Abstract
phenylhydrazine and hydrogen peroxide were prepared fresh as needed for the various experimental procedures. The hydrogen peroxide concentration was determined by titration with a standardized permanganate solution. Horseradish peroxidase was obtained from Nutritional Biochemicals Corporation. Diethylaminoethyl cellulose1 was prepared from Solka-Floe as described by Peterson and Sober (8). Titration curves of the lyophilized preparation showed the presence of 0.9 m.eq. of ionizing groups per gm. of dry material. Methods-All spectrophotometric measurements were made with a model DU Beckman spectrophotometer. Optical density readings at 270 rnp were used as a routine measure of the protein concentration in eluent fractions. The optical density readings at 270 rnp of a solution of the purified enzyme preparation were correlated with the protein nitrogen content of this same sample by a nitrogen analysis carried out by the Kjeldahl procedure (9). Catalase activity was measured by the method of Feinstein (10).
Keywords
PeroxidaseChemistryGlutathioneBiochemistryGPX6GPX3Glutathione peroxidaseEnzyme
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Publication Info
- Year
- 1959
- Type
- article
- Volume
- 234
- Issue
- 3
- Pages
- 502-506
- Citations
- 241
- Access
- Closed
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Cite This
Gordon C. Mills
(1959).
The Purification and Properties of Glutathione Peroxidase of Erythrocytes.
Journal of Biological Chemistry
, 234
(3)
, 502-506.
https://doi.org/10.1016/s0021-9258(18)70234-2
Identifiers
- DOI
- 10.1016/s0021-9258(18)70234-2