Abstract
The subcellular distributions of glutathione peroxidase and 75Se in rat liver were determined. Approximately 75% of the enzyme and 58% of the 73Se were contained in the cytosolic fraction. Rat liver cytosol glutathione peroxidase was purified 1029-fold from homogenate to yield a sample with a specific activity of 278 μmol of NADPH oxidized/ min/mg of protein. The purified enzyme was subjected to disc-gel and sodium dodecyl sulfate-disc-gel electrophoresis, which confirmed the purity of the enzyme as well as the existence of multiple electrophoretic forms. Glutathione peroxidase existed as a large aggregate after homogenization, and means of dissociating the aggregate were investigated. The enzyme was isolated as a neutrally charged protein and became negatively charged upon storage, a phenomenon that was independent of the aggregation.
Original language | English |
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Pages (from-to) | 490-497 |
Number of pages | 8 |
Journal | Archives of Biochemistry and Biophysics |
Volume | 183 |
Issue number | 2 |
DOIs | |
State | Published - 10 1977 |
Externally published | Yes |