presented clear differences in their electrophoretic patterns. The sexual organs of females showed the highest SOD activities of all the tissues examined. The finding of such high levels of superoxide dismutase inA. suumreflects the importance of this enzyme in the metabolism of this helminth parasite.

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12

Meier, B., C. Michel, M. Saran, J. Hüttermann, F. Parak, and G. Rotilio. "Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii that is active with iron or manganese: pH-dependence." Biochemical Journal 310, no. 3 (September 15, 1995): 945–50. http://dx.doi.org/10.1042/bj3100945.

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Kinetic studies were performed on the superoxide dismutases isolated from the anaerobic bacterium Propionibacterium shermanii as active enzymes with either iron or manganese, which were naturally incorporated into the same molecule depending on the metal supply. Both the Fe- and Mn- forms showed decreasing activity with increasing pH. This suggests the protonation of some groups near the metal, possibly a metal-bound water molecule. Thus the kinetic behaviour of this superoxide dismutase is much more dependent on the protein structure than on the metal incorporated into the active site. The secondary structures of both forms were not influenced by variations in pH, whereas the EPR spectra of the Fe-superoxide dismutase changed as a function of pH. The EPR spectra apparently consist of two overlapping species. Steady-state experiments proved that all iron-containing species show catalytic activity, but the species predominating in the alkaline pH range displays a lower reaction rate. The Michaelis constant and maximal turnover number for the Fe-superoxide dismutase were determined polarographically as Km = 0.54 mmol/l and Vmax. = 2000 mol.s-1 at pH 9.5. These data indicate that, in anaerobic bacteria under physiological conditions, the superoxide dismutase is not saturable with O2-. and the catalytic activity is similar to that of metal-specific Fe- or Mn-superoxide dismutases from aerobic organisms.

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13

Gutteridge, J. M. C., and J. V. Bannister. "Copper + zinc and manganese superoxide dismutases inhibit deoxyribose degradation by the superoxide-driven Fenton reaction at two different stages. Implications for the redox states of copper and manganese." Biochemical Journal 234, no. 1 (February 15, 1986): 225–28. http://dx.doi.org/10.1042/bj2340225.

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When OH. radicals are formed in a superoxide-driven Fenton reaction, in which O2.- is generated enzymically, deoxyribose degradation is effectively inhibited by CuZn- and Mn-superoxide dismutases. The products of this reaction are H2O2 and a Fe3+-EDTA chelate. The mixing of H2O2 and a Fe3+-EDTA chelate also generates OH. radicals able to degrade deoxyribose with the release of thiobarbituric acid-reactive material. This reaction too is inhibited by CuZn- and Mn-superoxide dismutases, suggesting that most of the OH. is formed by a non-enzymic O2.- -dependent reduction of the Fe3+-EDTA chelate. Since the reaction between the Fe3+-EDTA chelate and H2O2 leads to a superoxide dismutase-inhibitable formation of OH. radicals, it could suggest a much wider protective role for the superoxide dismutase enzymes in biological systems. Urate produced during the reaction of xanthine oxidase and hypoxanthine limits deoxyribose degradation as well as the effectiveness of the superoxide dismutase enzymes to inhibit damage to deoxyribose by H2O2 and the Fe3+-EDTA chelate. Some of this damage may result from an O2.--independent pathway to OH. formation in which urate reduces the ferric complex.

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14

Park, Joong-ho, and Jae-heon Kim. "Comparison of enzyme activities of the native and N-terminal 6xHis-tagged Fe supreoxide dismutase from Streptomyces subrutilus P5." Korean Journal of Microbiology 52, no. 2 (June 30, 2016): 230–35. http://dx.doi.org/10.7845/kjm.2016.6030.

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15

IÑARREA, Pedro, Hadi MOINI, Daniel RETTORI, Derick HAN, Jesús MARTÍNEZ, Inés GARCÍA, Erika FERNÁNDEZ-VIZARRA, María ITURRALDE, and Enrique CADENAS. "Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase." Biochemical Journal 387, no. 1 (March 22, 2005): 203–9. http://dx.doi.org/10.1042/bj20041683.

