scholarly journals Changes in Superoxide Dismutase Activity during Thidiazuron-induced Lateral Budbreak of Apple

HortScience ◽  
1991 ◽  
Vol 26 (9) ◽  
pp. 1202-1204 ◽  
Author(s):  
Shiow Y. Wang ◽  
Miklos Faust ◽  
Hong J. Jiao
Keyword(s):  
Superoxide Dismutase ◽  
Malus Domestica ◽  
Trace Amount ◽  
Rapid Expansion ◽  
Superoxide Dismutase Activity ◽  
Sod Activity ◽  
Cu And Zn

The effects of thidiazuron on changes in superoxide dismutase (SOD) activity in apple (Malus domestica Borkh cv. York Imperial) buds during dormancy break were determined. Dormant buds had low SOD activity. Increased SOD activity was correlated with budbreak induced by thidiazuron. Buds contained three distinct forms of SOD: Cu, Zn-SOD; Mn-SOD; and Fe-SOD. Most of the SOD activity in apple buds was attributed to Cu and Zn-SOD, followed by Mn-SOD. Iron-SOD was not present in dormant buds, and only a trace amount was found as buds started rapid expansion. Chemical name used: N-phenyl-N′-1,2,3,-thidiazol-5-ylurea (thidiazuron).

scholarly journals Differences in the Activity of Superoxide Dismutase, Polyphenol Oxidase and Cu-Zn Content in the Fruits of Gordal and Manzanilla Olive Varieties

2002 ◽  
Vol 57 (1-2) ◽  
pp. 113-120 ◽  
Author(s):  
Dámaso Hornero-Méndez ◽  
Lourdes Gallardo-Guerrero ◽  
Manuel Jarén-Galán ◽  
María Isabel Mínguez-Mosquera
Keyword(s):  
Superoxide Dismutase ◽  
Polyphenol Oxidase ◽  
Copper Content ◽  
Redox Balance ◽  
Sod Activity ◽  
Activity Peak ◽  
Olive Variety ◽  
Zn Content ◽  
Olive Varieties ◽  
Cu And Zn

Activity of the enzymes superoxide dismutase (SOD) and polyphenol oxidase (PPO) as well as Cu-Zn content have been monitored during the thirteen weeks growth of both Gordal and Manzanilla olive variety fruits. These metalloenzymes, with Cu and Zn in the prostetic group, are involved in controlling the redox balance in the chloroplast environment. The results indicated that, under similar phenological and environmental conditions, there are periodic peaks of SOD activity in both varieties, followed by fluctuations in the copper content of the fruit. This was interpreted as a common and simultaneous response to situations of oxidative stress, and this response was more intense in the variety Gordal. The enzyme PPO showed an activity peak at start of growth and then practically disappeared. Thus, its activity cannot be correlated with situations of stress or with changes of Cu and Zn in the fruit.

Cyanide Insensitive Iron Superoxide Dismutase in Euglena gracilis Comparison of the Reliabilities of Different Test Systems for Superoxide Dismutases

1979 ◽  
Vol 34 (5-6) ◽  
pp. 374-380 ◽  
Author(s):  
E. Lengfelder ◽  
E. F. Elstner
Keyword(s):  
Superoxide Dismutase ◽  
Xanthine Oxidase ◽  
Euglena Gracilis ◽  
Spectral Properties ◽  
Superoxide Dismutase Activity ◽  
Superoxide Dismutases ◽  
Sod Activity ◽  
Iron Superoxide Dismutase ◽  
Test Systems

Abstract Two proteins (P1 and P2 , with mol weights of 57,500 and 27,500, respectively) were isolated from Euglena gracilis. Both proteins show cyanide-insensitive superoxide dismutase activity in the “classical” superoxide dismutase assay, using xanthine-xanthine oxidase as O2·− generator. If O2·− is generated chemically (autoxidation of reduced anthraquinone), photochemically (illuminated riboflavine) or pulse radiolytically, only protein P1 but not P2 shows SOD activity. Protein P1 contains 1 g atom (determined: 0.82) iron (no Mn or Cu) per mole protein and may thus be defined as iron-superoxide dismutase. Protein P2 , showing the spectral properties of a flavoprotein, exhibits the activities of ferredoxin-NADP-oxidoreductase and “diaphorase”. The cyanide-insensitive SOD-activity of this “diaphorase” in the xanthine oxidase-assay for superoxide dismutase makes this classical and commonly used test unreliable for assaying cyanide insensitive SOD activities. The existence of the “prokaryote-type” of superoxide dismutase (Fe-SOD) in Euglena gracilis is exceptional for an eukaryotic, autotrophically grown organisms.

Effects of Cypermethrin on the Superoxide Dismutase Activity of Macrobrachium nipponense

2014 ◽  
Vol 955-959 ◽  
pp. 554-557 ◽  
Author(s):  
Hong Wei Wang ◽  
Hui Wang ◽  
Chun Long Zhao ◽  
Gao Fei Yuan ◽  
Liang Ma ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Control Diet ◽  
Diet Group ◽  
Superoxide Dismutase Activity ◽  
Sod Activity ◽  
Macrobrachium Nipponense ◽  
Dietary Selenium ◽  
Low Concentrations ◽  
Oriental River Prawn

To determine the effects of dietary selenium (Se) supplementary on muscle superoxide dismutase (SOD) activity, oriental river prawn, Macrobrachium nipponense were exposed to three commonly used pesticides - cypermethrin. For each concentration of each pesticide, the shrimps were grouped into control diet group, inorganic Se group and organic Se group. For each concentration of each pesticide, the order of total SOD activities were organic Se diet group > inorganic Se diet group > control diet group. With the increasing concentrations of pesticides, the total SOD activities increased first and then decreased dramatically. This study indicated that Se supplementary in diet could enhance the resistance of shrimps against low concentrations of ambient contaminants.

