Literature DB >> 2996939

Myeloperoxidase oxidation of sulfur-centered and benzoic acid hydroxyl radical scavengers.

T R Green, J H Fellman, A L Eicher.   

Abstract

Myeloperoxidase (MPO) oxidizes sulfur-centered and benzoate hydroxyl radical scavengers through formation of HOCl. Sulfur-centered hydroxyl radical scavengers compete with benzoate as antioxidants of HOCl. We conclude from these observations that competition experiments between benzoate and sulfur-centered hydroxyl radical scavengers are not sufficiently specific to infer participation of hydroxyl radicals in oxidative reactions mediated by neutrophils because of the unique action of MPO in affecting oxidation of the test radical scavengers.

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Year:  1985        PMID: 2996939     DOI: 10.1016/0014-5793(85)80037-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  The specificity of thiourea, dimethylthiourea and dimethyl sulphoxide as scavengers of hydroxyl radicals. Their protection of alpha 1-antiproteinase against inactivation by hypochlorous acid.

Authors:  M Wasil; B Halliwell; M Grootveld; C P Moorhouse; D C Hutchison; H Baum
Journal:  Biochem J       Date:  1987-05-01       Impact factor: 3.857

2.  The antioxidant action of human extracellular fluids. Effect of human serum and its protein components on the inactivation of alpha 1-antiproteinase by hypochlorous acid and by hydrogen peroxide.

Authors:  M Wasil; B Halliwell; D C Hutchison; H Baum
Journal:  Biochem J       Date:  1987-04-01       Impact factor: 3.857

3.  Neutrophil degranulation inhibits potential hydroxyl-radical formation. Relative impact of myeloperoxidase and lactoferrin release on hydroxyl-radical production by iron-supplemented neutrophils assessed by spin-trapping techniques.

Authors:  B E Britigan; D J Hassett; G M Rosen; D R Hamill; M S Cohen
Journal:  Biochem J       Date:  1989-12-01       Impact factor: 3.857

4.  Rapid and sensitive detection of hydroxyl radicals formed by activated neutrophils in the presence of chelated iron: hydroxylation of deoxyguanosine to 8-hydroxydeoxyguanosine.

Authors:  P Leanderson; C Tagesson
Journal:  Agents Actions       Date:  1992-05
  4 in total

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