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Related Experiment Videos

Ascorbate induced cross-linking of oxyhemoglobin subunits.

A Sur1, K Pal, S Sen

  • 1Department of Biochemistry, University College of Medicine, Calcutta, India.

Indian Journal of Experimental Biology
|August 6, 2000
PubMed
Summary

Ascorbic acid oxidation generates hydrogen peroxide (H2O2), causing oxyhemoglobin cross-linking in vitro. This reaction, independent of hydroxyl radicals, may occur in red blood cells.

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Area of Science:

  • Biochemistry
  • Oxidative Stress
  • Redox Biology

Background:

  • Ascorbic acid (Vitamin C) is a potent antioxidant.
  • Oxidation of ascorbic acid can produce reactive oxygen species.
  • Oxyhemoglobin is the oxygenated form of hemoglobin.

Purpose of the Study:

  • To investigate the in vitro cross-linking of oxyhemoglobin induced by ascorbic acid oxidation.
  • To determine the mechanism of oxyhemoglobin cross-linking mediated by hydrogen peroxide.
  • To explore the potential in vivo physiological significance of this pro-oxidant effect.

Main Methods:

  • In vitro incubation of ascorbic acid and oxyhemoglobin.
  • Oxidation of ascorbic acid to generate hydrogen peroxide.
  • Assessment of non-disulphide covalent cross-linking of oxyhemoglobin.

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  • Use of radical scavengers (mannitol, dimethyl sulphoxide) and a metal-chelator to test for hydroxyl radical involvement.

    • Main Results:

    • Ascorbic acid oxidation generated hydrogen peroxide (H2O2).
    • H2O2 induced non-disulphide covalent cross-linking of coincubated oxyhemoglobin.
    • Radical scavengers and a metal-chelator failed to inhibit the cross-linking process, suggesting no hydroxyl radical involvement.
    • The cross-linking was mediated by H2O2.

    Conclusions:

    • Ascorbic acid's pro-oxidant activity can lead to oxyhemoglobin cross-linking via H2O2.
    • The cross-linking mechanism appears independent of hydroxyl radicals.
    • This process may have physiological relevance in red blood cells in vivo.