Phenol and catechol induce prehemolytic and hemolytic changes in human erythrocytes.

The toxic potency of two industrially used compounds (phenol and catechol) was studied in human blood cells in vitro. Catechol was found to be a more harmful toxin than phenol, since it provokes statistically significant changes in the function of erythrocytes even at low doses. Most of the changes was statistically significant for the doses of 50 ppm of catechol and 250 ppm of phenol. Both compounds induced methaemoglobin formation, glutathione depletion and conversion of oxyhaemoglobin to methaemoglobin, which is associated with superoxide anion production and lead to formation of ferryl hemoglobin, hydrogen peroxide or hydroxyl radicals. It is known that oxidation of catechol leads to formation of semiquinone radicals. Semiquinones are able to bind to nucleophilic residues like -SH or -NH2 of proteins and these macromolecules may undergo inactivation. We observed among especially susceptible to action of catechol are catalase (CAT) (100 ppm) and superoxide dismutase (SOD) (250 ppm). Decrease of the activity of catalase and SOD by catechol induced radical species formation. This lead to inhibition of another protective enzymes such as glutathione-S-transferase (500 ppm), glutathione reductase (1000 ppm), glucose-6-phosphate dehydrogenase activity (1000 ppm). Cytotoxicity of phenol or catechol was noted as hemolysis. Haemoglobin liberated from erythrocytes in this process may further generate oxygen free radicals and subsequently initiate enzymes damage. It seems to be essential that in phenol and catechol toxicity special role play damages of heme proteins and other proteins molecule, and damages of lipids are not so important.