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Substrate specificity of healthy human sera IgG antibodies with peroxidase and oxydoreductase activities. / Tolmacheva, Anna S.; Ermakov, Evgeny A.; Buneva, Valentina N. et al.
In: Royal Society Open Science, Vol. 5, No. 1, 171097, 31.01.2018, p. 171097.Research output: Contribution to journal › Article › peer-review
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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 -
ID: 10423025