scholarly journals Influence of mouse age and erythrocyte age on glutathione metabolism

1978 ◽  
Vol 174 (3) ◽  
pp. 819-825 ◽  
Author(s):  
E C Abraham ◽  
J F Taylor ◽  
C A Lang
Keyword(s):  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Specific Radioactivity ◽  
Phthalate Ester ◽  
Pulse Labelling ◽  
Very Old ◽  
Free Thiol ◽  
Glutathione Reductase Activity

In order to determine whether the biological age of a mouse influences erythrocyte metabolism and erythrocyte aging in vivo, blood samples were collected from male C57/BL6J mice of different biological ages ranging from mature (10 months) to “very old” (37 months). In the very old mouse, compared with the mature mouse, the erythrocyte survival time was decreased, erythrocyte densities were increased, the concentrations of total free thiol and reduced glutathione, and glutathione reductase activity were decreased. Erythrocytes were separated into different density (age) groups by phthalate ester two-phase centrifugation or by albumin density-gradient centrifugation. The density-age relationship of erythrocytes was established by pulse-labelling with 59Fe in vivo and by subsequent determinations of specific radioactivity of erythrocyte fractions of different densities prepared during a chase period of 60 days. The age of erythrocytes in mice of all ages was directly related to density. Also, in older erythrocytes compared with younger erythrocytes, decreased concentrations of total free thiol and reduced glutathione, and decreased glutathione reductase activity were observed. These were the lowest in the old erythrocytes of very old mice. These results in aging erythrocytes from aging mice suggest that the glutathione status the erythrocyte may be an index of aging, not only of the cell but also of the organism.

scholarly journals In Vivo Bioavailability of Selenium in Selenium-Enriched Streptococcus thermophilus and Enterococcus faecium in CD IGS Rats

Antioxidants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 463
Author(s):  
Gabriela Krausova ◽  
Antonin Kana ◽  
Marek Vecka ◽  
Ivana Hyrslova ◽  
Barbora Stankova ◽  
...  
Keyword(s):  
Glutathione Reductase ◽  
Enterococcus Faecium ◽  
Reductase Activity ◽  
Streptococcus Thermophilus ◽  
Heart Tissue ◽  
Sprague Dawley ◽  
Glutathione Reductase Activity ◽  
Novel Concept ◽  
The Individual

The selenium (Se) enrichment of yeasts and lactic acid bacteria (LAB) has recently emerged as a novel concept; the individual health effects of these beneficial microorganisms are combined by supplying the essential micronutrient Se in a more bioavailable and less toxic form. This study investigated the bioavailability of Se in the strains Enterococcus faecium CCDM 922A (EF) and Streptococcus thermophilus CCDM 144 (ST) and their respective Se-enriched forms, SeEF and SeST, in a CD (SD-Sprague Dawley) IGS rat model. Se-enriched LAB administration resulted in higher Se concentrations in the liver and kidneys of rats, where selenocystine was the prevalent Se species. The administration of both Se-enriched strains improved the antioxidant status of the animals. The effect of the diet was more pronounced in the heart tissue, where a lower glutathione reductase content was observed, irrespective of the Se fortification in LAB. Interestingly, rats fed diets with EF and SeEF had higher glutathione reductase activity. Reduced concentrations of serum malondialdehyde were noted following Se supplementation. Diets containing Se-enriched strains showed no macroscopic effects on the liver, kidneys, heart, and brain and had no apparent influence on the basic parameters of the lipid metabolism. Both the strains tested herein showed potential for further applications as promising sources of organically bound Se and Se nanoparticles.

