Abstract
Purified rat liver soluble glutathione peroxidase, with a specific activity of 280 μmol of NADPH oxidized/min/mg of protein, was studied by X-ray photoelectron spectroscopy. The sampling technique developed required only 20–25 μg of protein for each sample. Selenium 3 d electron signals were found in the 55.0 ± 0.3 eV region. The spectrum at the 55 eV region was free from interfering magnesium and iron. The selenium 3 d electron signals observed gave evidence that selenium in glutathione peroxidase is not bound to oxygen.
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