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The localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2•−) released into this compartment. The present study was aimed at examining the functionality of Cu,Zn-superoxide dismutase and elucidating the molecular basis for its activation in the intermembrane space. Intact rat liver mitochondria neither scavenged nor dismutated externally generated O2•−, unless the mitochondrial outer membrane was disrupted selectively by digitonin. The activation of the intermembrane space Cu,Zn-superoxide dismutase following the disruption of mitochondrial outer membrane was largely inhibited by bacitracin, an inhibitor of protein disulphide-isomerase. Thiol alkylating agents, such as N-methylmaleimide or iodoacetamide, decreased intermembrane space Cu,Zn-superoxide dismutase activation during, but not after, disruption of the outer membrane. This inhibitory effect was overcome by exposing mitochondria to low micromolar concentrations of H2O2 before disruption of the outer membrane in the presence of the alkylating agents. Moreover, H2O2 treatment alone enabled intact mitochondria to scavenge externally generated O2•−. These findings suggest that intermembrane space Cu,Zn-superoxide dismutase is inactive in intact mitochondria and that an oxidative modification of its critical thiol groups is necessary for its activation.

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16

Campanella, Luigi, Gabriele Favero, and Mauro Tomassetti. "Superoxide Dismutase Biosensors for Superoxide Radical Analysis." Analytical Letters 32, no. 13 (January 1999): 2559–81. http://dx.doi.org/10.1080/00032719908542988.

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17

Kuratsuji, Tadatoshi, and Noriaki Shinomiya. "Superoxide and Superoxide Dismutase in Bronchial Asthma." Pediatrics International 29, no. 5 (October 1987): 680–85. http://dx.doi.org/10.1111/j.1442-200x.1987.tb00360.x.

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18

Rump, Alexis F. E., Renate Rösen, and Wolfgang Klaus. "Cardioprotection by Superoxide Dismutase." Anesthesia & Analgesia 76, no. 2 (February 1993): 239–46. http://dx.doi.org/10.1213/00000539-199302000-00007.

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19

WATANABE, KAZUTADA. "Superoxide Dismutase and Aging." Sen'i Gakkaishi 44, no. 5 (1988): P168—P173. http://dx.doi.org/10.2115/fiber.44.5_p168.

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20

Bowler, Chris, Wim Van Camp, Marc Van Montagu, Dirk Inzé, and Kozi Asada. "Superoxide Dismutase in Plants." Critical Reviews in Plant Sciences 13, no. 3 (January 1994): 199–218. http://dx.doi.org/10.1080/07352689409701914.

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21

Bowler, C., W. Van Camp, M. Van Montagu, and D. Inze. "Superoxide Dismutase in Plants." Critical Reviews in Plant Sciences 13, no. 3 (1994): 199. http://dx.doi.org/10.1080/713608062.

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22

Elmer, G. I., J. L. Evans, S. R. Goldberg, C. J. Epstein, and J. L. Cadet. "Transgenic superoxide dismutase mice." Behavioural Pharmacology 7, no. 7 (November 1996): 628???639. http://dx.doi.org/10.1097/00008877-199611000-00008.

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23

BORMAN, STU. "Superoxide dismutase mimic developed." Chemical & Engineering News 77, no. 41 (October 11, 1999): 18. http://dx.doi.org/10.1021/cen-v077n041.p018.

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24

Orrell, RichardW, and JacquelineS deBelleroche. "Superoxide dismutase and ALS." Lancet 344, no. 8938 (December 1994): 1651–52. http://dx.doi.org/10.1016/s0140-6736(94)90452-9.

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25

Chen, Dan-Dan, and Alex F. Chen. "CuZn Superoxide Dismutase Deficiency." Hypertension 48, no. 6 (December 2006): 1026–28. http://dx.doi.org/10.1161/01.hyp.0000247304.56192.ce.

