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Cell Biochem Funct. 2000 Jun;18(2):77-84.

Allergy to drugs: antioxidant enzymic activities, lipid peroxidation and protein oxidative damage in human blood.

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  • 1Department of Molecular Biology and Biochemistry, Faculty of Sciences, University of Málaga, Spain.


Reactive oxygen species lead to lipid peroxidation and specific oxidation of some specific enzymes, proteins and other macromolecules, thus affecting many intra- and intercellular systems. Recently, antioxidant functions have been linked to anti-inflammatory properties. Cell defences against toxic oxygen include antioxidant enzymes. We studied the enzymic antioxidant capacity in human blood of both erythrocytes and mononuclear cells from patients suffering from an allergic reaction to different drugs. We determined superoxide dismutases (SODs), glutathione peroxidase (GSHPx) and catalase (CAT) activities in each cell type. We also determined the extent of thiobarbituric acid reactive substances (TBARS) and the oxidative damage to proteins, in order to study the correlation between the cellular enzymic activities, the oxidative status and the allergic reaction. In mononuclear cells from allergic patients, SODs and CAT activities were enhanced compared with controls. Conversely, a decrease in GSHPx activity was found. In erythrocytes, higher values for CAT, GSHPx and SODs activities were found in allergic patients. TBARS were also enhanced in both types of cells, and the carbonyl content of serum was equally increased. The respective enzymic imbalances in mononuclear cells and erythrocytes, namely, GSHPx/SOD and CAT/SOD, and their consequences are discussed. To our knowledge, this is the first global study of antioxidant enzyme determinations, including TBARS level and carbonyl content, in patients suffering from allergies to drugs.

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