Catalase activity of IgG antibodies from the sera of healthy donors and patients with schizophrenia

Evgeny A. Ermakov, Ludmila P. Smirnova, Nikolay A. Bokhan, Arkadiy V. Semke, Svetlana A. Ivanova, Valentina N. Buneva, Georgy A. Nevinsky

Результат исследования: Научные публикации в периодических изданияхстатья

6 Цитирования (Scopus)

Аннотация

We present first evidence showing that some electrophoretically homogeneous IgGs from the sera of patients with schizophrenia (36.4%) and their Fab and F(ab)2 fragments as well as from healthy donors (33.3%) possess catalase activity. The relative catalase activity of IgGs from the sera of individual schizophrenia patients (and healthy donors) significantly varied from patient to patient, but the activity of IgGs from healthy donors is on average 15.8-fold lower than that for schizophrenia patients. After extensive dialysis of purified IgGs against EDTA chelating metal ions, the relative catalase activity of IgGs decreases on average approximately 2.5-3.7-fold; all IgGs possess metal-dependent and independent catalase activity. The addition of external Me2+ ions to dialyzed and non-dialyzed IgGs leads to a significant increase in their activity. The best activator of dialyzed and non-dialyzed IgGs is Co2+, the activation by Cu2+, Mn2+, and Ni2+ ions were rare and always lower than by Co2+. Every IgG preparation demonstrates several individual sets of very well expressed pH optima in the pH range from 4.0 to 9.5. These data speak for the individual repertoire of catalase IgGs in every person and an extreme diversity of abzymes in their pH optima and activation by different metal ions. It is known that antioxidant enzymes such as superoxide dismutases, catalases, and glutathione peroxidases represent critical defense mechanisms preventing oxidative modifications of DNA, proteins, and lipids. Catalase activity of human IgGs could probably also play a major role in the protection of organisms from oxidative stress and toxic compounds.

Язык оригиналаанглийский
Номер статьиe0183867
Страницы (с-по)e0183867
Число страниц25
ЖурналPLoS ONE
Том12
Номер выпуска9
DOI
СостояниеОпубликовано - 1 сен 2017

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