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26

Gillissen, Adrian, James H. Roum, Robert F. Hoyt, and Ronald G. Crystal. "Aerosolization of Superoxide Dismutase." Chest 104, no. 3 (September 1993): 811–15. http://dx.doi.org/10.1378/chest.104.3.811.

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27

Robinson, D. S., J. K. Donnelly, S. M. Lawlor, P. J. Frazier, and N. W. R. Daniels. "Wheat Superoxide Dismutase Isoenzymes." Journal of Cereal Science 23, no. 1 (January 1996): 93–101. http://dx.doi.org/10.1006/jcrs.1996.0009.

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28

Miller, Anne-Frances, K. Padmakumar, David L. Sorkin, A. Karapetian, and Carrie K. Vance. "Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase." Journal of Inorganic Biochemistry 93, no. 1-2 (January 2003): 71–83. http://dx.doi.org/10.1016/s0162-0134(02)00621-9.

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29

Natvig, D. O., K. Imlay, D. Touati, and R. A. Hallewell. "Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants." Journal of Biological Chemistry 262, no. 30 (October 1987): 14697–701. http://dx.doi.org/10.1016/s0021-9258(18)47851-9.

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30

Andersen, P. M., P. Nilsson, L. Forsgren, and S. L. Marklund. "CuZn-Superoxide Dismutase, Extracellular Superoxide Dismutase, and Glutathione Peroxidase in Blood from Individuals Homozygous for Asp90Ala CuZn-Superoxide Dismutase Mutation." Journal of Neurochemistry 70, no. 2 (November 14, 2002): 715–20. http://dx.doi.org/10.1046/j.1471-4159.1998.70020715.x.

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31

Schäfer, G., and S. Kardinahl. "Iron superoxide dismutases: structure and function of an archaic enzyme." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1330–34. http://dx.doi.org/10.1042/bst0311330.

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Iron and manganese superoxide dismutases are phylogenetically closely related. They are compared by in silico analysis with regard to their metal specificity and their three-dimensional structure. Special attention is given to the structure and properties of superoxide dismutases from archaeal prokaryotes. The mechanism and the extreme thermostability of superoxide dismutase from Sulfolobus acidocaldarius are discussed on the basis of its high-resolution X-ray structure. An alternating-site mechanism and an evolutionary origin of superoxide dismutases under the environmental conditions on the early Earth are proposed.

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32

Canini, Antonella, Patrizia Albertano, Donatella Leonardi, Daniela Di Somma, and Maria Grilli Caiola. "Superoxide dismutase in cyanobacteria of the Baltic Sea." Algological Studies/Archiv für Hydrobiologie, Supplement Volumes 83 (December 19, 1996): 129–43. http://dx.doi.org/10.1127/algol_stud/83/1996/129.

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33

Battistoni, A. "Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1326–29. http://dx.doi.org/10.1042/bst0311326.

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Several bacterial pathogens possess sodC genes that encode periplasmic or membrane-associated Cu,Zn superoxide dismutases. Since professional phagocytes generate large amounts of reactive oxygen species to control the growth of invading micro-organisms, Cu,Zn superoxide dismutase might protect infectious bacteria from oxy-radical damage and facilitate their survival within the host. This idea has gained support from studies showing that sodC-null mutants of different bacteria are less virulent than their parental wild-type strains, and from the discovery that, despite apparent dispensability for growth under laboratory conditions, various pathogens (including several highly virulent Salmonella strains) possess multiple copies of sodC. Our studies indicate that Cu,Zn superoxide dismutase effectively protects bacteria from phagocytic killing, and that the role in infection of the redundant sodC genes may vary in distinct Salmonella enterica serovars. More unexpectedly, we have found that Cu,Zn superoxide dismutase also modulates bacterial survival within epithelial cells, where bacterial killing appears to be mediated by an NAD(P)H oxidase resembling the enzyme complex typical of phagocytes. Finally, a striking feature of Cu,Zn superoxide dismutases from bacterial pathogens is their apparent ability to exploit the structural versatility of the enzyme to modulate its function. In fact, several enzyme variants exhibit unique properties that may lead to the acquisition of novel specialized functions distinct from superoxide dismutation.

