scholarly journals Superoxide dismutase, catalase, and peroxidase in ammonium-grown and nitrogen-fixing Azospirillum brasilense

1984 ◽  
Vol 30 (10) ◽  
pp. 1222-1228 ◽  
Author(s):  
Richard W. Clara ◽  
Roger Knowles
Keyword(s):  
Superoxide Dismutase ◽  
Electron Acceptor ◽  
Azospirillum Brasilense ◽  
Polyacrylamide Gel Electrophoresis ◽  
Growth Conditions ◽  
Sod Activity ◽  
Batch Cultures ◽  
Physiological Conditions ◽  
Azospirillum Brasilense Sp7 ◽  
In Cells

Superoxide dismutase (SOD), catalase (CAT), and peroxidase (PER) activities were studied in ammonium-grown and N2-fixing batch cultures of Azospirillum brasilense Sp7. PER activity, as measured using o-dianisidine or 3,3′-diaminobenzidine as the H donor, was not significant in most growth conditions. SOD activity increased in response to higher O2 concentrations but was also present in cells grown anaerobically with nitrate [Formula: see text] or nitrous oxide (N2O) as electron acceptor. CAT activity increased at lower O2 concentrations and was highest in cells grown anaerobically with [Formula: see text] as electron acceptor. Polyacrylamide gel electrophoresis of cell-free extracts revealed only one band of SOD activity under each of the physiological conditions employed, compared with three for aerobically grown Escherichia coli K12. This band proved to be iron-containing SOD (FeSOD) on the basis of inhibitor sensitivity.

scholarly journals Phasin PhaP1 is involved in polyhydroxybutyrate granules morphology and in controlling early biopolymer accumulation in Azospirillum brasilense Sp7

AMB Express ◽  
2019 ◽  
Vol 9 (1) ◽  
Author(s):  
María de los Angeles Martínez-Martínez ◽  
Bertha González-Pedrajo ◽  
Georges Dreyfus ◽  
Lucía Soto-Urzúa ◽  
Luis Javier Martínez-Morales
Keyword(s):  
Azospirillum Brasilense ◽  
C:N Ratio ◽  
Growth Conditions ◽  
Low Oxygen ◽  
Rt Pcr ◽  
Transmission Electron ◽  
Azospirillum Brasilense Sp7 ◽  
Plant Growth Promoting ◽  
Growth Promoting

Abstract Phasins are amphiphilic proteins involved in the regulation of the number and size of polyhydroxybutyrate (PHB) granules. The plant growth promoting bacterium Azospirillum brasilense Sp7 accumulates high quantities of bioplastic PHB as carbon and energy source. By analyzing the genome, we identified six genes that code for proteins with a Phasin_2 domain. To understand the role of A. brasilense Sp7 PhaP1 (PhaP1Abs) on PHB synthesis, the phaP1 gene (AMK58_RS17065) was deleted. The morphology of the PHB granules was analyzed by transmission electron microscopy (TEM) and the PHB produced was quantified under three different C:N ratios in cultures subjected to null or low-oxygen transfer. The results showed that PhaP1Abs is involved in PHB granules morphology and in controlling early biopolymer accumulation. Using RT-PCR it was found that phasin genes, except phaP4, are transcribed in accordance with the C:N ratio used for the growth of A. brasilense. phaP1, phaP2 and phaP3 genes were able to respond to the growth conditions tested. This study reports the first analysis of a phasin protein in A. brasilense Sp7.

A heat-stable Cu/Zn superoxide dismutase from the viscera of sardinelle (Sardinella aurita): purification and biochemical characterization

Biologia ◽  
2014 ◽  
Vol 69 (12) ◽  
Author(s):  
Hayet Ben Khaled ◽  
Naourez Ktari ◽  
Rayda Siala ◽  
Noomen Hmidet ◽  
Ahmed Bayoudh ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Sequence Similarity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Native Enzyme ◽  
Sod Activity ◽  
Sardinella Aurita

AbstractSuperoxide dismutase (SOD) is an enzyme that protects against oxidative stress from superoxide radicals in living cells. This enzyme was extracted from sardinelle (Sardinella aurita) viscera, purified and characterized. The Cu/Zn-SOD was purified to homogeneity by the three-step procedure consisting of the heating at 65°C for 15 min, precipitation with ammonium sulphate (30–60%, w/v) and Sephadex G-100 gel filtration with a 7.17-fold increase in specific activity. The molecular weight of the native enzyme was estimated to be 40 kDa by G-125 gel filtration on HPLC column and that of the subunit mass, deduced by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, was 20 kDa. Thus the native enzyme appeared to be a homodimer. The optimum pH and temperature for the purified SOD activity were determined to be pH 7.0 and 40°C, respectively. It retained more than 85% of its initial activity after 1 h of incubation at 50°C. The enzyme had a broad stability pH range of 6.0–9.0. The N-terminal sequence of the purified enzyme was VLKAVCVLKGTGEVT. This sequence exhibited a high degree of sequence similarity with other fish Cu/Zn SODs.

