Nonselenium Glutathione Peroxidase in Human Brain
نویسندگان
چکیده
منابع مشابه
Phospholipid hydroperoxide glutathione peroxidase activity of human glutathione transferases.
Human glutathione transferases (GSTs) from Alpha (A), Mu (M) and Theta (T) classes exhibited glutathione peroxidase activity towards phospholipid hydroperoxide. The specific activities are in the order: GST A1-1>GST T1-1>GST M1-1>GST A2-2>GST A4-4. Using a specific and sensitive HPLC method, specific activities towards the phospholipid hydroperoxide,1-palmitoyl-2-(13-hydroper oxy-cis-9, trans-1...
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Glutathione peroxidase has been purified to homogeneity from human erythrocytes. The purification steps involved ammonium sulfate precipitation of hemolysate, CM-cellulose (CM-52), DEAE-cellulose (DE52), Sephadex G-200, and DEAE-Sephadex column chromatography. In the last step, i.e. DEAE-Sephadex A-25 column chromatography, the enzyme was eluted in a major peak and tailing fraction. The major p...
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Glutathione peroxidase (glutathione--H2O2 oxidoreductase; EC 1.11.1.9) was purified to homogeneity from human placenta by using (NH4)2SO4 precipitation, ion-exchange chromatography, Sephadex gel filtration and preparative polyacrylamide-disc-gel electrophoresis. Glutathione peroxidase from human placenta is a tetramer, having 4g-atoms of selenium/mol of protein. The molecular weight of the enzy...
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ژورنال
عنوان ژورنال: The American Journal of Pathology
سال: 2002
ISSN: 0002-9440
DOI: 10.1016/s0002-9440(10)64249-6