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Substrate specificity of IgGs with peroxidase and oxidoreductase activities from sera of patients with systemic lupus erythematosus and multiple sclerosis. / Tolmacheva, Anna S.; Buneva, Valentina N.; Nevinsky, Georgy A.

в: Journal of Molecular Recognition, Том 32, № 12, 2807, 01.12.2019, стр. e2807.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

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Tolmacheva AS, Buneva VN, Nevinsky GA. Substrate specificity of IgGs with peroxidase and oxidoreductase activities from sera of patients with systemic lupus erythematosus and multiple sclerosis. Journal of Molecular Recognition. 2019 дек. 1;32(12):e2807. 2807. Epub 2019 авг. 6. doi: 10.1002/jmr.2807

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@article{9ac5b9a10cac4dcda2456757096a1449,
title = "Substrate specificity of IgGs with peroxidase and oxidoreductase activities from sera of patients with systemic lupus erythematosus and multiple sclerosis",
abstract = "The analysis of IgGs to protect humans from oxidative stress through oxidation of harmful compounds was carried out. We have compared here for the first time peroxidase (in the presence of H2O2) and oxidoreductase (in the absence of H2O2) activities of IgGs from sera of healthy humans and patients with systemic lupus erythematosus (SLE) and multiple sclerosis (MS). In addition, substrate specificity of SLE and MS IgG preparations in the oxidation of different compounds was analyzed: 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), 3,3′-diaminobenzidine (DAB), homovanillic acid (HVA), o-phenylenediamine (OPD), α-naphthol, 3-amino-9-ethylcarbazole (AEC), p-hydroquinone (pHQ), and adrenaline. IgGs of healthy humans and SLE and MS patients oxidized DAB, ABTS, and OPD due to their peroxidase and oxidoreductase activities, while other compounds were substrates of IgGs only in the presence of H2O2: adrenaline was not oxidized by both activities of IgGs. The average SLE IgGs peroxidase activity increased statistically significant in comparison with abzymes from healthy humans in the order (-fold): OPD (1.2) < DAB (1.7) < α-naphtol (2.2) ≤ AEC (2.4) < ABTS (4.5) < 5-ASA (10.6), while with oxidoreductase activity: OPD (1.8) ≤ DAB (2.1-fold) < ABTS (5.0). Only HVA was oxidized by IgGs with peroxidase activity of healthy donors faster than by SLE (1.3-fold) and MS abzymes (2.4-fold). In the oxidation of several substrates, only three IgGs of MS patients were used. The data speak of a tendency to increase the peroxidase and oxidoreductase activities of MS IgGs in comparison with healthy donors, but to a lesser extent: OPD (1.1 to 1.2-fold) ≤ ABTS (1.2 to 1.8-fold). It was shown that development of SLE and MS leads to increase in peroxidase and oxidoreductase activities of IgGs toward most of classical substrates. Thus, abzymes can serve as an additional factor of reactive oxygen species detoxification protecting of patients with SLE and MS from some harmful compounds somewhat better than healthy peoples.",
keywords = "healthy human, IgGs abzymes of sera, multiple sclerosis, oxidoreductase and peroxidase activities, substrate specificities, systemic lupus erythematosus, CATALYTIC ANTIBODIES, COLONY FORMATION, ANTIOXIDANT ENZYMES, RATS, PROLIFERATION, VIRAL-INFECTION, DIFFERENT ABZYMES, AUTOIMMUNE, MICE, DIVERSITY",
author = "Tolmacheva, {Anna S.} and Buneva, {Valentina N.} and Nevinsky, {Georgy A.}",
note = "Publisher Copyright: {\textcopyright} 2019 John Wiley & Sons, Ltd.",
year = "2019",
month = dec,
day = "1",
doi = "10.1002/jmr.2807",
language = "English",
volume = "32",
pages = "e2807",
journal = "Journal of Molecular Recognition",
issn = "0952-3499",
publisher = "John Wiley and Sons Ltd",
number = "12",

}

RIS

TY - JOUR

T1 - Substrate specificity of IgGs with peroxidase and oxidoreductase activities from sera of patients with systemic lupus erythematosus and multiple sclerosis

AU - Tolmacheva, Anna S.

AU - Buneva, Valentina N.

AU - Nevinsky, Georgy A.

N1 - Publisher Copyright: © 2019 John Wiley & Sons, Ltd.