Cytochrome content in Azospirillum brasilense Sp 7 grown under aerobic and denitrifying conditions

1987 ◽  
Vol 33 (2) ◽  
pp. 151-156 ◽  
Author(s):  
Roger Lalande ◽  
Roger Knowles
Keyword(s):  
Electron Acceptor ◽  
Azospirillum Brasilense ◽  
Nitrate Reductase Activity ◽  
Soluble Fraction ◽  
Reductase Activity ◽  
Batch Cultures ◽  
Final Electron ◽  
Cytochrome Content ◽  
Soluble C ◽  
Final Electron Acceptor

Azospirillum brasilense Sp 7 was grown in batch cultures with O2, [Formula: see text], [Formula: see text], or N2O as final electron acceptor. There were marked differences in cytochrome composition depending on the O2 status of the culture and the electron acceptor utilized. Highly aerated cultures showed no [Formula: see text] reduction and the cytochrome composition (a soluble c-type and particulate aa3, b, and c cytochromes) was not affected by the presence of[Formula: see text]. Under low aeration, in the presence of [Formula: see text], nitrate reductase activity occurred and there was a significant increase in the soluble and particulate cytochromes. Particulate cytochrome b-556 was observed only under high aeration and the cytochrome aa3, observed under both high and low aeration, decreased as the O2 concentration decreased. A particulate CO-binding cytochrome of type o was observed in the cells grown under high aeration. Cytochrome cd nitrite reductase was observed only in the soluble fraction of [Formula: see text]-grown cultures, which also contained the highest concentrations of the soluble cytochrome c-548 and the particulate c-551. N2O-grown cultures showed b-560 and c-551 cytochromes in the particulate and the c-548 cytochrome in the soluble fraction.

CuZn superoxide dismutase activities from Fasciola hepatica

Parasitology ◽  
1998 ◽  
Vol 117 (6) ◽  
pp. 555-562 ◽  
Author(s):  
L. PIACENZA ◽  
R. RADI ◽  
F. GOÑI ◽  
C. CARMONA
Keyword(s):  
Molecular Weight ◽  
Superoxide Dismutase ◽  
Fasciola Hepatica ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Exchange Chromatography ◽  
Soluble Extract ◽  
Sod Activity

The levels of superoxide dismutase (SOD) were determined in detergent-soluble, somatic and excretion–secretion (E–S) preparations from adult Fasciola hepatica using the xanthine oxidase system and visualized in substrate gels. Compared to detergent-soluble and somatic extracts, E–S products showed the highest SOD activity (88 ·5 U/mg), indicating active release to the medium in which parasites were maintained. SOD specific activity was also detected at high levels in E–S products from 3-week-old and 5-week-old immature migrating flukes (25 and 143 U/mg, respectively). In all preparations except for the somatic extract, the activity was characterized as cyanide-sensitive CuZn SOD. Differences in SOD isoenzyme profiles between the extracts were observed in native polyacrylamide gel electrophoresis: the somatic and detergent-soluble extracts exhibited 1 band of activity while the E–S products from immature and adults flukes contained 2 and 3 migrating bands, respectively. SOD was purified from the detergent-soluble extract and E–S products of adult worms by a combination of ultrafiltration, gel filtration on Sephacryl S-200 HR and ion-exchange chromatography on QAE Sephadex A-50. The SOD from detergent-soluble extract showed, by SDS–PAGE analysis, 1 band of 16 kDa apparent molecular weight. The SOD from E–S products showed 2 bands of 16 and 60 kDa apparent molecular weight. N-terminal sequence analysis of the 16 kDa band from the detergent-soluble preparation showed some similarity with Schistosoma mansoni cytoplasmic SOD. These enzymes may have a potential role in the evasion of the oxidative burst killing mechanism by immune cells.

