Methods compared for determining glutathione peroxidase activity in blood.

1987 ◽  
Vol 33 (4) ◽  
pp. 539-543 ◽  
Author(s):  
B Faraji ◽  
H K Kang ◽  
J L Valentine
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Reference Intervals ◽  
The Other ◽  
Specific Time ◽  
Glutathione Peroxidase Activity ◽  
Time Intervals ◽  
Indirect Methods ◽  
Blood Samples

Abstract We compared four methods for determination of glutathione peroxidase (EC 1.11.1.9) activity, using blood samples from 52 healthy volunteers. Two methods depended on direct assay of the amount of glutathione remaining at specific time intervals; the two indirect methods involved measuring the rate of disappearance of NADPH. We assessed the precision and reproducibility of each method. One of the indirect assays proved to be far superior to the other methods. Results of each of the methods were correlated with one another. We present the normal reference intervals for glutathione peroxidase activity for all four methods.

Determination of glutathione peroxidase activity in human milk

Nahrung/Food ◽  
2003 ◽  
Vol 47 (6) ◽  
pp. 430-433 ◽  
Author(s):  
Angeles Torres ◽  
Rosaura Farré ◽  
María Jesús Lagarda ◽  
Javier Monleón
Keyword(s):  
Glutathione Peroxidase ◽  
Human Milk ◽  
Peroxidase Activity ◽  
Glutathione Peroxidase Activity

Determination of selenium concentration and glutathione peroxidase activity in plasma and erythrocytes.

1982 ◽  
Vol 28 (2) ◽  
pp. 311-316 ◽  
Author(s):  
P A Pleban ◽  
A Munyani ◽  
J Beachum
Keyword(s):  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Zeeman Effect ◽  
Selenium Concentration ◽  
Glutathione Peroxidase Activity ◽  
Plasma Selenium ◽  
Plasma Glutathione Peroxidase ◽  
Flameless Atomic Absorption Spectroscopy ◽  
Plasma Glutathione

Abstract We determined selenium concentrations and activities of the selenoenzyme, glutathione peroxidase (EC 1.11.1.9), in the plasma and erythrocytes of 38 apparently healthy women. We determined selenium concentrations directly by polarized Zeeman-effect flameless atomic absorption spectroscopy. Within-run precision studies for the assays gave CVs of 5.6% for a mean erythrocyte selenium concentration of 149.9 (SD 8.3) microgram/L (n = 10) and 6.4% for a mean plasma selenium concentration of 97.3 (SD 6.2) microgram/L (n = 12). For the women, mean selenium concentrations were 141.4 (SD 14.3) microgram/L of erythrocytes [0.49 (SD 0.07) microgram/g of hemoglobin and 96.3 (SD 14.2) microgram/L of plasma. Glutathione peroxidase activities were measured by a modification of the method of Paglia and Valentine (J. Lab. Clin. Med. 70: 158--169, 1967). Within-run precision studies for the glutathione peroxidase assays gave CVs of 12.8% for mean erythrocyte glutathione peroxidase activity of 77.2 (SD 9.9) U/g of hemoglobin (n = 13), and 8.1% for mean plasma activity of 312.5 (SD 25.2) U/L (n = 11). Mean enzyme activity was 78.7 (SD 12.9) U/g of hemoglobin for erythrocytes and 424 (SD 40) U/L for plasma. Erythrocyte selenium concentrations and glutathione peroxidase activities were positively, but poorly, correlated (r = 0.41, p less than 0.01).

scholarly journals Haemoglobin Oxidation in Whole Blood Samples From Sheep in Relation to Glutathione Peroxidase Activity

1979 ◽  
Vol 32 (5) ◽  
pp. 451 ◽  
Author(s):  
JF Wilkins
Keyword(s):  
Glutathione Peroxidase ◽  
Oxidative Damage ◽  
Peroxidase Activity ◽  
Whole Blood ◽  
Alternative Assessment ◽  
Selenium Status ◽  
Glutathione Peroxidase Activity ◽  
Blood Samples ◽  
Whole Blood Samples

A high correlation was observed between HzOz-induced oxidation of haemoglobin and glutathione peroxidase activity in whole blood samples from sheep. A role of this enzyme in the prevention of oxidative damage to the erythrocyte and its contents has been previously demonstrated. The possibility of using haemoglobin oxidation in whole blood as an alternative assessment of glutathione peroxidase activity and hence of selenium status is proposed.