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34

Strålin, P., and S. L. Marklund. "Effects of oxidative stress on expression of extracellular superoxide dismutase, CuZn-superoxide dismutase and Mn-superoxide dismutase in human dermal fibroblasts." Biochemical Journal 298, no. 2 (March 1, 1994): 347–52. http://dx.doi.org/10.1042/bj2980347.

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To determine the effect of oxidative stress on expression of extracellular superoxide dismutase (EC-SOD), CuZn-SOD and Mn-SOD, two fibroblast lines were exposed for periods of up to 4 days to a wide concentration range of oxidizing agents: xanthine oxidase plus hypoxanthine, paraquat, pyrogallol, alpha-naphthoflavone, hydroquinone, catechol, Fe2+ ions, Cu2+ ions, buthionine sulphoximine, diethylmaleate, t-butyl hydroperoxide, cumene hydroperoxide, selenite, citiolone and high oxygen partial pressure. The cell lines were cultured both under serum starvation and at a serum concentration that permitted growth. Under no condition was there any evidence of EC-SOD induction. Instead, the agents uniformly, dose-dependently and continuously reduced EC-SOD expression. We interpret the effect to be due to toxicity. Enhancement of the protection against oxidative stress by addition of CuZn-SOD, catalase and low concentrations of selenite did not influence the expression of any of the SOD isoenzymes. Removal of EC-SOD from cell surfaces by heparin also did not influence SOD expression. Mn-SOD was moderately induced by high doses of the first 11 oxidants. Apart from reduction at high toxic doses, there were no significant effects on the CuZn-SOD activity by any of the treatments. Thus EC-SOD, previously shown to be profoundly influenced by inflammatory cytokines, was not induced by its substrate or other oxidants. In a similar fashion, Mn-SOD, previously shown to be greatly induced and depressed by cytokines, was only moderately influenced by oxidants. We suggest that the regulation of these SOD isoenzymes in mammalian tissues primarily occurs in a manner co-ordinated by cytokines, rather than as a response of individual cells to oxidants.

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35

Chen, Longyan, Yang Liu, Yonggang Zhang, Yanmin Zhang, Wei Wang, Hongyu Han, Chunyu Yang, and Xueqian Dong. "Superoxide dismutase ameliorates oxidative stress and regulates liver transcriptomics to provide therapeutic benefits in hepatic inflammation." PeerJ 11 (August 11, 2023): e15829. http://dx.doi.org/10.7717/peerj.15829.

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Background Oxidative stress refers to the imbalance between oxidants and antioxidants in organisms and often induces hepatic inflammation. Supplementing exogenous superoxide dismutase is an effective way to alleviate oxidative stress; however, the effects and mechanisms by which superoxide dismutase alleviates hepatic inflammation remain unclear. Methods This study established a Kunming mouse model to verify and investigate the oxidative stress and hepatic inflammation-alleviating effects of the superoxide dismutase oral supplement that was prepared by our research group in a previous study. Results The superoxide dismutase product significantly restored the body weight and liver alanine transaminase, aspartate aminotransferase, superoxide dismutase, catalase, glutathione, and glutathione peroxidase levels of oxidative stress induced mice. Moreover, exogenous superoxide dismutase significantly inhibited interleukin 1β and interleukin 6 mRNA expression in the livers of mice with hepatic inflammation. Transcriptomic analysis indicated that superoxide dismutase had a significant inhibitory effect on Endog expression, alleviating oxidative stress damage, and mediating liver cell apoptosis by regulating the expression of Rab5if, Hnrnpab, and Ifit1. Conclusion Our research verified the oxidative stress remediation effects of superoxide dismutase and its therapeutic role against hepatic inflammation. This study can lay a foundation for investigating the mechanism by which superoxide dismutase alleviates hepatic disease.

