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.

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.

scholarly journals Isoniazid acetylating phenotype in patients with paracoccidioidomycosis and its relationship with serum sulfadoxin levels, glucose-6-phosphate dehydrogenase and glutathione reductase activities

1991 ◽  
Vol 24 (2) ◽  
pp. 111-114 ◽  
Author(s):  
Benedito Barraviera ◽  
Paulo Câmara Marques Pereira ◽  
Jussara Marcondes Machado ◽  
Maria Julia de Souza ◽  
Carlos Roberto G. Lima ◽  
...  
Keyword(s):  
Glutathione Reductase ◽  
Reductase Activity ◽  
Serum Levels ◽  
Slow Acetylators ◽  
Slow Acetylator ◽  
A Value ◽  
Acti Vity ◽  
Glutathione Reductase Activity ◽  
Glutathione Reductase Deficiency ◽  
Glucose 6 Phosphate Dehydrogenase

The authors evaluated the isoniazid acetylating phenotype and measured hematocrit, hemoglobin, glucose-6-phosphate dehydrogenase and glutathione reductase activities plus serum sulfadoxin levels in 39 patients with paracoccidioidomycosis (33 males and 6 females) aged 17 to 58 years. Twenty one (53.84%) of the patients presented a slow acetylatingphenotype and 18(46.16%) a fast acetylating phenotype. Glucose-6-phosphate- dehydrogenase (G6PD) acti vity was decreased in 5(23.80%) slow acetylators and in 4(22.22%) fast acetylators. Glutathione reductase activity was decreased in 14 (66.66%) slow acetylators and in 12 (66.66%) fast acetylators. Serum levels of free and total sulfadoxin Were higher in slow acetylator (p < 0.02). Analysis of the resultspermitted us to conclude that serum sulfadoxin levels are related to the acetylatorphenotype. Furthermore, sulfadoxin levels were always above 50 µg/ml, a value considered therapeutic. Glutathione reductase deficiency observed in 66% of patients may be related to the intestinal malabsorption of nutrients, among them riboflavin, a FAD precursor vitamin, inpatients with paracoceidioidomycosis.

Measurement of glucose-6-phosphate dehydrogenase and glutathione reductase activity in patients with paracoccidioidomycosis treated with ketoconazole

1988 ◽  
Vol 104 (2) ◽  
pp. 87-91
Author(s):  
Benedito Barraviera ◽  
Rinaldo Poncio Mendes ◽  
Paulo Câmara Marques Pereira ◽  
Jussara Marcondes Machado ◽  
Paulo Roberto Curi ◽  
...  
Keyword(s):  
Glutathione Reductase ◽  
Reductase Activity ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

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.

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.

scholarly journals DETERMINATION OF GLUTATHIONE REDUCTASE ACTIVITY IN MICROGRAM SAMPLES OF TISSUE, QUANTITATIVE HISTOLOGIC DISTRIBUTION OF THE ENZYME IN THE RAT ADRENAL AND EFFECT OF ADRENOCORTICOTROPIN

1968 ◽  
Vol 16 (3) ◽  
pp. 185-190 ◽  
Author(s):  
NORBERTO A. SCHOR ◽  
DAVID GLICK
Keyword(s):  
Glutathione Reductase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Reductase Activity ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Border Region ◽  
Nicotinamide Adenine ◽  
Subcutaneous Injections ◽  
Glutathione Reductase Activity ◽  
Reduced Nicotinamide Adenine Dinucleotide

A fluorometric method for determination of glutathione reductase activity in microgram samples of tissue, i.e., microtome sections, based on measurement of the decrease of reduced nicotinamide adenine dinucleotide phosphate due to its oxidation on reaction with oxidized glutathione, was developed and applied to the quantitative histologic distribution of the enzyme in the adrenal gland of the rat. Single subcutaneous injections of adrenocorticotropin in saline solution (25 mg/kg) produced little change of enzyme activity in any of the histologic zones, although there was some tendency for the peak activity to shift from fasciculata to the fascicular-reticular border region. The possible interrelationship of glutathione reductase with ascorbic acid and reduced nicotinamide adenine dinucleotide phosphate in adrenal function was considered.

scholarly journals Acute Hemolytic Anemia in the Newborn Infant due to Naphthalene Poisoning: Report of Two Cases, with Investigations into the Mechanism of the Disease

Blood ◽  
1958 ◽  
Vol 13 (12) ◽  
pp. 1113-1125 ◽  
Author(s):  
JEAN P. DAWSON ◽  
WILLIAM W. THAYER ◽  
JANE F. DESFORGES ◽  
Alice C. Manchester ◽  
Reda Lendraitis
Keyword(s):  
Methylene Blue ◽  
Glutathione Reductase ◽  
Dehydrogenase Activity ◽  
Hemolytic Anemia ◽  
Newborn Infant ◽  
Reductase Activity ◽  
Newborn Period ◽  
Glutathione Reductase Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract 1. Two cases of naphthalene hemolytic anemia in the newborn period are reported. 2. Both exhibited glutathione instability upon incubation with acetyl phenylhydrazine and naphthol months to years later. Several members of their families exhibited a similar defect with evidence that it is inherited as a simple dominant. 3. In those individuals with glutathione instability there was deficient TPNH2 generation by their hemolysates in the presence of glucose-6-phosphate and TPN, indicating a deficiency in glucose-6-phosphate dehydrogenase activity. Glutathione reductase activity was normal or decreased. 4. TPNH2-linked reduction of methemoglobin by erythrocyte suspensions in the presence of glucose and methylene blue was also decreased in those subjects tested, a finding consistent with the deficiency in glucose-6-phosphate dehydrogenase.

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