PY - 2019/12/1

Y1 - 2019/12/1

N2 - The analysis of IgGs to protect humans from oxidative stress through oxidation of harmful compounds was carried out. We have compared here for the first time peroxidase (in the presence of H2O2) and oxidoreductase (in the absence of H2O2) activities of IgGs from sera of healthy humans and patients with systemic lupus erythematosus (SLE) and multiple sclerosis (MS). In addition, substrate specificity of SLE and MS IgG preparations in the oxidation of different compounds was analyzed: 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), 3,3′-diaminobenzidine (DAB), homovanillic acid (HVA), o-phenylenediamine (OPD), α-naphthol, 3-amino-9-ethylcarbazole (AEC), p-hydroquinone (pHQ), and adrenaline. IgGs of healthy humans and SLE and MS patients oxidized DAB, ABTS, and OPD due to their peroxidase and oxidoreductase activities, while other compounds were substrates of IgGs only in the presence of H2O2: adrenaline was not oxidized by both activities of IgGs. The average SLE IgGs peroxidase activity increased statistically significant in comparison with abzymes from healthy humans in the order (-fold): OPD (1.2) < DAB (1.7) < α-naphtol (2.2) ≤ AEC (2.4) < ABTS (4.5) < 5-ASA (10.6), while with oxidoreductase activity: OPD (1.8) ≤ DAB (2.1-fold) < ABTS (5.0). Only HVA was oxidized by IgGs with peroxidase activity of healthy donors faster than by SLE (1.3-fold) and MS abzymes (2.4-fold). In the oxidation of several substrates, only three IgGs of MS patients were used. The data speak of a tendency to increase the peroxidase and oxidoreductase activities of MS IgGs in comparison with healthy donors, but to a lesser extent: OPD (1.1 to 1.2-fold) ≤ ABTS (1.2 to 1.8-fold). It was shown that development of SLE and MS leads to increase in peroxidase and oxidoreductase activities of IgGs toward most of classical substrates. Thus, abzymes can serve as an additional factor of reactive oxygen species detoxification protecting of patients with SLE and MS from some harmful compounds somewhat better than healthy peoples.

AB - The analysis of IgGs to protect humans from oxidative stress through oxidation of harmful compounds was carried out. We have compared here for the first time peroxidase (in the presence of H2O2) and oxidoreductase (in the absence of H2O2) activities of IgGs from sera of healthy humans and patients with systemic lupus erythematosus (SLE) and multiple sclerosis (MS). In addition, substrate specificity of SLE and MS IgG preparations in the oxidation of different compounds was analyzed: 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), 3,3′-diaminobenzidine (DAB), homovanillic acid (HVA), o-phenylenediamine (OPD), α-naphthol, 3-amino-9-ethylcarbazole (AEC), p-hydroquinone (pHQ), and adrenaline. IgGs of healthy humans and SLE and MS patients oxidized DAB, ABTS, and OPD due to their peroxidase and oxidoreductase activities, while other compounds were substrates of IgGs only in the presence of H2O2: adrenaline was not oxidized by both activities of IgGs. The average SLE IgGs peroxidase activity increased statistically significant in comparison with abzymes from healthy humans in the order (-fold): OPD (1.2) < DAB (1.7) < α-naphtol (2.2) ≤ AEC (2.4) < ABTS (4.5) < 5-ASA (10.6), while with oxidoreductase activity: OPD (1.8) ≤ DAB (2.1-fold) < ABTS (5.0). Only HVA was oxidized by IgGs with peroxidase activity of healthy donors faster than by SLE (1.3-fold) and MS abzymes (2.4-fold). In the oxidation of several substrates, only three IgGs of MS patients were used. The data speak of a tendency to increase the peroxidase and oxidoreductase activities of MS IgGs in comparison with healthy donors, but to a lesser extent: OPD (1.1 to 1.2-fold) ≤ ABTS (1.2 to 1.8-fold). It was shown that development of SLE and MS leads to increase in peroxidase and oxidoreductase activities of IgGs toward most of classical substrates. Thus, abzymes can serve as an additional factor of reactive oxygen species detoxification protecting of patients with SLE and MS from some harmful compounds somewhat better than healthy peoples.

KW - healthy human

KW - IgGs abzymes of sera

KW - multiple sclerosis

KW - oxidoreductase and peroxidase activities

KW - substrate specificities

KW - systemic lupus erythematosus

KW - CATALYTIC ANTIBODIES

KW - COLONY FORMATION

KW - ANTIOXIDANT ENZYMES

KW - RATS

KW - PROLIFERATION

KW - VIRAL-INFECTION

KW - DIFFERENT ABZYMES

KW - AUTOIMMUNE

KW - MICE

KW - DIVERSITY

UR - http://www.scopus.com/inward/record.url?scp=85070503293&partnerID=8YFLogxK

U2 - 10.1002/jmr.2807

DO - 10.1002/jmr.2807

M3 - Article

C2 - 31389073

AN - SCOPUS:85070503293

VL - 32

SP - e2807

JO - Journal of Molecular Recognition

JF - Journal of Molecular Recognition

SN - 0952-3499

IS - 12

M1 - 2807

ER -

ID: 21240137