Stable selones in glutathione-peroxidase-like catalytic cycle of selenonicotinamide derivative

2014 ◽  
Vol 12 (15) ◽  
pp. 2404-2412 ◽  
Author(s):  
Parashiva Prabhu ◽  
Beena G. Singh ◽  
Masato Noguchi ◽  
Prasad P. Phadnis ◽  
Vimal K. Jain ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Exchange Reaction ◽  
Catalytic Cycle ◽  
Sulfur Exchange

Stable selone formation in 2,2′-diselenobis[3-amidopyridine], reduces unwanted sulfur exchange reaction in glutathione peroxidase like catalytic cycle and enhances its enzyme activity.

scholarly journals Вплив хлориду кадмію на стан антиоксидантної системи у печінці щурів

2013 ◽  
pp. 102-103
Author(s):  
Б. В. Гутий
Keyword(s):  
Lipid Peroxidation ◽  
Superoxide Dismutase ◽  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Antioxidant System ◽  
Cadmium Chloride

Розкрито особливості антиоксидантної системиорганізму щурів за хронічного кадмієвого токсикозу.Встановлено, що хлорид кадмію у токсичній дозісприяє зниженню активності ферментної й нефер-ментної системи антиоксидантного захисту, на щовказує зниження ферментів глутатіонпероксидази,глутатіонредуктази, супероксиддисмутази, катала-зи та відновленого глутатіону у печінці щурів. Ре-зультати досліджень вказують на те, що хронічнийкадмієвий токсикоз призводить до посиленої акти-вації процесів ліпопероксидації. The features of the antioxidant system of rats with chronic cadmium toxicosiare disclosed. It wasresearched that cadmium chloride in toxic doses reduces enzyme activity of antioxidant system, asindicated by the decrease in enzyme glutathione peroxidase, hlutationreduktazy, superoxide dismutase,catalase and restored glutathione in the liver and blood of rats. The results indicate that chroniccadmium toxicosis leads to enhanced activation of lipid peroxidation.

scholarly journals Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 640-645 ◽  
Author(s):  
K Takahashi ◽  
HJ Cohen
Keyword(s):  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Protein Content ◽  
Polyclonal Antibodies ◽  
Plasma Enzyme ◽  
Plasma Enzymes ◽  
Erythrocyte Enzyme ◽  
Dependent Protein ◽  
Gshpx Activity ◽  
Almost All

Selenium-deficient humans and animals are known to be deficient in glutathione peroxidase (GSHPx) activity in their cells and plasma. To determine the relationship between enzyme activity and protein content, the enzyme was purified from human erythrocytes, and polyclonal antibodies were made against the purified protein in rabbits. These antibodies were found to be monospecific, noninhibitory, and capable of precipitating the enzymatic activity. All the GSHPx activity in erythrocytes and almost all the activity in neutrophils and platelets was precipitated by these antibodies. None of the plasma enzyme was precipitated by these antibodies, indicating that the plasma enzyme activity was attributable to a different selenium dependent protein moiety. Utilizing a radioimmunoassay, we were able to determine that there was a direct relationship between GSHPx activity and protein content in the erythrocytes of both normal and selenium-deficient individuals, and a similar relationship between control and selenium- deficient rat erythrocytes and liver cells. Thus, the ability to examine GSHPx as a protein resulted in two new observations concerning the selenium-dependent GSHPx. The first is that the plasma enzyme is antigenically distinct from the erythrocyte enzyme, and the second is that in the absence of selenium, there is a concomitant decrease in GSHPx protein.

scholarly journals A validated method to assess glutathione peroxidase enzyme activity

2021 ◽  
Author(s):  
Ahmed Yasser Ahmed ◽  
Saadon Abdulla Aowda ◽  
Mahmoud Hussein Hadwan
Keyword(s):  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Peroxidase Enzyme

Enabling Oxygen–Sulfur Exchange Reaction to Produce Semicrystalline Copolymers from Carbon Disulfide and Ethylene Oxide

2020 ◽  
pp. 2000472
Author(s):  
Jia‐Liang Yang ◽  
Ying Wang ◽  
Xiao‐Han Cao ◽  
Cheng‐Jian Zhang ◽  
Zheng Chen ◽  
...  
Keyword(s):  
Ethylene Oxide ◽  
Exchange Reaction ◽  
Carbon Disulfide ◽  
Sulfur Exchange

scholarly journals Quantification of cysteine hydropersulfide with a ratiometric near-infrared fluorescent probe based on selenium–sulfur exchange reaction

2016 ◽  
Vol 7 (8) ◽  
pp. 5098-5107 ◽  
Author(s):  
Xiaoyue Han ◽  
Fabiao Yu ◽  
Xinyu Song ◽  
Lingxin Chen
Keyword(s):  
Exchange Reaction ◽  
Fluorescent Probe ◽  
Near Infrared ◽  
Living Cells ◽  
Hepatic Carcinoma ◽  
Sulfur Exchange

A ratiometric near-infrared fluorescent probe based on a selenium–sulfur exchange reaction to quantify cysteine hydropersulfide in living cells and hepatic carcinoma rats.

scholarly journals Phosphorylation of purified bovine heart and rat liver 6-phosphofructo-2-kinase by protein kinase C and comparison of the fructose-2,6-bisphosphatase activity of the two enzymes

