scholarly journals Superoxide dismutase in Bacteroides fragilis and related Bacteroides species

1977 ◽  
Vol 6 (3) ◽  
pp. 280-284
Author(s):  
J Carlsson ◽  
J Wrethén ◽  
G Beckman
Keyword(s):  
Escherichia Coli ◽  
Superoxide Dismutase ◽  
Isoelectric Focusing ◽  
Specific Activity ◽  
Bacteroides Fragilis ◽  
Anaerobic Conditions ◽  
Sod Activity ◽  
Bacteroides Species ◽  
Bacteroides Ovatus ◽  
Escherichia Coli B

Superoxide dismutase (SOD) activity was demonstrated in cell-free extracts of Bacteroides fragilis, Bacteroides vulgatus, Bacteroides distasonis, Bacteroides ovatus, and Bacteroides thetaiotaomicron. The strains were grown under anaerobic conditions in Trypticase soy broth, and the specific activity of SOD in the extracts was, in most strains, higher than in cell-free extracts of Escherichia coli B grown under anaerobic conditions. Isoelectric focusing of the extracts in polyacrylamide gel demonstrated distinct forms of SOD in the different species.

scholarly journals Developmental regulation of rat lung Cu,Zn-superoxide dismutase

1987 ◽  
Vol 246 (3) ◽  
pp. 697-703 ◽  
Author(s):  
M A Hass ◽  
D Massaro
Keyword(s):  
Superoxide Dismutase ◽  
Half Life ◽  
Specific Activity ◽  
Developmental Regulation ◽  
Progressive Increase ◽  
Enzyme Synthesis ◽  
Enzyme Activation ◽  
Sod Activity ◽  
Adult Rats ◽  
Copper Chelation

In the present investigation we found that lung Cu, Zn-superoxide dismutase (SOD) activity (units/mg of DNA) increases steadily in the rat from birth to adulthood. The specific activity (units/micrograms of enzyme) of Cu, Zn-SOD was unchanged from birth to adulthood, excluding enzyme activation as a mechanism responsible for the increase in enzyme activity. Lung synthesis of Cu, Zn-SOD peaked at 1 day before birth and decreased thereafter to adult values. Calculations, based on rates of Cu, Zn-SOD synthesis and the tissue content of the enzyme, indicated that lung Cu, Zn-SOD activity increased during development owing to the rate of enzyme synthesis exceeding its rate of degradation by 5-10%. These calculations were supported by measurements of enzyme degradation in the neonatal (half-life, t1/2, = 12 h) and adult lung (t1/2 = greater than 100 h); the difference in half-life did not reflect the rates of overall protein degradation in the lung, since these rates were not different in lungs from neonatal and adult rats. We did not detect differences in the Mr or pI of Cu, Zn-SOD during development, but the susceptibility of the enzyme to inactivation by heat or copper chelation decreased with increasing age of the rats. We conclude that the progressive increase in activity of Cu, Zn-SOD is due to a rate of synthesis that exceeds degradation of the enzyme. The data also suggest that increased stabilization of enzyme conformation accounts for the greater half-life of the enzyme in lungs of adult compared with neonatal rats.

Further investigation of the mechanism of Vitreoscilla hemoglobin (VHb) protection from oxidative stress in Escherichia coli

Biologia ◽  
2011 ◽  
Vol 66 (5) ◽  
Author(s):  
Meltem Akbas ◽  
Tugrul Doruk ◽  
Serhat Ozdemir ◽  
Benjamin Stark
Keyword(s):  
Oxidative Stress ◽  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Stationary Phase ◽  
Exponential Phase ◽  
Vitreoscilla Hemoglobin ◽  
Sod Activity ◽  
E Coli ◽  
Hydrogen Peroxide Treatment

