Ascorbate-dependent formation of hydroxyl radicals in the presence of iron chelates.

H. R. Prabhu, S. Krishnamurthy

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The autoxidation of L-ascorbate on incubation in saline phosphate buffer (pH 7.4) is accompanied by hydroxyl radical (.OH) generation. The metal chelator EDTA showed significant inhibition of ascorbate autoxidation and ascorbate-dependent .OH release. On the other hand, Fe2+ (EDTA) greatly augmented both ascorbate autoxidation and ascorbate-dependent .OH production. The biological iron chelating compounds such as ATP, ADP, citrate and pyrophosphate suppressed both ascorbate autoxidation and ascorbate-mediated .OH production, thereby indicating that these compounds suppress the activating effect of iron. Ascorbate autoxidation and ascorbate-dependent .OH formation, stimulated by Fe2+ (EDTA) were significantly inhibited by .OH scavengers, namely mannitol, thiourea and sodium formate, as well as by catalase and to a lesser extent by bovine serum albumin, superoxide dismutase (native and heat denatured) and heat denatured catalase.

Original languageEnglish
Pages (from-to)289-292
Number of pages4
JournalIndian Journal of Biochemistry and Biophysics
Volume30
Issue number5
Publication statusPublished - 01-10-1993
Externally publishedYes

Fingerprint

Iron Chelating Agents
Edetic Acid
Hydroxyl Radical
formic acid
Catalase
Iron
Hot Temperature
Iron Compounds
Thiourea
Mannitol
Chelating Agents
Bovine Serum Albumin
Chelation
Citric Acid
Adenosine Diphosphate
Superoxide Dismutase
Buffers
Adenosine Triphosphate
Metals
Phosphates

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics

Cite this

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abstract = "The autoxidation of L-ascorbate on incubation in saline phosphate buffer (pH 7.4) is accompanied by hydroxyl radical (.OH) generation. The metal chelator EDTA showed significant inhibition of ascorbate autoxidation and ascorbate-dependent .OH release. On the other hand, Fe2+ (EDTA) greatly augmented both ascorbate autoxidation and ascorbate-dependent .OH production. The biological iron chelating compounds such as ATP, ADP, citrate and pyrophosphate suppressed both ascorbate autoxidation and ascorbate-mediated .OH production, thereby indicating that these compounds suppress the activating effect of iron. Ascorbate autoxidation and ascorbate-dependent .OH formation, stimulated by Fe2+ (EDTA) were significantly inhibited by .OH scavengers, namely mannitol, thiourea and sodium formate, as well as by catalase and to a lesser extent by bovine serum albumin, superoxide dismutase (native and heat denatured) and heat denatured catalase.",
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Ascorbate-dependent formation of hydroxyl radicals in the presence of iron chelates. / Prabhu, H. R.; Krishnamurthy, S.

In: Indian Journal of Biochemistry and Biophysics, Vol. 30, No. 5, 01.10.1993, p. 289-292.

Research output: Contribution to journalArticle

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AB - The autoxidation of L-ascorbate on incubation in saline phosphate buffer (pH 7.4) is accompanied by hydroxyl radical (.OH) generation. The metal chelator EDTA showed significant inhibition of ascorbate autoxidation and ascorbate-dependent .OH release. On the other hand, Fe2+ (EDTA) greatly augmented both ascorbate autoxidation and ascorbate-dependent .OH production. The biological iron chelating compounds such as ATP, ADP, citrate and pyrophosphate suppressed both ascorbate autoxidation and ascorbate-mediated .OH production, thereby indicating that these compounds suppress the activating effect of iron. Ascorbate autoxidation and ascorbate-dependent .OH formation, stimulated by Fe2+ (EDTA) were significantly inhibited by .OH scavengers, namely mannitol, thiourea and sodium formate, as well as by catalase and to a lesser extent by bovine serum albumin, superoxide dismutase (native and heat denatured) and heat denatured catalase.

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