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We have carried out an analysis of whether blood IgG antibodies can protect humans from oxidative stress by oxidizing different harmful compounds. A somewhat unexpected result was obtained. We show here for the first time that healthy human sera IgGs with the peroxidase (in the presence H 2 O 2 ) efficiently oxidize different compounds: 3,3′-diaminobenzidine ( 1 ; DAB), 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt ( 2 ; ATBS),  o -phenylenediamine ( 3 ; OPD), homovanillic acid ( 4 ; HVA), α-naphthol ( 5 ), 5-aminosalicylic acid ( 6 ; 5-ASA) and 3-amino-9-ethylcarbazole ( 7 ; AEC), but seven of nine IgG preparations from different volunteers cannot oxidize  p -hydroquinone ( 8 : pHQ). The average apparent  k  cat  values in the H 2 O 2 -dependent oxidation by human IgGs decreased in the following order (min −1 ): ATBS (73.7) ≥ DAB (66.3) > AEC (38.0) ≥ HVA (19.8) ≥ α-naphthol (8.6) > OPD (0.62) ≥ 5-ASA (0.48) > pHQ (0.24). In the absence of H 2 O 2  (oxidoreductase activity), the relative average  k  cat  values decreased in the following order (min −1 ): DAB (52.1) ≥ ATBS (50.5) > OPD (0.25). The peroxidase average activity of human IgGs was higher than the oxidoreductase one: 1.2-, 1.5- and 2.5-fold for DAB, ATBS and OPD, respectively. It should be assumed that antibodies can oxidize in addition to the large number of other different compounds analysed by us. As a whole, the specific wide repertoire of polyclonal human IgGs oxidizing various compounds could play an important role in protecting humans from oxidative stress and serve as an additional natural system destroying H 2 O 2  and different toxic mutagenic and carcinogenic compounds.

Substrate specificity of healthy human sera IgG antibodies with peroxidase and oxydoreductase activities