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36

Jeon, Byeong-Wook, Byung-Hak Kim, Yun-Sang Lee, Sung-Sub Kim, Jong-Bok Yoon, and Tae-Yoon Kim. "Inactive extracellular superoxide dismutase disrupts secretion and function of active extracellular superoxide dismutase." BMB Reports 44, no. 1 (January 31, 2011): 40–45. http://dx.doi.org/10.5483/bmbrep.2011.44.1.40.

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37

Dreyer, Thomas, Martin Ottesen, and Aase Hvidt. "Hydrogen-deuterium exchange in yeast Cu2,Zn2-superoxide dismutase and apo-superoxide dismutase." Carlsberg Research Communications 51, no. 3 (January 1986): 219–26. http://dx.doi.org/10.1007/bf02907326.

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38

Nakane, Hiroshi, Yi Chu, Frank M. Faraci, Larry W. Oberley, and Donald D. Heistad. "Gene Transfer of Extracellular Superoxide Dismutase Increases Superoxide Dismutase Activity in Cerebrospinal Fluid." Stroke 32, no. 1 (January 2001): 184–89. http://dx.doi.org/10.1161/01.str.32.1.184.

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39

Novelli, Ethel L. B., Ney L. Rodrigues, Bartolomé O. Ribas, and Paulo R. Curi. "Intratracheal injection of nickel chloride and copper–zinc superoxide dismutase activity in lung of rats." Canadian Journal of Physiology and Pharmacology 70, no. 5 (May 1, 1992): 709–11. http://dx.doi.org/10.1139/y92-091.

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Superoxide radical [Formula: see text] is a free radical that may be involved in various toxic processes. Cu–Zn superoxide dismutase catalyses the dismutation of the superoxide free radical and protects cells from oxidative damage, and it has been used clinically. The concentration of Ni2+ and Cu–Zn superoxide dismutase activity were measured in lungs of rats at time intervals of 5, 12, 19, 26, 33, and 40 days following an intratracheal injection of 127 nmol of NiCl2. Nickel chloride increased nickel content and resulted in a significant increase of Cu–Zn superoxide dismutase activity in lungs. This elevation of Cu–Zn superoxide dismutase activity was highest on the 12th day (approximately threefold) and is at levels comparable to controls rats on day 40 onwards. Since Cu–Zn superoxide dismutase activity was increased in lung throughout our experimental period without corresponding increases of Cu2+ and Zn2+, we speculate that the elevation of Cu–Zn superoxide dismutase activity might be due to an increased half-life of the enzyme, induced by nickel.Key words: nickel chloride, intratracheal, Cu–Zn superoxide dismutase, lung.

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40

Beissenhirtz, Moritz K., Frieder W. Scheller, Maria S. Viezzoli, and Fred Lisdat. "Engineered Superoxide Dismutase Monomers for Superoxide Biosensor Applications." Analytical Chemistry 78, no. 3 (February 2006): 928–35. http://dx.doi.org/10.1021/ac051465g.

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41

Park, Eun-Jeong, Haeng-Soon Lee, Suk-Yoon Kwon, Kwan-Sam Choi, and Sang-Soo Kwak. "Transgenic Tomato Plants That Overexpress Superoxide Dismutase in Fruits." Journal of Plant Biotechnology 29, no. 1 (March 1, 2002): 7–13. http://dx.doi.org/10.5010/jpb.2002.29.1.007.

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42

Holovská, K., V. Lenártová, K. Holovská, and P. Javorský. "Characterization of superoxide dismutase in the rumen bacteriumStreptococcus bovis." Veterinární Medicína 47, No. 2 - 3 (March 30, 2012): 38–44. http://dx.doi.org/10.17221/5801-vetmed.

