• Journal of Periodontal and Implant Science
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• v.25 no.2
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• pp.222-238
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• 1995

Inflammatory cells may produce active species of oxygen in antimicrobial defense. While such species can directly damage surrounding tissue, their major secondary role may be to mediate important components of the inflammatory response. Superoxide dismutase, antioxidant, have significant anti-inflammatory properties in rheumatoid arthritis, ischemic tissue injury and gastrointestinal disease. Increased oxidative product formation diseases. And superoxide dismutase produced by Porphyromonas Gingivalis is resistant to killing by polymorphonuclear leukocyte. The purpose of this study was to investigate on the effects of superoxide dismutase in 3T3 fibroblast and in experimental gingivitis in the rats. The effect of superoxide dismutase(SOD) to cell morphology and cell activity was measured in cultured mouse 3T3 fibroblast. After experimental gingivitis were induced by lipopolysaccharide(LPb) and bovine serum albumin(BSA), injection of SOD were done. WBC count and histologic findings were observed at 1, 2, 3, and 7 days. The results were as follows; 1. There was a little difference between LPS treated groups and SOD treated groups in 3T3 fibroblast morpholoy. 2. There was no difference between only SOD treated groups (except SOD 150U at 3days) and control in 3T3 fibroblast activity. 3. LPS $0.5{\mu}g/ml$ and SOD treated groups (except 150U) had decreased 3T3 fibroblast activity and no significant difference at 3 days. 4. LPS $5.0{\mu}g/ml$ and SOD treated groups were significantly increased cell activity of 3T3 fibroblast than control group at 1 day(P<0.05). 5. In LPS induced gingivitis, the number of leukocytes in SOD treated was significantly decreased than in saline treated at 1 day(P<0.05). 6. In histopathologic findings of LPS or BSA induced gingivitis, inflammatorycell infiltration in SOD treated groups were less than in saline treated group at 1, 2 and 3 days.

• BMB Reports
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• v.36 no.3
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• pp.282-287
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• 2003

The production of superoxide dismutase (SOD) varied in Deinococcus radiophilus, the UV resistant bacterium, depending upon different phases of growth, UV irradiation, and superoxide treatment. A gradual increase in total SOD activity occurred up to the stationary phases. The electrophoretic resolution of the SOD in cell extracts of D. radiophilus at each growth phase revealed the occurrence of MnSOD throughout the growth phases. The SOD profiles of D. radiophilus at the exponential phase received oxidative stress by the potassium superoxide treatment or UV irradiation also revealed the occurrence of a single SOD. However, these treatments caused an increase in SOD activity. The data strongly suggest that D. radiophilus has only one species of SOD as a constitutive enzyme, which seems to be a membrane-associated protein.

• Applied Biological Chemistry
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• v.43 no.1
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• pp.46-51
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• 2000

The resistance of Cornyza bonariensis to herbicide paraquat was investigated by evaluating the activities of three enzymes concerning in scavenging paraquat-generated toxic oxygen species such as superoxide radical and hydrogen peroxide in resistant and susceptible biotypes. Conyza bonariensis inhabited in cultivated area was more tolerant to paraquat than that of uncultivated area. This is the first report that a biotype of Cornyza bonariensis has appeared in an area with repeated paraquat treatments of Korea. Superoxide dismutase activity of resistant biotype was 20% higher as 150 than that of susceptible biotype. Ascorbate peroxidase activity of resistant biotype was 44% higher than that of susceptible biotype. Glutathione reductase activity of resistant biotype was 64% higher than that of susceptible biotype. It can be concluded from above results that the resistance of Conyza bonariensis to paraquat depends partially on the toxic oxygen species-scavenging efficiency of protective multienzymatic system which is composed of three enzymes, superoxide dismutase, ascorbate peroxidase, and glutathione reductase.

• Journal of Food Hygiene and Safety
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• v.16 no.1
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• pp.41-47
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• 2001

The purpose of this study was to elucidate the effects of green tea catechins (GTC) on the lipid peroxidation and superoxide dismutase (SOD). GTC showed the high SOD activity, while sitgnificantly inhibited the peroxide value of linoleic acid (93%) and lipid peroxidation (84%) from rat liver microsomal fraction induced by Fe$^{2+}$ascorbate system. The effects of GTC on the SOD and catalase activities, and lipid peroxidation after oral administration were investigated. GTC (50 mg/kg) significantly increased SOD (62%) and catalase activities (75%), while significantly inhibited the lipid peroxidation (52%) of rat liver microsome in a dose-dependent manner. These results suggest that GTC has the antioxidative effect which is rotated to the prevention of aging and cancer.r.

• International Journal of Industrial Entomology and Biomaterials
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• v.9 no.2
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• pp.225-228
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• 2004

Superoxide dismutase (SOD) is an important enzyme which catalyzes superoxide radicals to hydrogen peroxide. A Cu, Zn sod-like gene was found in Bombyx mori nuclear polyhedrosis virus encoding 151 amino acids. To demonstrate its function, a recombinant virus named dsBmNPV with deleted sod gene was constructed. It was discovered that the sod gene was not essential for viral replication. Studies on growth of budded virus in BmN cells and superoxide dismutase and catalase activities in vivo after dsBmNPV infection showed that the titer of dsBmNPV decreased obviously comparing to wild type BmNPV, the sod gene was effective on genomic DNA replication of baculovirus, the peak of SOD activity of silkworm infected with wt-BmNPV appeared between 36 and 48 hrs post infection, and with dsBmNPV, it did not appear. And the changes of CAT activity after infection were similar to SOD activity.

