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

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 HO) efficiently oxidize different compounds: 3,3'-diaminobenzidine (; DAB), 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (; ATBS), -phenylenediamine (; OPD), homovanillic acid (; HVA), α-naphthol (), 5-aminosalicylic acid (; 5-ASA) and 3-amino-9-ethylcarbazole (; AEC), but seven of nine IgG preparations from different volunteers cannot oxidize -hydroquinone (: pHQ). The average apparent values in the HO-dependent oxidation by human IgGs decreased in the following order (min): 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 HO (oxidoreductase activity), the relative average values decreased in the following order (min): 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 HO and different toxic mutagenic and carcinogenic compounds.