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Superoxide dismutase (SOD) isoenzymes of the rumen bacterium Streptococcus bovis 4/1 were studied. Native PAGE showed a single band of Mn-SOD, unaffected by 10 mM cyanide or 5 mM hydrogen peroxide under both aerobic and anaerobic growth conditions. When the metals were removed from the growth medium by Chelex 100, the addition of manganese increased enzymatic activity, while addition of iron inhibited SOD activity. Changes in Mn-SOD and glutathione peroxidase (GSHPx) activities evoked by paraquat and increased values of TBARS indicated that these enzymes were not able to sufficiently prevent oxidative stress at given paraquat concentrations.

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43

Vinita, Thakur. "Role of Superoxide Dismutase and Glutathione Peroxidase in Infertility." International Journal of Scientific Research 2, no. 11 (June 1, 2012): 353–54. http://dx.doi.org/10.15373/22778179/nov2013/112.

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44

Broide, Efrat, Elieser Klinowski, Rina Varsano, Jerachmiel Eshchar, Mehrdad Herbert, and Eitan Scapa. "Superoxide Dismutase Activity in Helicobacter pylori—Positive Antral Gastritis in Children." Journal of Pediatric Gastroenterology and Nutrition 23, no. 5 (December 1996): 609–13. http://dx.doi.org/10.1002/j.1536-4801.1996.tb00351.x.

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SummaryReactive oxygen metabolites have been implicated in gastric mucosal injuries. Superoxide dismutase, a scavenger of superoxide radical, is a key enzyme in gastric mucosal protection against several damaging factors. This study was aimed at investigating the relationship of superoxide dismutase activity to Helicobacter pylori—induced antral gastritis in children. Two groups of 11 children each, one positive and the other negative for Helicobacter pylori, were studied. Biopsies from the antrum and corpus were obtained for evaluation of Helicobacter pylori by CLOtest and histology as well as for superoxide dismutase activity (cytochrome c method). Erythrocytic and serum superoxide dismutase levels were determined as well. Superoxide dismutase activity was significantly higher only in the antrum of children with Helicobacter pylori—induced antral gastritis. There was no significant difference in superoxide dismutase activity in the corpus, erythrocytes, or serum of both groups. These findings may suggest a pathogenic relationship between the presence of Helicobacter pylori and oxygen radicals in inducing antral mucosal injury.

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Bafana, Amit, Som Dutt, Sanjay Kumar, and Paramvir S. Ahuja. "Superoxide dismutase: an industrial perspective." Critical Reviews in Biotechnology 31, no. 1 (October 4, 2010): 65–76. http://dx.doi.org/10.3109/07388551.2010.490937.

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Peterson, Douglas A., Daniel C. Peterson, Stephen L. Archer, and E. Kenneth Weir. "Superoxide dismutase: an antireductant enzyme?" Biochemical Society Transactions 21, no. 2 (May 1, 1993): 88S. http://dx.doi.org/10.1042/bst021088s.

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Ohkuma, Noritaka, Shinobu Matsuo, Hajime Iizuka, and Akira Ohkawara. "Superoxide Dismutase in Epidermis (1)." Journal of Dermatology 14, no. 3 (June 1987): 218–23. http://dx.doi.org/10.1111/j.1346-8138.1987.tb03564.x.

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Kang, N. G., J. M. Lim, M. Y. Chang, S. G. Park, W. G. Cho, and S. Y. Choi. "Modified superoxide dismutase for cosmeceuticals." International Journal of Cosmetic Science 27, no. 5 (October 2005): 299. http://dx.doi.org/10.1111/j.0142-5463.2005.00278_1.x.

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Gibson, G., A. OʼGrady, M. Leader, and G. M. Murphy. "Superoxide dismutase and skin cancer." Melanoma Research 3 (September 1993): 19. http://dx.doi.org/10.1097/00008390-199309002-00066.

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Lee, Y. M., D. J. Friedman, and F. J. Ayala. "Superoxide dismutase: an evolutionary puzzle." Proceedings of the National Academy of Sciences 82, no. 3 (February 1, 1985): 824–28. http://dx.doi.org/10.1073/pnas.82.3.824.

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