AbstractIn Escherichia coli, Vitreoscilla hemoglobin (VHb) protects against oxidative stress, perhaps, in part, by oxidizing OxyR. Here this protection, specifically VHb-associated effects on superoxide dismutase (SOD) and catalase levels, was examined. Exponential or stationary phase cultures of SOD+ or SOD− E. coli strains with or without VHb and oxyR antisense were treated with 2 mM hydrogen peroxide without sublethal peroxide induction, and compared to untreated control cultures. The hydrogen peroxide treatment was toxic to both SOD+ and SOD− cells, but much more to SOD− cells; expression of VHb in SOD+ strains enhanced this toxicity. In contrast, the presence of VHb was generally associated in the SOD+ background with a modest increase in SOD activity that was not greatly affected by oxyR antisense or peroxide treatment. In both SOD+ and SOD− backgrounds, VHb was associated with higher catalase activity both in the presence and absence of peroxide. Contrary to its stimulatory effects in stationary phase, in exponential phase oxyR antisense generally decreased VHb levels.

Superoxide dismutase isoelectric focusing patterns as a tool to differentiate pathotypes of Globodera spp.

Nematology ◽  
2010 ◽  
Vol 12 (5) ◽  
pp. 751-758 ◽  
Author(s):  
Sergio Molinari ◽  
Nicola Greco ◽  
Miloslav Zouhar
Keyword(s):  
Cluster Analysis ◽  
Superoxide Dismutase ◽  
Isoelectric Focusing ◽  
Cyst Nematode ◽  
Globodera Pallida ◽  
Data Matrix ◽  
Sod Activity ◽  
Isozyme Electrophoresis ◽  
Fourth Group ◽  
High Level

Abstract Isoelectric focusing was used to separate proteins from cyst extracts of potato cyst nematode (PCN) populations. In a first set of assays, cyst extracts from standard populations of Globodera rostochiensis pathotypes Ro1, Ro2, Ro3, Ro2/3, Ro4, and Ro5, and G. pallida pathotypes Pa2 and Pa3, were loaded on isoelectric focusing gels. Gels were stained for superoxide dismutase (SOD), esterase, and glucose-6-phosphate isomerase (GPI). Twelve bands of SOD activity were detected, six (B1-B6) migrating towards the basic zone and the other six (A1-A6) migrating towards the acidic zone, starting from the loading point. A cluster analysis was carried out based on a data matrix that reported the presence or absence of SOD bands on the isozyme electrophoresis patterns (IEPs). Globodera spp. were clearly distinguished and, within G. rostochiensis, Ro2 and Ro4 shared a high level of similarity, respectively, with Ro3 and Ro5; moreover, Ro1 could be clearly distinguished from Ro2/3 and Ro4/5. Globodera pallida Pa2 and Pa3 also shared a high level of similarity. In contrast, esterase and GPI IEPs did not discriminate among G. rostochiensis standard pathotypes. Subsequently, 14 field populations of G. rostochiensis, five from Italy and nine from Venezuela, and three field populations of G. pallida, two from Italy and one from Chile, were assayed to obtain SOD IEPs. Italian populations had previously been identified at pathotype level by bioassays according to the generally accepted international test using different resistant potato cultivars and clones. The cluster analysis carried out on the SOD IEPs of all the populations tested formed four distinct groups within G. rostochiensis and only one within G. pallida. Pathotype identification of Globodera populations by SOD IEPs was not able to discriminate between bioassay standard couples Ro2/Ro3, Ro4/Ro5 and Pa2/Pa3. Therefore, three groups were assigned to Ro1, Ro2/3 and Ro4/5, and a fourth group to Pa2/Pa3. Four Venezuelan populations, not identified at pathotype level by bioassays, formed a distinct fifth group. By means of the method described herein, four additional unknown Venezuelan populations could be assigned to Ro1 group and one to Ro2/Ro3 group; one G. pallida population from Chile was assigned to Pa2/Pa3 group.

