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

doi:10.1016/0003-9861(77)90344-7

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 journal › Journal 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 language	English
Pages (from-to)	209-214
Number of pages	6
Journal	Archives of Biochemistry and Biophysics
Volume	184
Issue number	1
DOIs	https://doi.org/10.1016/0003-9861(77)90344-7
State	Published - 11 1977
Externally published	Yes

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

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.",

author = "Danny Chiu and Tappel, {Al L.} and Millard, {M. M.}",

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AU - Chiu, Danny

AU - Tappel, Al L.

AU - Millard, M. M.

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Y1 - 1977/11

N2 - 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.

AB - 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.

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U2 - 10.1016/0003-9861(77)90344-7

DO - 10.1016/0003-9861(77)90344-7

M3 - 文章

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AN - SCOPUS:0017658102

SN - 0003-9861

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JO - Archives of Biochemistry and Biophysics

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IS - 1

ER -

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

Abstract

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