Cited by 148Antioxidant Activity and Oxidative StressFree Radicals and AntioxidantsRedox biology and oxidative stress

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Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins

Gutteridge, John M.C., Quinlan, Gregory J.·1992·Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

DOI 10.1016/0167-4838(92)90052-f

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Abstract

Normal human plasma contains numerous high- and low-molecular-mass redox-active molecules that are able to react rapidly with organic and inorganic oxygen radicals. The ability of such plasma molecules to substantially inhibit, or delay, free-radical mediated oxidation of added substrates has led to their classification as important biological antioxidants. Using phospholipids to detect organic oxygen radicals and deoxyribose to detect inorganic oxygen radicals, we here show that the primary antioxidants of normal human plasma reside mainly in two plasma proteins representing no more than 4% of the total proteins present. The iron-binding properties of transferrin and the iron-oxidising properties of caeruloplasmin, at a reaction dilution of 1:50, offer considerable protection against organic and inorganic oxygen radicals generated by iron and ascorbate. Plasma thiol-group-containing molecules, at concentrations well below those that would be required to compete with the detector molecule (based on known second-order rate constants for reaction with hydroxyl radicals) inhibited damage to deoxyribose, but stimulated damage to phospholipids.

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Authors: Gutteridge, J. M. C., & Quinlan, G. J.
Affiliations: Royal Brompton Hospital (GB)
Corresponding author: Gutteridge, John M.C.
ORCID: Quinlan, Gregory J.
Venue: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Publisher: Elsevier BV
Published: 1992-10
Volume: 1159
Issue: 3
Pages: 248-254
ISSN: 0167-4838 (ISSN-L)
DOI: 10.1016/0167-4838(92)90052-f
OpenAlex: W2026312693
Cited by: 148
References: 46
Citations by year: 2024: 1 · 2023: 3 · 2021: 3 · 2020: 1 · 2017: 1 · 2015: 1 · 2014: 4 · 2013: 5 · 2012: 4
FWCI: 5.92
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (publishedVersion)
PubMed (publishedVersion)
PubMed
Funders: British Lung Foundation
Topics: Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: plasma antioxidants, oxygen free radicals, hydroxyl radicals, superoxide, transferrin, ceruloplasmin, iron-binding proteins, phospholipid oxidation, deoxyribose oxidation, vitamin C, sulfhydryl groups, human plasma
MeSH terms: Antioxidants, Blood Proteins, Carrier Proteins, Humans, Hydroxides, Iron, Plasma, Free Radical Scavengers, Hydroxyl Radical, Iron-Binding Proteins, Transferrin-Binding Proteins, In Vitro Techniques

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Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins

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