• Journal of Microbiology and Biotechnology
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• v.17 no.8
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• pp.1399-1402
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• 2007

The virulence of superoxide dismutase (SOD) mutants of Vibrio vulnificus, as tested by intraperitoneal injection into mice, decreases in the order of sodC mutant, sodA mutant, and sodB mutant lacking CuZnSOD, MnSOD, and FeSOD, respectively. The survival of SOD mutants under superoxide stress also decreases in the same order. The virulence of soxR mutant, which is unable to induce MnSOD in response to superoxide, is similar to that of the sodA mutant, as the survival of the soxR mutant under superoxide stress is similar to that of the sodA mutant. Consistently, the lowered survival of the soxR mutant is complemented not only with soxR but also with sodA. Thus, the virulence of V. vulnificus is significantly affected by the cellular level of SOD activity, and an increase in SOD level through MnSOD induction by SoxR under superoxide stress is essential for virulence.

• Korean Journal of Microbiology
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• v.52 no.2
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• pp.230-235
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• 2016

This study was carried out to analyze the differences in enzyme activity and stability between the native Fe superoxide dismutase (FeSOD) and the 6xHis-tagged superoxide dismutase (6xHis-FeSOD) of Streptomyces subrutilus P5. The optimum pHs for both native FeSOD and 6xHis-FeSOD were 7, while the pH range of the activity was narrower for the 6xHis-FeSOD. The native FeSOD was stable at pH 4-9, but the 6xHis-FeSOD lost its stability at pH > 9. The temperatures of the optimum activities were same for both types of enzymes. However, the heat stability of the 6xHis-FeSOD was clearly decreased; even at $20^{\circ}C$ the enzyme lost the activity after 360 min. In contrast, the native FeSOD was stable after 720 min at below $40^{\circ}C$. $H_2O_2$ inhibition was occurred already at 0.5 mM for the 6xHis-tagged enzyme. Therefore, from the results that the 6xHis-FeSOD retained the enzyme activity at pH 6-7 and $20-40^{\circ}C$, it can be assumed that the protein structure became destabilized under different storage conditions and sensitive to the enzyme inhibitor.

• Korean Journal of Veterinary Research
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• v.38 no.2
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• pp.273-279
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• 1998

The ability of bovine intact red blood cells to scavenge superoxide and hydrogen peroxide by superoxide dismutase, catalase and glutathione peroxidase was investigated. Intact red cells(up to 0.4%) suspensions did not inhibit ferricytochrome c reduction by superoxide in the superoxide generating system. On the other hand, intact red cell(0.4%) suspensions almost completely inhibit ferrocytochrome c oxidation by hydrogen peroxide. The ability of intact red cells to scavenge hydrogen peroxide was mainly attributed to either membrane bound catalase or glutathione peroxidase. The scavenge of hydrogen peroxide by 0.1~0.2% intact red cells showed a trend of dependence on mainly glutathione peroxidase. However, at blood cell concentration higher than 0.3%, the process depended upon peroxidase-independent scavengers like catalase. Enhancement of ferrocytochrome c oxidation by red cells treated with aminotriazole proved that the protection against hydrogen peroxide was due to catalase, while the protection in the presence of glutathione indicated scavenging effect of glutathione peroxidase against hydrogen peroxide.

• Journal of Ginseng Research
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• v.21 no.3
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• pp.153-159
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• 1997

Living organisms have antioxidant enzymes, such as superoxide dismutase, catalase SE glutathione peroxidase, that protect themselves from the toxic effect of superoxide free radicals. Some report says that intracellular oxidation stress is involved in pathogenesis of chronic complications of diabetes mellitus. This study was performed to evaluate the effect of red ginseng on lipid peroxidation of red blood cell and antioxidant SOD activity of serum in NIDDM patients. As a result, there were trends for decrease of lipid peroxidases of RBC and Increase of SOD activity of serum in ginseng group but that were not statistically significant. Therefore, we suggest long term and large sized control study is necessary to confirm the protective effects of red ginseng on oxidative damage in NIDDM patients.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.732-736
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• 1999

The superoxide dismutase (SOD) in Lactococcus lactis was measured quantitatively and qualitatively under various culture conditions. The L. lactis SOD was induced by oxidative stress. As the concentration of paraquat to produce superoxide radicals increased, the growth of L. lactis decreased with concomitant increase of SOD activity. The SOD activity was found to be growth-phase dependent: when aerobically grown cells entered to the stationary phase, the activity increased gradually until the late stationary phase. From inhibition studies, L. lactis SOD was found to be insensitive to KCN and $H_2O_2$ which are known to inhibit Cu/ZnSOD and FeSOD, respectively. Moreover, as the concentration of manganese in the medium increased, the activity of SOD also increased. These data strongly suggested that L. lactis possessed a single manganese-containing SOD (MnSOD). Finally, a putative sod gene fragment of 510 bp was identified in L. lactis using a polymerase chain reaction (PCR) with degenerate primers designed from the deduced DNA sequences of known SOD genes.