Статья

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

A. Tolmacheva, E. Ermakov, V. Buneva, G. Nevinsky,
2021

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. © 2018 The Authors.

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  • 1. Version of Record от 2021-04-27

Метаданные

Об авторах
  • A. Tolmacheva
    Institute of Cytology and Genetics, Siberian Division of Russian Academy of Sciences, 10 Lavrentiev Avenue, Novosibirsk, Russian Federation
  • E. Ermakov
    Siberian Division of Russian Academy of Sciences, Institute of Chemical Biology and Fundamental Medicine, 8 Lavrentiev Avenue, Novosibirsk, 630090, Russian Federation
  • V. Buneva
    Novosibirsk State University, 2 Pirogova Street, Novosibirsk, 630090, Russian Federation
  • G. Nevinsky
Название журнала
  • Royal Society Open Science
Том
  • 5
Выпуск
  • 1
Страницы
  • -
Издатель
  • Royal Society Publishing
Тип документа
  • journal article
Тип лицензии Creative Commons
  • CC
Правовой статус документа
  • Свободная лицензия
Источник
  • scopus