Effect of Prolonged Storage on the Activities of Superoxide Dismutase, Glutathione Reductase, and Glutathione Peroxidase

[摘要] Reactive oxygen species such as superoxide and hydrogen peroxide react in human tissues to form hydroxyl free radicals, especially when catalyzed by transition metals, e.g., iron [Fe(II)] and copper [Cu(I)]. The product is highly electrophilic and damaging to surrounding tissues and is implicated in the pathology of debilitating human diseases such as atherosclerosis (1), Parkinson disease and other neurodegenerative disorders (2), and cancer (3). Copper zinc-superoxide dismutase (CuZn-SOD; EC 1.15.1.1), glutathione peroxidase (GPX; EC 1.11.1.9), and glutathione reductase (GR; EC 1.6.4.2) are cellular antioxidants that can protect cells from the potentially harmful effects of reactive oxygen species (4)(5)(6). Assays of the activities of these mainly intracellular enzymes form part of the indirect determination of the activity of free radicals.Measurements of erythrocyte CuZn-SOD, GPX, and GR activities usually are performed in the assessment of antioxidant status, and there has been speculation on the stability of these enzymes over a long period of storage. In this study, we investigated the long-term stability of CuZn-SOD, GPX, and GR in washed erythrocyte hemolysates by comparing the activities in stored hemolysates with those in hemolysates from freshly drawn blood. Subjects were recruited from blood donors (n = 24) with the consent of the ethics committee. The blood donors fulfilled the health requirements of the blood transfusion center, i.e., absence of contagious disease, medication, or history of viral hepatitis, …

[学科分类] 过敏症与临床免疫学