6.7 Erythrocyte Cu:Zn Superoxide Dismutase Activity and Hair or Fleece Copper Concentrations in the Diagnosis of Hypocuprosis in Ruminants

1983 ◽  
Vol 7 ◽  
pp. 134-135
Author(s):  
N. F. Suttle ◽  
C. H. McMurray
Keyword(s):  
Superoxide Dismutase ◽  
Clinical Condition ◽  
Diagnostic Value ◽  
Superoxide Dismutase Activity ◽  
Clinically Normal ◽  
Temporal Relationships ◽  
Animal Remains ◽  
Cu And Zn

The conventional criteria of copper (Cu) status in ruminants, liver and blood or plasma Cu concentrations, show rapid reductions during depletion while the animal remains clinically normal. Criteria which change less rapidly in response to depletion might be more closely correlated with clinical and sub-clinical condition. Among such criteria are superoxide dismutase (SOD), which occurs as Cu- and Zn-containing enzyme in erythrocytes, and hair or fleece Cu. We have examined the temporal relationships between these different criteria of Cu status in two experiments, in which steers and lambs had been depleted of Cu, to assess their diagnostic value.

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. .

Endogenous superoxide dismutase activity in two Babesia species

Parasitology ◽  
1992 ◽  
Vol 105 (2) ◽  
pp. 177-182 ◽  
Author(s):  
P. Becuwe ◽  
C. Slomianny ◽  
A. Valentin ◽  
J. Schrevel ◽  
D. Camus ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Isoelectric Focusing ◽  
Main Part ◽  
Enzyme Assay ◽  
Superoxide Dismutase Activity ◽  
Babesia Species ◽  
Sod Activity

SUMMARYBabesia hylomysci and B. divergens were studied for superoxide dismutase (SOD) activity by enzyme assay and isoelectric focusing (IEF). In the two Babesia species, parasite-associated SOD is cyanide-insensitive and inhibited by H2 O2, indicating that iron is the cofactor metal. Measurements of SOD activity from purified parasites show that the SOD activity detected in Babesia is, for the main part, due to an endogenous enzyme.

Diazoxide Modulates Cardiac Hypertrophy by Targeting H2O2 Generation and Mitochondrial Superoxide Dismutase Activity

2020 ◽  
Vol 13 (1) ◽  
pp. 76-83
Author(s):  
Aline Maria Brito Lucas ◽  
Joana Varlla de Lacerda Alexandre ◽  
Maria Thalyne Silva Araújo ◽  
Cicera Edna Barbosa David ◽  
Yuana Ivia Ponte Viana ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Cardiac Hypertrophy ◽  
Superoxide Dismutase Activity ◽  
Heart Weight ◽  
Pharmacological Intervention ◽  
Wall Thickening ◽  
H2o2 Production ◽  
Mitochondrial Superoxide ◽  
Mitochondrial Superoxide Dismutase

Background: Cardiac hypertrophy involves marked wall thickening or chamber enlargement. If sustained, this condition will lead to dysfunctional mitochondria and oxidative stress. Mitochondria have ATP-sensitive K+ channels (mitoKATP) in the inner membrane that modulate the redox status of the cell. Objective: We investigated the in vivo effects of mitoKATP opening on oxidative stress in isoproterenol- induced cardiac hypertrophy. Methods: Cardiac hypertrophy was induced in Swiss mice treated intraperitoneally with isoproterenol (ISO - 30 mg/kg/day) for 8 days. From day 4, diazoxide (DZX - 5 mg/kg/day) was used in order to open mitoKATP (a clinically relevant therapy scheme) and 5-hydroxydecanoate (5HD - 5 mg/kg/day) or glibenclamide (GLI - 3 mg/kg/day) were used as mitoKATP blockers. Results: Isoproterenol-treated mice had elevated heart weight/tibia length ratios (HW/TL). Additionally, hypertrophic hearts had elevated levels of carbonylated proteins and Thiobarbituric Acid Reactive Substances (TBARS), markers of protein and lipid oxidation. In contrast, mitoKATP opening with DZX avoided ISO effects on gross hypertrophic markers (HW/TL), carbonylated proteins and TBARS, in a manner reversed by 5HD and GLI. Moreover, DZX improved mitochondrial superoxide dismutase activity. This effect was also blocked by 5HD and GLI. Additionally, ex vivo treatment of isoproterenol- induced hypertrophic cardiac tissue with DZX decreased H2O2 production in a manner sensitive to 5HD, indicating that this drug also acutely avoids oxidative stress. Conclusion: Our results suggest that diazoxide blocks oxidative stress and reverses cardiac hypertrophy. This pharmacological intervention could be a potential therapeutic strategy to prevent oxidative stress associated with cardiac hypertrophy.

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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