Comparative aspects of methemoglobin formation and reduction in opossum (Didelphis virginiana) and human erythrocytes

doi:10.1016/0300-9629(83)90433-4

Comparative Biochemistry and Physiology Part A: Physiology

Volume 75, Issue 4, 1983, Pages 635-639

Comparative Biochemi...

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Abstract

1.
1.Glucose-depleted, nitrite-treated opossum erythrocytes effectively reduce methemoglobin in an environment of physiological saline and added glucose does not accelerate the rate of reduction.
2.
2.In autologous plasma or 25 mM phosphate-buffered saline pH 7.4, added glucose significantly accelerates methemoglobin reduction in glucose-depleted, nitrite-treated opossum erythrocytes.
3.
3.Human red cells require added glucose to carry out reduction of methemoglobin and increased phosphate concentration or autologous plasma does not alter the rate of this process.
4.
4.Within the opossum red cell in vitro, autooxidation of hemoglobin proceeds at a much slower rate than that observed in human erythrocytes.

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Cytosolic and membrane-bound methemoglobin reductases in erythrocytes of the Opossum Didelphis virginiana
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K.A Evelyn et al.
Microdetermination of oxygenhemoglobin and sulfhemoglobin in a simple sample of blood
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Oxidation-reduction properties of the hemoglobin of the Opossum Didelphis virginiana
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Analysis of met-form hemoglobin in glucose-depleted human red cells
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C.V Tondo
Increased erythrocyte glutathione reductase activity in a hemoglobin Porto Alegre (β9ser → cys) carrier
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E Beutler

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Effect of freezing red blood cells and hemolysates at different temperatures. Electrophoretic and methemoglobin studies

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R.G Chapman et al.

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Energy metabolism in human erythrocytes. l. Effects of sodium fluoride

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The NADH/NADPH methemoglobin reduction system of erythrocytes

Cited by (10)

Asymmetric hemoglobins, their thiol content, and blood glutathione of the scalloped hammerhead shark, Sphyrna lewini
1997, Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Starch gel electrophoresis pH 8.6, or PAGE pH 8.9, of the scalloped hammerhead shark hemolysates showed three hemoglobins (Hb). An additional Hb between the two most mobile electrophoretic components was seen in starch gel electrophoresis, pH 8.1, and also in highly loaded PAGE gels. The relative concentration of these Hbs was variable among individuals, when accessed at pH 8.1. Dilution of hemolysates led to a redistribution of the Hb tetramer subunits. Under denaturing conditions, the unfractionated hemolysate was resolved in 3 Hb subunits. Isolated Hbs, named SL I–SL IV, showed unusual subunit compositions: SL I, the least mobile, is “b₃c”; SL II is “a₂bc”; SL III and SL IV are composed only by “a” subunits. Hemoglobins in the whole hemolysate have an average of two reactive cysteines per tetramer, which were not easily S-thiolated by glutathione, as is the case for related species. After hemoglobin denaturation, six additional -SH groups were titrated by Ellman's reagent. Methemoglobin content was low in the erythrocytes of nine examined specimens, 1.13 ± 1.90%. High values for total erythrocyte glutathione (GSH) were found: 4.5 ± 0.7 mM; n = 7. The ratio of 1.4 ± 0.4 GSH/Hb is higher than usually reported for mammalians.
Studies on the energy metabolism of opossum (didelphis virginiana) erythrocytes-VI. De novo purine nucleotide biosynthesis is limited to the final steps of the pathway in vitro
1990, Comparative Biochemistry and Physiology -- Part B: Biochemistry and
- 1.
  1. High pressure liquid radiochromatography was used to show the incorporation of [¹⁴C] formate with Z-compounds into ATP and GTP in opossum erythrocytes.
- 2.
  2. The use of Z-riboside with [¹⁴C] formate resulted in more extensive labeling of ATP than the Z-base/[¹⁴C] formate combination as substrates for nucleotide biosynthesis
- 3.
  3. Substantial accumulation of ZMP and ZTP, but no ZDP was detected in the chromatograms.
- 4.
  4. ATP was unstable in red cells metabolizing in the presence of Z-compounds under an atmosphere of air as gas phase in these experiments.
Studies on the energy metabolism of opossum Didelphis Virginiana erythrocytes-IV. Red cells have low adenosine deaminase activity and high levels of deoxyadenosine nucleotides
1989, Life Sciences
Alkaline extracts of adult opossum red cells were used to determine triphosphates of adenosine, deoxyadenosine and guanosine by anion exchange HPLC. Mean (nm/g Hg) ATP content of erythrocytes was 3713 and that of dATP 1913 (n = 12). Sonicates of red cells deaminated adenosine (ADO) at a rate of 1.55 nm/mg Hg/h and deoxyadenosine (dADO) at 1.82 nm/mg Hg/h. dATP synthesis from provided dADO was one order of magnitude greater in opossum than in human erythrocytes at both low and high dADO and Pi concentrations.
Studies on the energy metabolism of opossum Didelphis virginiana erythrocytes-III. Metabolic depletion with 2-deoxyglucose markedly accelerates methemoglobin reduction in opossum but not in human erythrocytes
1988, Comparative Biochemistry and Physiology -- Part A: Physiology
- 1.
  1. Glucose-depleted, nitrite-treated erythrocytes reduce ferriheme in vitro in an environment 100 mM to 2-deoxy-d-glucose at a rate of 2.4μM/ml cells/hr (opossum) and 0.37 μM/ml cells/hr (human).
- 2.
  2. During the process of methemoglobin reduction the breakdown of adenine ribonucleotides is more rapid in opossum (0.9μM/g hg/hr) than in human (0.36μM/g hg/hr) erythrocytes.
- 3.
  3. Radiolabelled ribose from [U-¹⁴C] ATP is catabolized exclusively to [¹⁴C] lactate in opossum, and to [¹⁴C] pyruvate and [¹⁴C] lactate in human red cells.
Studies on the energy metabolism of opossum Didelphis virginiana erythrocytes-II. Comparative aspects of 2-deoxy-d-glucose catabolism in opossum and human red cells in vitro
1988, Comparative Biochemistry and Physiology -- Part A: Physiology
- 1.
  1. G-6-P, F-6-P, F-1, 6-P, DHAP and GA-3-P in opossum erythrocytes were found at levels above those reported in human red cells.
- 2.
  2. About 1% of the radioactivity provided as [1-¹⁴C] DOG to red cells of both species was recovered as ¹⁴CO₂ in 1 hr.
- 3.
  3. Unlike [1-¹⁴C] DOG, radiochromatography of extracts of cells incubated with [U-¹⁴C] or [2,6 P³H] DOG revealed two diffusible radiolabelled compounds in the supernatant of cell suspensions.
- 4.
  4. The catabolism of DOG was quantitatively and qualitatively similar in opossum and human erythrocytes under the conditions of this study.
High sulfhydryl content in turtle erythrocytes: Is there a relation with resistance to hypoxia?
1986, Comparative Biochemistry and Physiology -- Part B: Biochemistry and
- 1.
  1. Glutathione concentration in the erythrocytes of the fresh-water turtle Phrynops hilarii, as determined by the enzymic recycling method is 1.9 ± 0.2 mM.
- 2.
  2. The erythrocyte non-protein —SH, NPSH, content, as determined by the 5,5′ dithiobis(2-nitrobenzoic acid), DTNB, reducing capacity is 4.6 ± 0.8 mM.
- 3.
  3. The total DTNB reducing capacity in the erythrocytes, including hemoglobin, is 26 ± 5 mM.
- 4.
  4. Incubation with oxidized glutathione, greatly increases the electrophoretic mobility of both hemoglobin components present in the erythrocytes of Phrynops hilarii, indicating the formation of mixed disulphides with glutathione.
- 5.
  5. The high—SH content in the erythrocytes of P. hilarii might be part of a redox buffering principally an antioxidant mechanism involved in resistance to hypoxia, possibly along the hypoxic period as well as during reperfusion with oxygen.

