scholarly journals A critical appraisal of the effect of oxidized glutathione on hepatic glucose 6-phosphate dehydrogenase activity

1983 ◽  
Vol 214 (3) ◽  
pp. 959-965 ◽  
Author(s):  
H R Levy ◽  
M Christoff
Keyword(s):  
Glutathione Reductase ◽  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Critical Appraisal ◽  
Oxidized Glutathione ◽  
Assay Procedure ◽  
Low Concentrations ◽  
Hepatic Glucose ◽  
Spurious Effect ◽  
Glucose 6 Phosphate Dehydrogenase

Experiments were undertaken to elucidate the mechanism of the reversal of NADPH inhibition of rat liver glucose 6-phosphate dehydrogenase by oxidized gluthathione alone and in combination with a putative cofactor described by Eggleston & Krebs [(1974) Biochem. J. 138, 425-435]. Evidence is presented that this reversal is largely an artifact, caused by the incorrect application of a control assay procedure and a spurious effect of Zn2+ (added in order to inhibit glutathione reductase) in crude enzyme solutions. When the proper assay procedure is used and glutathione reductase is inhibited with low concentrations of Hg2+, glutathione addition has no effect on NADPH inhibition of glucose 6-phosphate dehydrogenase. No evidence was found for the existence of a cofactor that mediates an effect of glutathione on glucose 6-phosphate dehydrogenase.

scholarly journals Investigation of the Defect in a Variant of Hereditary Methemoglobinemia

Blood ◽  
1962 ◽  
Vol 19 (1) ◽  
pp. 60-74 ◽  
Author(s):  
PHILIP L. TOWNES ◽  
MARTIN MORRISON
Keyword(s):  
Lactic Acid ◽  
Glutathione Reductase ◽  
Dehydrogenase Activity ◽  
Reduced Glutathione ◽  
Coupled System ◽  
Oxidized Glutathione ◽  
Total Glutathione ◽  
Primary Defect ◽  
New Variant ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract 1. Further evidence has been presented to confirm the fact that the methemoglobin found in a new variant of hereditary methemoglobinemia was normal methemoglobin. 2. The reduced glutathione content of the red cells of this variant was less than 50 per cent of normal. 3. The total glutathione and oxidized glutathione were proportionally deficient. 4. The low glutathione content did not result from abnormal degradation nor lack of adequate reducing mechanisms. The primary defect was considered to be one of inadequate glutathione synthesis. 5. Various enzymes were assayed, including the following: glucose 6-phosphate dehydrogenase, lactic acid dehydrogenase, triosephosphate dehydrogenase, glutathione reductase, glucose 6-phosphate dehydrogenase-glutathione reductase (coupled system) and catalase. 6. This variant of methemoglobinemia was considered to result from inadequate synthesis of glutathione. The deficiency of this essential co-factor apparently results in an impairment of triosephosphate dehydrogenase activity and consequently insufficient reduction of DPN, an essential component of the DPNH-dependent methemoglobin reductase.

scholarly journals Characterization of the glucose 6-phosphate dehydrogenase activity in rat liver mitochondria

1976 ◽  
Vol 159 (3) ◽  
pp. 683-687 ◽  
Author(s):  
M Grunwald ◽  
H Z Hill
Keyword(s):  
Dehydrogenase Activity ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Kinetic Behaviour ◽  
Two Peaks ◽  
Glucose 6 Phosphate Dehydrogenase

Glucose 6-phosphate dehydrogenase activity in rat liver mitochondria can be released by detergent. The released activity is separated by chromatography into two peaks. One peak has the kinetic behaviour and mobility similar to the soluble sex-linked enzyme, whereas the other peak is similar to the microsomal hexose 6-phosphate dehydrogenase. There is no evidence for the existence of a new glucose 6-phosphate dehydrogenase activity in rat liver mitochondria.

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.

THE EFFECT OF NECROGENIC DIETS ON THE ACTIVITIES OF CERTAIN ENZYME SYSTEMS IN THE RED BLOOD CELLS OF RATS

1964 ◽  
Vol 42 (12) ◽  
pp. 1809-1814 ◽  
Author(s):  
Beverley B. Lazier ◽  
J. M. R. Beveridge
Keyword(s):  
Red Blood Cells ◽  
Glutathione Reductase ◽  
Dehydrogenase Activity ◽  
Blood Cells ◽  
Sodium Selenite ◽  
Basal Diet ◽  
Hepatic Necrosis ◽  
Male Rats ◽  
Enzyme Systems ◽  
Glucose 6 Phosphate Dehydrogenase

The enzymic activities of glucose-6-phosphate dehydrogenase, glutathione reductase, and catalase were studied in the red blood cells of male rats which were fed a basal diet designed to induce acute hepatic necrosis. Significant decreases in the activity were found for all three systems. These changes were prevented by supplementing the basal diet with one of the following: methionine, sodium selenite, DL-α-tocopherol acetate, or all three factors plus cystine.There was no significant change in 6-phosphogluconic dehydrogenase activity when it was investigated under similar circumstances.

scholarly journals The transport of oxidized glutathione from the erythrocytes of various species in the prescence of chromate

1969 ◽  
Vol 114 (4) ◽  
pp. 833-837 ◽  
Author(s):  
Satish K. Srivastava ◽  
Ernest Beutler
Keyword(s):  
Hydrogen Peroxide ◽  
Glutathione Reductase ◽  
Pyruvate Kinase ◽  
Transport Rate ◽  
Oxidized Glutathione ◽  
Phosphogluconate Dehydrogenase ◽  
Presence And Absence ◽  
Glucose 6 Phosphate Dehydrogenase

1. Erythrocytes from normal and glucose 6-phosphate dehydrogenase-deficient humans were subjected to hydrogen peroxide diffusion to oxidize the GSH. Studies were carried out in the presence and absence of chromate to inhibit glutathione reductase and with or without the addition of glucose. 2. The GSH content of erythrocytes from other species was oxidized by subjecting them to hydrogen peroxide diffusion in the presence of chromate and glucose. 3. Chromate (1·3mm) inhibited glutathione reductase by about 80%, whereas glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, hexokinase, phosphofructokinase and pyruvate kinase were not inhibited. 4. The GSSG formed was transported from the erythrocytes to the medium. 5. The transport rate of GSSG from glucose 6-phosphate dehydrogenase-deficient erythrocytes subjected to hydrogen peroxide diffusion in the presence of chromate was comparable with that from normal and glucose 6-phosphate dehydrogenase-deficient erythrocytes. 6. The rate of transport of GSSG from erythrocytes of various species studied could be ranked: pigeon>rabbit>rat>donkey>man>dog>horse>sheep>chicken>fish.

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