Improved procedure for X-ray photoelectron spectroscopy of selenium-glutathione peroxidase and application to the rat liver enzyme

Danny Chiu*, Al L. Tappel, M. M. Millard

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

17 Scopus citations

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 3d 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 3d electron signals observed gave evidence that selenium in glutathione peroxidase is not bound to oxygen.

Original languageEnglish
Pages (from-to)209-214
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume184
Issue number1
DOIs
StatePublished - 11 1977
Externally publishedYes

Fingerprint

Dive into the research topics of 'Improved procedure for X-ray photoelectron spectroscopy of selenium-glutathione peroxidase and application to the rat liver enzyme'. Together they form a unique fingerprint.

Cite this