1986 ◽  
Vol 240 (1) ◽  
pp. 57-61 ◽  
Author(s):  
M H Rider ◽  
L Hue
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Exchange Reaction ◽  
Liver Enzyme ◽  
Rat Liver ◽  
Phosphorylation State ◽  
Bovine Heart ◽  
Kinase C

Purified bovine heart 6-phosphofructo-2-kinase can be phosphorylated in the presence of protein kinase C and dephosphorylated by alkaline phosphatase; changes in phosphorylation state have no effect on enzyme activity. By contrast, the rat liver enzyme is a poor substrate for protein kinase C. Unlike the liver enzyme, which is bifunctional and is phosphorylated by fructose 2,6-[2-32P]bisphosphate, the heart enzyme contains 10 times less fructose 2,6-bisphosphatase activity and is phosphorylated at a slower rate and to a lesser extent than the liver enzyme. Both rat liver and bovine heart enzymes catalyse a similar exchange reaction between [U-14C]ADP and ATP.

P2499Effects of aerobic and resistance exercise on skeletal muscle of infarcted rats

2019 ◽  
Vol 40 (Supplement_1) ◽  
Author(s):  
M J Gomes ◽  
A R R Lima ◽  
L U Pagan ◽  
F C Damatto ◽  
L R S Oliveira ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Myocardial Infarction ◽  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Resistance Exercise ◽  
Lipid Hydroperoxide ◽  
The Other ◽  
Species Production ◽  
Hydroperoxide Concentration

Abstract Background Skeletal muscle changes contribute to reduced physical performance after myocardial infarction (MI). Exercise has been recommended to stable patients. However, the effects of resistance exercise after MI are not clear. We compared the effects of aerobic and resistance exercise initiated during compensated cardiac remodeling in infarcted rat gastrocnemius muscle. Methods Three months after MI induction, Wistar rats were divided into four groups: Sham (n=20); sedentary MI (MI-S, n=9); aerobic exercised MI (MI-A, n=9); and resistance exercised MI (MI-R, n=13). Exercised rats trained three times a week for 12 weeks on a treadmill or ladder. Energy metabolism, oxidative stress markers, and antioxidant enzyme activities were assessed by spectrophotometry. Satellite cells activation markers (MyoD, NCAM, and myosin heavy chain neonatal isoform) were assessed by immunofluorescence or Western blot (Pax-7). Statistical analysis: ANOVA or Mann Whitney. Results Physical aerobic capacity was greater in MI-A and strength gain higher in MI-R. Cardiac structures and left ventricular function evaluated by echocardiogram did not differ between infarcted groups. Histological analysis showed that MI size and gastrocnemius cross sectional area did not differ between infarcted groups. Oxygen reactive species production was higher in MI-S than Sham and lipid hydroperoxide concentration was lower in MI-A than the other groups. Catalase activity was higher and glutathione peroxidase lower in infarcted groups than Sham. Superoxide dismutase activity was higher in Sham and MI-R than MI-S. Skeletal muscle metabolism enzyme activity did not differ between groups, except for increase pyruvate kinase in MI-S against the other groups, and β-hydroxyacyl CoA dehydrogenase in MI-S against Sham. Satellite cell activation and protein expression of MAPK and NF-kB did not differ between groups. Conclusion Aerobic and resistance exercise respectively improves physical capacity and muscle strength without changing echocardiographic parameters of infarcted rats. Myocardial infarction increases oxygen reactive species production and changes antioxidant enzyme activity and glucose and fatty acid metabolism. Aerobic exercise is superior to resistance exercise against oxidative stress reducing muscle lipid hydroperoxide concentration and attenuating change in glutathione peroxidase activity. Acknowledgement/Funding Financial support: Fapesp, CNPq, Capes, and UNESP

scholarly journals Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 640-645 ◽  
Author(s):  
K Takahashi ◽  
HJ Cohen
Keyword(s):  
Enzyme Activity ◽  
Glutathione Peroxidase ◽  
Protein Content ◽  
Polyclonal Antibodies ◽  
Plasma Enzyme ◽  
Plasma Enzymes ◽  
Erythrocyte Enzyme ◽  
Dependent Protein ◽  
Gshpx Activity ◽  
Almost All

Abstract Selenium-deficient humans and animals are known to be deficient in glutathione peroxidase (GSHPx) activity in their cells and plasma. To determine the relationship between enzyme activity and protein content, the enzyme was purified from human erythrocytes, and polyclonal antibodies were made against the purified protein in rabbits. These antibodies were found to be monospecific, noninhibitory, and capable of precipitating the enzymatic activity. All the GSHPx activity in erythrocytes and almost all the activity in neutrophils and platelets was precipitated by these antibodies. None of the plasma enzyme was precipitated by these antibodies, indicating that the plasma enzyme activity was attributable to a different selenium dependent protein moiety. Utilizing a radioimmunoassay, we were able to determine that there was a direct relationship between GSHPx activity and protein content in the erythrocytes of both normal and selenium-deficient individuals, and a similar relationship between control and selenium- deficient rat erythrocytes and liver cells. Thus, the ability to examine GSHPx as a protein resulted in two new observations concerning the selenium-dependent GSHPx. The first is that the plasma enzyme is antigenically distinct from the erythrocyte enzyme, and the second is that in the absence of selenium, there is a concomitant decrease in GSHPx protein.

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