Alpha 1-adrenergic stimulation induces cardiac tolerance to hypoxia via induction and activation of Mn-SOD

1996 ◽  
Vol 271 (4) ◽  
pp. H1356-H1362 ◽  
Author(s):  
N. Yamashita ◽  
M. Nishida ◽  
S. Hoshida ◽  
J. Igarashi ◽  
M. Hori ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Creatine Kinase ◽  
Cardiac Myocytes ◽  
Total Protein ◽  
Manganese Superoxide Dismutase ◽  
Specific Activity ◽  
Adrenergic Stimulation ◽  
Sod Activity ◽  
Manganese Superoxide ◽  
Tolerance To Hypoxia

We examined whether or not alpha 1-adrenergic stimulation increases the tolerance of the heart to ischemia using a hypoxia-reoxygenation model of cardiac myocytes. After exposure to norepinephrine (NE; 0.2 microM) for 24 h, the manganese superoxide dismutase (Mn-SOD) content and activity in the cells were increased from 0.61 +/- 0.03 to 0.87 +/- 0.04 microgram/dish and 22 +/- 1 to 55 +/- 4 U/dish, respectively. The specific activity of Mn-SOD was also increased from 36 to 63 U/microgram Mn-SOD protein after the stimulation with NE. Prazosin (2 microM) abolished the increase in Mn-SOD activity (U/mg total protein). Creatine kinase (CK) release after hypoxia (PO2 7 mmHg; 3 h)-reoxygenation (1 h) from cells pretreated with NE in the presence of propranolol and yohimbine for 24 h was attenuated by 48% compared with that from cells without NE stimulation. When antisense oligodeoxyribonucleotides to Mn-SOD were added to myocyte cultures, the increase in Mn-SOD activity (U/mg total protein) and the attenuation of CK release after the addition of NE in the presence of propranolol and yohimbine were not observed. These results suggest that alpha 1-adrenergic stimulation increases the tolerance of myocytes to hypoxia through induction and activation of Mn-SOD.

scholarly journals Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp

2004 ◽  
Vol 69 (1) ◽  
pp. 9-16 ◽  
Author(s):  
Svetlana Seatovic ◽  
Ljubinka Gligic ◽  
Zeljka Radulovic ◽  
Ratko Jankov
Keyword(s):  
Molecular Weight ◽  
Superoxide Dismutase ◽  
Specific Activity ◽  
Thermophilic Bacteria ◽  
Noncovalent Interactions ◽  
Gel Filtration ◽  
Antioxidant Defense System ◽  
Exchange Chromatography ◽  
Gel Chromatography ◽  
Sod Activity

Superoxide dismutase (SOD; EC 1.15.1.1), a high molecular weight component of the antioxidant defense system, provided promising results in the treatment of oxidative damage. Thermothrix sp., isolated from thermal spa water in Serbia, showed high superoxide dismutase activity. The SOD, from cell free extract, was purified to homogenity by ammonium sulfate precipitation, Sephadex G 75 gel filtration chromatography and QAE Sephadex ion exchange chromatography. The specific activity of the purified enzyme was 9191 U/mg. The purified enzyme was analyzed and partially characterized. SOD was localized in polyacrylamide gel by activity staining, based on the reduction of nitroblue tetrazolium (NBT) by superoxide. The enzyme molecular weight determined by gel chromatography is 37 kD. According to SDS PAGE it is composed of two subunits of equal size, joined by noncovalent interactions. The isoelectric point, assessed by isoelectric focusing is 5.3. The optimum pH for enzyme activity was in the range of 8 to 10. The optimum temperature for SOD activity was 60 ?C. After one hour of incubation at 40, 50 and 60 ?C the SOD activity increases, but at 80 ?C, the SOD is denaturated. After 24 hours of incubation at 25 ?C SO Dactivity only slightly decreases.

scholarly journals Thermal stability of purified superoxide dismutase from liver of commercially valuable fish, Labeo rohita Exposed to Pb+Cr mixture