THE AMPEROMETRIC DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN HUMAN ERYTHROCYTES

1955 ◽  
Vol 33 (3) ◽  
pp. 404-407 ◽  
Author(s):  
H. Bruce Collier ◽  
Sheila C. McRae
Keyword(s):  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Human Erythrocytes ◽  
Amperometric Titration ◽  
Amperometric Determination ◽  
Marked Inhibition ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Glutathione reductase activity of hemolyzates of human erythrocytes was measured by an amperometric titration of the reduced glutathione that is formed from oxidized glutathione. The electron donor in the system was reduced triphosphopyridine nucleotide, produced by the glucose-6-phosphate dehydrogenase of the cells. Removal of the red-cell stromata from hemolyzates slightly increased the reductase activity. Addition of Na+, K+, or Ca++ had no effect on the enzyme. No marked inhibition was observed in the presence of phenothiazine, phenothiazone, phenylhydrazine, or p-chloromercuribenzoate.

The Oxidation of Glutathione by Serum

1964 ◽  
Vol 10 (1) ◽  
pp. 53-61
Author(s):  
Hugo R Rony ◽  
Michael West ◽  
Hyman J Zimmerman
Keyword(s):  
Cytochrome C ◽  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Glutathione Reductase Activity

Abstract Studies of serum glutathione reductase activity in this laboratory prompted an attempt to demonstrate glutathione oxidase in the serum. The oxidation of reduced glutathione in the sera of patients with various diseases does not differ from normal sera. Preheating the serum and addition of cytochrome c does not effect the oxidizing capacity of the serum. The ability of serum to oxidize reduced glutathione appears to represent autoxidation, not the effect of an oxidizing enzyme.

THE AMPEROMETRIC DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN HUMAN ERYTHROCYTES

1955 ◽  
Vol 33 (1) ◽  
pp. 404-407 ◽  
Author(s):  
H. Bruce Collier ◽  
Sheila C. McRae
Keyword(s):  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Human Erythrocytes ◽  
Amperometric Titration ◽  
Amperometric Determination ◽  
Marked Inhibition ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Glutathione reductase activity of hemolyzates of human erythrocytes was measured by an amperometric titration of the reduced glutathione that is formed from oxidized glutathione. The electron donor in the system was reduced triphosphopyridine nucleotide, produced by the glucose-6-phosphate dehydrogenase of the cells. Removal of the red-cell stromata from hemolyzates slightly increased the reductase activity. Addition of Na+, K+, or Ca++ had no effect on the enzyme. No marked inhibition was observed in the presence of phenothiazine, phenothiazone, phenylhydrazine, or p-chloromercuribenzoate.

scholarly journals Familial deficiency of glutathione reductase in human blood cells

Blood ◽  
1976 ◽  
Vol 48 (1) ◽  
pp. 53-62 ◽  
Author(s):  
H Loos ◽  
D Roos ◽  
R Weening ◽  
J Houwerzijl
Keyword(s):  
Glutathione Reductase ◽  
Blood Cells ◽  
Normal Values ◽  
Reductase Activity ◽  
White Blood Cells ◽  
Human Blood Cells ◽  
Glutathione Reductase Activity ◽  
Fava Beans

A virtually complete absence of glutathione reductase activity was found in the erythrocytes of all three children (one male, two females) from a consanguineous marriage. Intermediate values were found in the erythrocytes of both parents. The enzyme activity could not be restored either by addition of FAD in vitro or by administration of riboflavin in vivo. The amount of reduced glutathione in the erythrocytes was normal in each case. Severely diminished glutathione stability during incubation with acetylphenylhydrazine was observed in the erythrocytes of the siblings, as well as intermediate stability in the parents' red cells. Clinically, this deficiency was manifested by hemolytic crises after eating fava beans in the eldest daughter (patient), and possibly by cataracts in her own and in her brother's eyes. Very low activities of glutathione reductase were also found in the leukocytes of this family: 13%-15% of normal values for the children and 64%-66% for the parents. Moreover, the same deficiency was found in the purified white blood cells of the propositus: 8% of normal values in the polymorphonuclear (PMN) cells, 4% in the lymphocytes, and 15% in the monocytes, together with 11% in the platelets. Finally, we found an abnormal oxygen consumption of the propositus' PMNs after phagocytosis of zymosan particles, suggesting that the glutathione reductase reaction was involved in the bactericidal capacity of these cells.

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