Low Selenium Status in the Elderly Influences Thyroid Hormones

1995 ◽  
Vol 89 (6) ◽  
pp. 637-642 ◽  
Author(s):  
Oliviero Olivieri ◽  
Domenico Girelli ◽  
Margherita Azzini ◽  
Anna Maria Stanzial ◽  
Carla Russo ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Thyroid Hormones ◽  
Peroxidase Activity ◽  
Controlled Trial ◽  
The Elderly ◽  
Serum Selenium ◽  
Selenium Status ◽  
Glutathione Peroxidase Activity ◽  
Double Blind ◽  
Double Blind Placebo

1. Iodothyronine 5′-deiodinase, which is mainly responsible for peripheral triiodothyronine (T3) production, has recently been demonstrated to be a selenium-containing enzyme. In the elderly, reduced peripheral conversion of thyroxine (T4) to T3 and overt hypothyroidism are frequently observed. 2. We measured serum selenium and erythrocyte glutathione peroxidase (as indices of selenium status), thyroid hormones and thyroid-stimulating hormone in 109 healthy euthyroid subjects (52 women, 57 men), carefully selected to exclude abnormally low thyroid hormone levels induced by acute or chronic diseases or calorie restriction. The subjects were subdivided into three age groups. To avoid conditions of undernutrition or malnutrition, dietary records were obtained for a sample of 24 subjects, randomly selected and representative of the whole population for age and sex. 3. In order to properly assess the influence of selenium status on iodothyronine 5′-deiodinase type I activity, a double-blind placebo-controlled trial was also carried out on 36 elderly subjects, resident at a privately owned nursing home. 4. In the free-living population, a progressive reduction of the T3/T4 ratio (due to increased T4 levels) and of selenium and erythrocyte glutathione peroxidase activity was observed with advancing age. A highly significant linear correlation between T4, T3/T4 and selenium was observed in the population as a whole (for T4, R = −0.312, P < 0.002; for T3/T4 ratio, R = 0.32, P < 0.01) and in older subjects (for T4, R = −0.40, P < 0.05; for T3/T4 ratio, R = 0.54, P < 0.002). 5. The main result of the double-blind placebo-controlled trial was a significant improvement of selenium indices and a decrease in the T4 level in selenium-treated subjects; serum selenium, erythrocyte glutathione peroxidase activity and thyroid hormones did not change in placebo-treated subjects. 6. We concluded that selenium status influences thyroid hormones in the elderly, mainly modulating T4 levels.

scholarly journals Selenium levels and glutathione peroxidase activity in patients with ataxia-telangiectasia: association with oxidative stress and lipid status biomarkers

2021 ◽  
Vol 16 (1) ◽  
Author(s):  
Itana Gomes Alves Andrade ◽  
Fabíola Isabel Suano-Souza ◽  
Fernando Luiz Affonso Fonseca ◽  
Carolina Sanchez Aranda Lago ◽  
Roseli Oselka Saccardo Sarni
Keyword(s):  
Oxidative Stress ◽  
Glutathione Peroxidase ◽  
Peroxidase Activity ◽  
Oxidized Ldl ◽  
Reference Value ◽  
Glutathione Peroxidase Activity ◽  
Oxidative Stress Biomarkers ◽  
Apo B ◽  
Lipid Status ◽  
And Oxidative Stress

Abstract Introduction Ataxia-Telangiectasia (A-T) is a multi-system disorder that may be associated with endocrine changes, oxidative stress in addition to inflammation. Studies suggest that selenium is a trace element related to protection against damage caused by oxidative stress. Objective To describe the plasma levels of selenium and erythrocyte glutathione peroxidase activity in A-T patients and to relate them to oxidative stress and lipid status biomarkers. Methods This is a cross-sectional and controlled study evaluating 22 A-T patients (age median, 12.2 years old) matched by gender and age with 18 healthy controls. We evaluated: nutritional status, food intake, plasma selenium levels, erythrocyte glutathione peroxidase activity, lipid status, inflammation and oxidative stress biomarkers. Results Adequate levels of selenium were observed in 24/36 (66.7%) in this evaluated population. There was no statistically significant difference between the groups in selenium levels [47.6 μg/L (43.2–57.0) vs 54.6 (45.2–62.6) μg/dL, p = 0.242]. Nine of A-T patients (41%) had selenium levels below the reference value. The A-T group presented higher levels of LDL-c, non-HDL-c, oxidized LDL, Apo B, Apo-B/Apo-A-I1, LDL-c/HDL-c ratio, malondialdehyde [3.8 µg/L vs 2.8 µg/L, p = 0.029] and lower Apo-A-I1/HDL-c and glutathione peroxidase activity [7300 U/L vs 8686 U/L, p = 0.005]. Selenium levels were influenced, in both groups, independently, by the concentrations of oxidized LDL, malonaldehyde and non-HDL-c. The oxidized LDL (AUC = 0.849) and ALT (AUC = 0.854) were the variables that showed the greatest discriminatory power between groups. Conclusion In conclusion, we observed the presence of selenium below the reference value in nearly 40% and low GPx activity in A-T patients. There was a significant, inverse and independent association between selenium concentrations and oxidative stress biomarkers. Those data reinforce the importance of assessing the nutritional status of selenium in those patients.

scholarly journals The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells

1989 ◽  
Vol 264 (3) ◽  
pp. 737-744 ◽  
Author(s):  
P Steinberg ◽  
H Schramm ◽  
L Schladt ◽  
L W Robertson ◽  
H Thomas ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Cell Types ◽  
Transferase Activity ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Liver Parenchymal ◽  
Parenchymal Cells

The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.

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