Basic components of glutathion system in rat erythrocytes under conditions of toxic damage on the background of an alimental protein lack

Author:

Kopylchuk Halyna1ORCID,Nykolaichuk Ivanna1ORCID

Affiliation:

1. Yuriy Fedkovych Chernivtsi National University

Abstract

The article is devoted to the study of the main components of the glutathione system under conditions of toxic damage against the background of nutritional protein deficiency: the content of reduced and oxidized glutathione with the determination of the GSH/GSSG ratio, the activity of glutathione-dependent enzymes – glutathione peroxidase, glutathione transferase, glutathione reductase, and glucose-6-phosphate dehydrogenase. The concentration of reduced glutathione in the erythrocyte hemolysate was studied using Elman's reagent after deproteinization of the samples. Glutathione transferase activity was determined by the rate of formation of glutathione S conjugates by reacting reduced glutathione with a substrate of 1-chloro-2.4-dinitrobenzene. Glutathione peroxidase activity was evaluated by the formation of oxidized glutathione. The activity of glutathione reductase in erythrocytes was determined by the method, is based on measuring the oxidation rate of NADPH+H+, which is recorded by decreasing absorption at a wavelength of 340 nm. A decrease in the ratio of GSH/GSSG in rat erythrocytes under conditions of toxic damage against a nutritional deficiency of protein is indicated by a functional shift in the thiol-disulfide balance towards increased use of the reduced form of glutathione for antioxidant protection. It was established that toxic damage is a key factor in reducing the level of glutathione transferase against the background of an increase in glutathione peroxidase activity in rat erythrocytes, the activation of which probably prevents the progression of LPO processes. At the same time, under conditions of toxic damage, against the background of alimentary protein deficiency, a decrease in glutathione reductase and glucose-6-phosphate dehydrogenase activity is observed, which leads to blocking of the first stage of glucose-6-phosphate metabolism in the pentose phosphate cycle, resulting in a decrease in the amount of NADPH and, accordingly reduced glutathione.

Publisher

Yuriy Fedkovych Chernivtsi National University

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