The Influence of Different Growth Conditions on the Structure of the Bacterial Surface Glycopolymers of Azospirillum brasilense Sp7

2014 ◽  
Vol 14 (2) ◽  
pp. 55-61
Author(s):  
Stella Sergeevna Evstigneeva ◽  
◽  
Yana Vladimirovna Khalepa ◽  
Elena Nikolaevna Sigida ◽  
Yulia Petrovna Fedonenko ◽  
...  
Keyword(s):  
Azospirillum Brasilense ◽  
Growth Conditions ◽  
Bacterial Surface ◽  
Azospirillum Brasilense Sp7

An inducible iron-containing superoxide dismutase in Rhizobium japonicum

1981 ◽  
Vol 27 (11) ◽  
pp. 1202-1208 ◽  
Author(s):  
Mark D. Stowers ◽  
Gerald H. Elkan
Keyword(s):  
Superoxide Dismutase ◽  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Metal Content ◽  
Methyl Viologen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Rhizobium Japonicum ◽  
Growth Media ◽  
Sod Activity ◽  
Rhizobium Spp

Crude extracts of Rhizobium japonicum contained a single superoxide dismutase (SOD) as revealed by polyacrylamide gel electrophoresis. Rhizobium japonicum SOD was determined to be iron-containing by criteria of sensitivity to 5 mM H2O2 and 1 mM NaN3. Growth media strongly influenced SOD activity. The addition of methyl viologen to cultures of R. japonicum 61A76NS, growing in complex medium, caused induction of the enzyme. Yeast extract was essential for induction of SOD. Puromycin blocked the induction of the enzyme. Rhizobium spp. were surveyed for SOD activity, electrophoretic mobility on polyacrylamide gels, and metal content.

scholarly journals Superoxide dismutase activity and isoenzyme profiles in bulbs of snake's head fritillary in response to cold treatment

2010 ◽  
Vol 62 (3) ◽  
pp. 553-558 ◽  
Author(s):  
Sladjana Jevremovic ◽  
Marija Petric ◽  
Suzana Zivkovic ◽  
Milana Trifunovic ◽  
Angelina Subotic
Keyword(s):  
Superoxide Dismutase ◽  
Gel Electrophoresis ◽  
Cold Treatment ◽  
Growth Conditions ◽  
Superoxide Dismutase Activity ◽  
Sod Activity ◽  
Native Gel

The activities and isoenzyme profiles of superoxide dismutase (SOD) in in vitro Fritillaria meleagris bulbs in response to cold treatment (4?C) were investigated. Differences in SOD activity and isoenzyme profiles in bulbs under standard growth conditions, six weeks chilling, as well as seven days after the completion of cold treatment are presented. SOD activity initially decreased but then rapidly increased seven days after cold treatment. Four isoforms of SOD are active under standard and chilling conditions, while three isoforms are presented 7 days after cold treatment. Native gel electrophoresis indicated the presence of mitochondrial and chloroplast localized SODs. .

scholarly journals Characterization of superoxide dismutase in the rumen bacteriumStreptococcus bovis

2012 ◽  
Vol 47 (No. 2 - 3) ◽  
pp. 38-44 ◽  
Author(s):  
K. Holovská ◽  
V. Lenártová ◽  
K. Holovská ◽  
P. Javorský
Keyword(s):  
Superoxide Dismutase ◽  
Growth Conditions ◽  
Anaerobic Growth ◽  
Rumen Bacterium ◽  
Sod Activity ◽  
Native Page ◽  
Chelex 100 ◽  
Aerobic And Anaerobic Growth ◽  
Aerobic And Anaerobic

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.

10-gingerol induces oxidative stress through HTR1A in cumulus cells: in-vitro and in-silico studies

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Kiptiyah Kiptiyah ◽  
Widodo Widodo ◽  
Gatot Ciptadi ◽  
Aulanni’am Aulanni’Am ◽  
Mohammad A. Widodo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Culture ◽  
Superoxide Dismutase ◽  
In Silico ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
Sod Activity ◽  
In Silico Studies ◽  
Incubation Periods

AbstractBackgroundWe investigated whether 10-gingerol is able to induce oxidative stress in cumulus cells.MethodsFor the in-vitro research, we used a cumulus cell culture in M199, containing 10-gingerol in various concentrations (0, 12, 16, and 20 µM), and detected oxidative stress through superoxide dismutase (SOD) activity and malondialdehyde (MDA) concentrations, with incubation periods of 24, 48, 72, and 96 h. The obtained results were confirmed by in-silico studies.ResultsThe in-vitro data revealed that SOD activity and MDA concentration increased with increasing incubation periods: SOD activity at 0 µM (1.39 ± 0.24i), 12 µM (16.42 ± 0.35ab), 16 µM (17.28 ± 0.55ab), 20 µM (17.81 ± 0.12a), with a contribution of 71.1%. MDA concentration at 0 µM (17.82 ± 1.39 l), 12 µM (72.99 ± 0.31c), 16 µM (79.77 ± 4.19b), 20 µM (85.07 ± 2.57a), with a contribution of 73.1%. Based on this, the in-silico data uncovered that 10˗gingerol induces oxidative stress in cumulus cells by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.Conclusions10-gingerol induces oxidative stress in cumulus cells through enhancing SOD activity and MDA concentration by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.

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