TY - JOUR

T1 - Substrate specificity of healthy human sera IgG antibodies with peroxidase and oxydoreductase activities

AU - Tolmacheva, Anna S.

AU - Ermakov, Evgeny A.

AU - Buneva, Valentina N.

AU - Nevinsky, Georgy A.

PY - 2018/1/31

Y1 - 2018/1/31

N2 - 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 H2 O2) 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 kcat values in the H2 O2 -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 H2 O2 (oxidoreductase activity), the relative average kcat 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 H2O2 and different toxic mutagenic and carcinogenic compounds.

AB - 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 H2 O2) 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 kcat values in the H2 O2 -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 H2 O2 (oxidoreductase activity), the relative average kcat 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 H2O2 and different toxic mutagenic and carcinogenic compounds.

KW - Abzymes

KW - IgGs

KW - Oxidoreductase and peroxidase activities

KW - Sera of healthy human

KW - Substrate specificities

KW - AUTOANTIBODIES

KW - CATALYTIC ANTIBODIES

KW - sera of healthy human

KW - COLONY FORMATION

KW - ANTIOXIDANT ENZYMES

KW - HYDROLYSIS

KW - RATS

KW - ABZYMES

KW - oxidoreductase and peroxidase activities

KW - MYELIN BASIC-PROTEIN

KW - AUTOIMMUNE

KW - substrate specificities

KW - OXIDOREDUCTASE ACTIVITIES

KW - abzymes

UR - http://www.scopus.com/inward/record.url?scp=85041540579&partnerID=8YFLogxK

U2 - 10.1098/rsos.171097

DO - 10.1098/rsos.171097

M3 - Article

C2 - 29410824

AN - SCOPUS:85041540579

VL - 5

SP - 171097

JO - Royal Society Open Science

JF - Royal Society Open Science

SN - 2054-5703

IS - 1

M1 - 171097

ER -