The autoxidation of horse hemoglobin: the effect of glutathione.
Abstract: The reduced glutathione in the erythrocyte was found to inhibit the autoxidation of purified horse hemoglobin. It was observed that much higher concentrations of oxidized glutathione also stabilize hemoglobin. The stabilization by oxidized glutathione most likely involves the formation of a mixed disulfide with the reactive β-93 sulfhydryl groups on the hemoglobin. A similar effect is also observed with N-ethyl- maleimide and HgCl2 which also react with the sulfhydryl groups. The apparent stabilization by reduced glutathione is partially due to the reduction of ferrihemoglobin formed by autoxidation. Reduced glutathione may also indirectly react with the β-93 sulfhydryl groups further stabilizing the hemoglobin. A mechanism coupling such a reaction to the one electron reduction of ferrihemoglobin by reduced glutathione is discussed.
Publication Date: 1972-06-26 PubMed ID: 5038285DOI: 10.1016/0304-4165(72)90188-2Google Scholar: Lookup
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- Journal Article
Summary
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The research article discusses the role of reduced glutathione in inhibiting the autoxidation process of horse hemoglobin and emphasizes on the potential mechanisms involved in this process.
Role of Glutathione in Inhibiting Autoxidation of Hemoglobin
- The study showed that reduced glutathione, present within the red blood cells, significantly inhibited the autoxidation process of horse hemoglobin. Autoxidation is a natural oxidizing process that damages the structure and function of hemoglobin, a protein responsible for carrying oxygen in the blood.
- The researchers also observed that not only reduced glutathione but also higher concentrations of oxidized glutathione could stabilize hemoglobin, suggesting a broader role of glutathione in hemoglobin stability.
Mechanism of Hemoglobin Stabilization by Glutathione
- The stabilization effect of oxidized glutathione on hemoglobin was theorized to involve the formation of a mixed disulfide bond with the β-93 sulfhydryl groups present on the hemoglobin. Sulfhydryl groups are reactive sulfur-containing entities found in proteins and can participate in a variety of molecular interactions.
- The study found a similar stabilization effect with two other compounds, N-ethyl-maleimide and HgCl2, which also interact with the sulfhydryl groups, confirming the essential role of these groups in hemoglobin stability.
Role of Reduced Glutathione in Hemoglobin Stabilization
- Interestingly, the apparent stabilization effect of reduced glutathione was seen to be due to its ability to reduce ferrihemoglobin, a form of hemoglobin that is produced during the autoxidation process.
- The researchers proposed that reduced glutathione might also indirectly interact with the β-93 sulfhydryl groups on the hemoglobin, further contributing to its stabilization.
- Evidence was provided to suggest a mechanism where this reaction is coupled with the one-electron reduction of ferrihemoglobin by reduced glutathione, although this aspect requires further investigation.
Cite This Article
APA
Rifkind JM.
(1972).
The autoxidation of horse hemoglobin: the effect of glutathione.
Biochim Biophys Acta, 273(1), 30-39.
https://doi.org/10.1016/0304-4165(72)90188-2 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Chemical Phenomena
- Chemistry
- Chromatography, Gel
- Disulfides / chemical synthesis
- Drug Stability
- Erythrocytes / analysis
- Ethylmaleimide
- Glutathione / blood
- Hemoglobins / isolation & purification
- Horses
- Kinetics
- Mercury
- Oxidation-Reduction
- Oxygen
- Protein Binding
- Spectrophotometry
- Sulfhydryl Compounds
Citations
This article has been cited 2 times.- Viskupicova J, Blaskovic D, Galiniak S, Soszyński M, Bartosz G, Horakova L, Sadowska-Bartosz I. Effect of high glucose concentrations on human erythrocytes in vitro.. Redox Biol 2015 Aug;5:381-387.
- Furlan M, Bachofen H. Auto-oxidation of hemoglobin in plasma.. Experientia 1976 Jan 15;32(1):113-4.
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