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The Biochemical journal1969; 114(4); 833-837; doi: 10.1042/bj1140833

The transport of oxidized glutathione from the erythrocytes of various species in the presence of chromate.

Abstract: 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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Publication Date: 1969-10-01 PubMed ID: 5387975PubMed Central: PMC1184972DOI: 10.1042/bj1140833Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research examined the way in which oxidized glutathione, or GSSG, is transported from the red blood cells (erythrocytes) of various species when exposed to a substance called chromate. Two types of human red blood cells were studied – normal cells, and those deficient in an enzyme called glucose 6-phosphate dehydrogenase.

Methodology

  • Red blood cells from both humans with normal glucose 6-phosphate dehydrogenase (G6PD) and those deficient in G6PD (an enzyme involved in breaking down carbohydrates) were oxidized by treating them with hydrogen peroxide.
  • The tests were done in both the presence and absence of chromate, used to inhibit an enzyme called glutathione reductase. Some tests also involved the addition of glucose.
  • The same oxidation process was then applied to red blood cells from a range of other species, this time in the presence of both chromate and glucose.

Findings

  • Chromate was found to inhibit glutathione reductase by around 80%. However, chromate appeared to have no inhibitory effect on several other enzymes involved in glucose metabolism, such as glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, hexokinase, phosphofructokinase, and pyruvate kinase.
  • After oxidation with hydrogen peroxide, the GSSG was successfully transported from the red blood cells into the testing medium.
  • The rate at which GSSG was transported from red blood cells deficient in G6PD appeared to be similar to the rate found in normal cells and those deficient in G6PD.
  • The study also found differences in the rate of GSSG transport among red blood cells from a variety of animal species. In descending order, the rates for different species were as follows: pigeon, rabbit, rat, donkey, man, dog, horse, sheep, chicken, fish.

Implications

  • This research may contribute to our understanding of how GSSG is transported in varying conditions, and how this process may differ among species. The findings may be helpful in shedding light on the role of different enzymes in this process.
  • The findings could also contribute to our understanding of diseases related to G6PD deficiency, as well as the potential use of chromate or other substances to interfere with particular enzymatic processes.

Cite This Article

APA
Srivastava SK, Beutler E. (1969). The transport of oxidized glutathione from the erythrocytes of various species in the presence of chromate. Biochem J, 114(4), 833-837. https://doi.org/10.1042/bj1140833

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 114
Issue: 4
Pages: 833-837

Researcher Affiliations

Srivastava, S K
    Beutler, E

      MeSH Terms

      • Adenosine Triphosphate / analysis
      • Animals
      • Biological Transport, Active
      • Chickens
      • Chromates / pharmacology
      • Columbidae
      • Dogs
      • Erythrocytes / metabolism
      • Fishes
      • Glucosephosphate Dehydrogenase Deficiency / metabolism
      • Glutathione / metabolism
      • Glutathione Reductase / antagonists & inhibitors
      • Horses
      • Humans
      • Hydrogen Peroxide
      • In Vitro Techniques
      • Perissodactyla
      • Rabbits
      • Rats
      • Sheep

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