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Activation of red blood cell glutathione peroxidase and morphological transformation of erythrocytes under the action of tert‐butyl hydroperoxide
Author(s) -
Zavodnik Lev B.,
Zavodnik Ilya B.,
Niekurzak Andrzej,
Szosland Konrad,
Bryszewska Maria
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201612
Subject(s) - tert butyl hydroperoxide , peroxidase , glutathione , transformation (genetics) , chemistry , red blood cell , glutathione peroxidase , biochemistry , blood cell , microbiology and biotechnology , biophysics , biology , enzyme , immunology , gene , catalysis
Susceptibility of control and diabetic erythrocytes to oxidative stress was measured after incubation with various concentration of tert‐butyl hydroperoxide (t‐BHP). TBA‐reactive substances (TBARS) formed were determined by the method of Stocks & Dormady [9] modified by Jain [2]. GSH and total glutathione were estimated by the procedure of Ellman [10] and Akerboom and Sies [11]. Activity of GSH peroxidase was determined by the method of Martinez et al. [12]. Protein SH groups were determined after membrane isolation by the method of Dodge et al. [13]. Cell morphology was viewed under phase contrast microscope with a magnification of 500x. All results were analyzed by the unpaired two tailed Student's t‐test. Oxidative treatment of erythrocytes with tert‐butyl hydroperoxide significantly increases the reaction rate but decreases the affinity for substrate (tert‐butyl hydroperoxide). The susceptibility of the enzyme from diabetic erythrocytes to oxidation is higher in comparison with normal cells. The oxidation of cellular reduced glutathione (GSH) is not correlated with oxidation of membranous protein SH‐groups. Oxidative damage of erythrocytes induces significant cell morphological transformations.