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^☆: The opinions or assertions contained herein are the private views of the authors and are not to be construed as official or as reflecting the views of the Department of the Army and the Department of Defense.

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Comparative Biochemistry and Physiology Part A: Physiology

Abstract

References (28)

Cytosolic and membrane-bound methemoglobin reductases in erythrocytes of the Opossum Didelphis virginiana

Comp. Biochem. Physiol.

Microdetermination of oxygenhemoglobin and sulfhemoglobin in a simple sample of blood

J. biol. Chem.

Oxidation-reduction properties of the hemoglobin of the Opossum Didelphis virginiana

Comp. Biochem. Physiol.

The metabolism of glutathione of human blood

Biochim. biophys Acta

The autoxidation of horse hemoglobin: the effect of glutathione

Biochim. biophys. Acta

Control of glycolysis in the human red blood cell

J. biol. Chem.

Opossum hemoglobin. The amino acid sequences of the alpha and beta chains

J. biol. Chem.

Analysis of met-form hemoglobin in glucose-depleted human red cells

FEBS Lett.

Increased erythrocyte glutathione reductase activity in a hemoglobin Porto Alegre (β9ser → cys) carrier

Biochem. biophys Res. Commun.

Effect of freezing red blood cells and hemolysates at different temperatures. Electrophoretic and methemoglobin studies

Archs Biochem. Biophys.

Erythrocyte metabolism. V. Levels of glycolytic enzymes and regulation of glycolysis

J. clin. Invest.

Energy metabolism in human erythrocytes. l. Effects of sodium fluoride

J. clin. Invest.

The NADH/NADPH methemoglobin reduction system of erythrocytes

Cited by (10)

Asymmetric hemoglobins, their thiol content, and blood glutathione of the scalloped hammerhead shark, Sphyrna lewini

Studies on the energy metabolism of opossum (didelphis virginiana) erythrocytes-VI. De novo purine nucleotide biosynthesis is limited to the final steps of the pathway in vitro

Studies on the energy metabolism of opossum Didelphis Virginiana erythrocytes-IV. Red cells have low adenosine deaminase activity and high levels of deoxyadenosine nucleotides

Studies on the energy metabolism of opossum Didelphis virginiana erythrocytes-III. Metabolic depletion with 2-deoxyglucose markedly accelerates methemoglobin reduction in opossum but not in human erythrocytes

Studies on the energy metabolism of opossum Didelphis virginiana erythrocytes-II. Comparative aspects of 2-deoxy-d-glucose catabolism in opossum and human red cells in vitro

High sulfhydryl content in turtle erythrocytes: Is there a relation with resistance to hypoxia?

Comparative aspects of methemoglobin formation and reduction in opossum (Didelphis virginiana) and human erythrocytes☆

Abstract

Comp. Biochem. Physiol.

J. biol. Chem.

Comp. Biochem. Physiol.

Biochim. biophys Acta

Biochim. biophys. Acta

J. biol. Chem.

J. biol. Chem.

FEBS Lett.

Biochem. biophys Res. Commun.

Effect of freezing red blood cells and hemolysates at different temperatures. Electrophoretic and methemoglobin studies

Archs Biochem. Biophys.

Erythrocyte metabolism. V. Levels of glycolytic enzymes and regulation of glycolysis

J. clin. Invest.

Energy metabolism in human erythrocytes. l. Effects of sodium fluoride

J. clin. Invest.

The NADH/NADPH methemoglobin reduction system of erythrocytes