2021 ◽  
Vol 58 (04) ◽  
pp. 1191-1196
Author(s):  
Huma Naz
Keyword(s):  
Superoxide Dismutase ◽  
Specific Activity ◽  
Labeo Rohita ◽  
Maximum Activity ◽  
Exchange Chromatography ◽  
Sod Activity ◽  
Exposed Fish ◽  
Ammonium Sulphate Precipitation ◽  
Km Value ◽  
Increasing Temperature

In this experiment, effect of lead (Pb) + chromium (Cr) mixture on superoxide dismutase (SOD) in the liver of Labeo rohita at a concentration of 11.1 mgL-1 was observed. The ammonium sulphate precipitation and ion exchange chromatography techniques were successfully used to purify SOD. After purification, SOD activity of control and Pb+Cr treated fish was noted as 581.00 and 645.45 UmL-1, respectively while the specific activity was 1383.33 and 1613.62 Umg-1, respectively. The fold purification value of SOD was 2.75 and 2.45 for control and stressed fish, respectively. The recovery was calculated as 77.06 and 57.43% for control and stressed fish, respectively. The results of kinetic characterization showed that SOD form control and exposed fish had maximum activity at pH 6.5 and 7.0. Temperature also had a significant effect on activity of SOD. The SOD activity was measured maximum at 30°C for both control and Pb+Cr exposed fish. The Km value of liver SOD for control and Pb+Cr treated L. rohita was calculated as 1.48 and 0.62 mM, respectively. The value of Vmax for SOD from liver of control and Pb+Cr exposed fish was 1000 and 570 U mL-1, respectively. The enthalpy of denaturation (∆H*) for liver SOD from control and Pb+Cr exposed L. rohita was computed as 3.492 and 2.802 KJ mol-1 at 40°C, respectively and these values were dropped off with increasing the temperature until it remains 3.251 and 2.561 KJ mol-1 at 70°C, respectively. The free energy of thermal denaturation (ΔGº) of liver SOD was slightly increased with increasing temperature until 75°C which shows its resistance against heat. The values of ΔGº was observed as 58.03 and 57.95 KJ mol-1 for control and exposed fish at 40°C, respectively while the same was increased upto 62.37 and 62.00 KJ mol-1 at 70°C, respectively. It was concluded from negative value of ΔS* (entropy of inactivation) that the SOD is stable thermodynamically.

scholarly journals Molecular Cloning and Nucleotide Sequence of the Superoxide Dismutase Gene and Characterization of Its Product fromBacillus subtilis

1998 ◽  
Vol 180 (14) ◽  
pp. 3697-3703 ◽  
Author(s):  
Takashi Inaoka ◽  
Yoshinobu Matsumura ◽  
Tetsuaki Tsuchido
Keyword(s):  
Superoxide Dismutase ◽  
Stationary Phase ◽  
Specific Activity ◽  
Upstream Region ◽  
Gene Encoding ◽  
Sod Activity ◽  
Vegetative Cells ◽  
Reading Frame ◽  
Superoxide Dismutase Gene

ABSTRACT Bacillus subtilis was found to possess one detectable superoxide dismutase (Sod) in both vegetative cells and spores. The Sod activity in vegetative cells was maximal at stationary phase. Manganese was necessary to sustain Sod activity at stationary phase, but paraquat, a superoxide generator, did not induce the expression of Sod. The specific activity of purified Sod was approximately 2,600 U/mg of protein, and the enzyme was a homodimer protein with a molecular mass of approximately 25,000 per monomer. The gene encoding Sod, designatedsodA, was cloned by the combination of several PCR methods and the Southern hybridization method. DNA sequence analysis revealed the presence of one open reading frame consisting of 606 bp. Several putative promoter sites were located in the upstream region ofsodA. The deduced amino acid sequence showed high homology with other bacterial manganese Sods. Conserved regions in bacterial manganese Sod could also be seen. The phenotype of double mutantEscherichia coli sodA sodB, which could not grow in minimal medium without supplemental amino acids, was complemented by the expression of B. subtilis sodA.

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